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UniProtKB - P33176 (KINH_HUMAN)

UniProt

P33176 - KINH_HUMAN

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Protein

Kinesin-1 heavy chain

Gene

KIF5B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Microtubule-dependent motor required for normal distribution of mitochondria and lysosomes.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi85 – 928ATP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-264876. Insulin processing.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-1 heavy chain
Alternative name(s):
Conventional kinesin heavy chain
Ubiquitous kinesin heavy chain
Short name:
UKHC
Gene namesi
Name:KIF5B
Synonyms:KNS, KNS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6324. KIF5B.

Subcellular locationi

  • Cytoplasm › cytoskeleton By similarity

    • Note: Uniformly distributed between soma and neurites in hippocampal neurons.By similarity

GO - Cellular componenti

  • ciliary rootlet Source: Ensembl
  • cytoplasm Source: HPA
  • endocytic vesicle Source: Ensembl
  • kinesin complex Source: ProtInc
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • microtubule organizing center Source: HPA
  • neuron projection Source: Ensembl
  • perinuclear region of cytoplasm Source: HGNC
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30108.

Polymorphism and mutation databases

BioMutaiKIF5B.
DMDMi417216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 963962Kinesin-1 heavy chainPRO_0000125351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei933 – 9331PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP33176.
PRIDEiP33176.

PTM databases

PhosphoSiteiP33176.

Expressioni

Gene expression databases

BgeeiP33176.
CleanExiHS_KIF5B.
ExpressionAtlasiP33176. baseline and differential.
GenevisibleiP33176. HS.

Organism-specific databases

HPAiCAB009846.
HPA037589.
HPA037590.

Interactioni

Subunit structurei

Oligomer composed of two heavy chains and two light chains. Interacts with GRIP1 and PPP1R42 (By similarity). Interacts with SYBU. Interacts with JAKMIP1. Interacts with PLEKHM2. Interacts with ECM29.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VACWR159P686193EBI-355878,EBI-7133540From a different organism.

Protein-protein interaction databases

BioGridi110000. 83 interactions.
DIPiDIP-29244N.
IntActiP33176. 24 interactions.
MINTiMINT-4999704.
STRINGi9606.ENSP00000307078.

Structurei

Secondary structure

1
963
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 158Combined sources
Helixi20 – 256Combined sources
Beta strandi32 – 343Combined sources
Turni35 – 373Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 474Combined sources
Beta strandi49 – 524Combined sources
Helixi58 – 658Combined sources
Helixi67 – 748Combined sources
Beta strandi79 – 846Combined sources
Helixi91 – 955Combined sources
Turni102 – 1043Combined sources
Helixi107 – 12216Combined sources
Beta strandi124 – 13815Combined sources
Beta strandi141 – 1466Combined sources
Beta strandi155 – 1573Combined sources
Beta strandi163 – 1653Combined sources
Beta strandi171 – 1733Combined sources
Helixi176 – 18914Combined sources
Turni190 – 1934Combined sources
Helixi197 – 2037Combined sources
Beta strandi204 – 21613Combined sources
Turni217 – 2193Combined sources
Beta strandi222 – 23110Combined sources
Helixi238 – 2414Combined sources
Beta strandi242 – 2443Combined sources
Helixi256 – 26914Combined sources
Helixi277 – 2793Combined sources
Helixi281 – 2855Combined sources
Helixi286 – 2883Combined sources
Beta strandi290 – 2934Combined sources
Beta strandi295 – 3028Combined sources
Helixi306 – 3083Combined sources
Helixi309 – 32012Combined sources
Beta strandi326 – 3294Combined sources
Helixi337 – 34812Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
3J8Xelectron microscopy5.00K1-349[»]
3J8Yelectron microscopy5.00K1-349[»]
4HNAX-ray3.19K1-349[»]
4LNUX-ray2.19K1-325[»]
ProteinModelPortaliP33176.
SMRiP33176. Positions 3-370.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33176.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 325318Kinesin motorPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni915 – 96349GlobularAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili329 – 914586Add
BLAST

Domaini

Composed of three structural domains: a large globular N-terminal domain which is responsible for the motor activity of kinesin (it hydrolyzes ATP and binds microtubule), a central alpha-helical coiled coil domain that mediates the heavy chain dimerization; and a small globular C-terminal domain which interacts with other proteins (such as the kinesin light chains), vesicles and membranous organelles.

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin subfamily.PROSITE-ProRule annotation
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG006210.
InParanoidiP33176.
KOiK10396.
OMAiINMEDLM.
OrthoDBiEOG7T4MJD.
PhylomeDBiP33176.
TreeFamiTF105225.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLAECNIK VMCRFRPLNE SEVNRGDKYI AKFQGEDTVV IASKPYAFDR 
        60         70         80         90        100
VFQSSTSQEQ VYNDCAKKIV KDVLEGYNGT IFAYGQTSSG KTHTMEGKLH 
       110        120        130        140        150
DPEGMGIIPR IVQDIFNYIY SMDENLEFHI KVSYFEIYLD KIRDLLDVSK 
       160        170        180        190        200
TNLSVHEDKN RVPYVKGCTE RFVCSPDEVM DTIDEGKSNR HVAVTNMNEH 
       210        220        230        240        250
SSRSHSIFLI NVKQENTQTE QKLSGKLYLV DLAGSEKVSK TGAEGAVLDE 
       260        270        280        290        300
AKNINKSLSA LGNVISALAE GSTYVPYRDS KMTRILQDSL GGNCRTTIVI 
       310        320        330        340        350
CCSPSSYNES ETKSTLLFGQ RAKTIKNTVC VNVELTAEQW KKKYEKEKEK 
       360        370        380        390        400
NKILRNTIQW LENELNRWRN GETVPIDEQF DKEKANLEAF TVDKDITLTN 
       410        420        430        440        450
DKPATAIGVI GNFTDAERRK CEEEIAKLYK QLDDKDEEIN QQSQLVEKLK 
       460        470        480        490        500
TQMLDQEELL ASTRRDQDNM QAELNRLQAE NDASKEEVKE VLQALEELAV 
       510        520        530        540        550
NYDQKSQEVE DKTKEYELLS DELNQKSATL ASIDAELQKL KEMTNHQKKR 
       560        570        580        590        600
AAEMMASLLK DLAEIGIAVG NNDVKQPEGT GMIDEEFTVA RLYISKMKSE 
       610        620        630        640        650
VKTMVKRCKQ LESTQTESNK KMEENEKELA ACQLRISQHE AKIKSLTEYL 
       660        670        680        690        700
QNVEQKKRQL EESVDALSEE LVQLRAQEKV HEMEKEHLNK VQTANEVKQA 
       710        720        730        740        750
VEQQIQSHRE THQKQISSLR DEVEAKAKLI TDLQDQNQKM MLEQERLRVE 
       760        770        780        790        800
HEKLKATDQE KSRKLHELTV MQDRREQARQ DLKGLEETVA KELQTLHNLR 
       810        820        830        840        850
KLFVQDLATR VKKSAEIDSD DTGGSAAQKQ KISFLENNLE QLTKVHKQLV 
       860        870        880        890        900
RDNADLRCEL PKLEKRLRAT AERVKALESA LKEAKENASR DRKRYQQEVD 
       910        920        930        940        950
RIKEAVRSKN MARRGHSAQI AKPIRPGQHP AASPTHPSAI RGGGAFVQNS 
       960 
QPVAVRGGGG KQV
Length:963
Mass (Da):109,685
Last modified:October 1, 1993 - v1
Checksum:iA1FE5760C3250C8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.
CCDSiCCDS7171.1.
PIRiA41919.
RefSeqiNP_004512.1. NM_004521.2.
UniGeneiHs.327736.

Genome annotation databases

EnsembliENST00000302418; ENSP00000307078; ENSG00000170759.
GeneIDi3799.
KEGGihsa:3799.
UCSCiuc001iwe.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65873 mRNA. Translation: CAA46703.1.
AL161932 Genomic DNA. Translation: CAH71618.1.
BC126279 mRNA. Translation: AAI26280.1.
BC126281 mRNA. Translation: AAI26282.1.
CCDSiCCDS7171.1.
PIRiA41919.
RefSeqiNP_004512.1. NM_004521.2.
UniGeneiHs.327736.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG2X-ray1.80A1-325[»]
1MKJX-ray2.70A1-349[»]
2P4Nelectron microscopy9.00K1-325[»]
3J8Xelectron microscopy5.00K1-349[»]
3J8Yelectron microscopy5.00K1-349[»]
4HNAX-ray3.19K1-349[»]
4LNUX-ray2.19K1-325[»]
ProteinModelPortaliP33176.
SMRiP33176. Positions 3-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110000. 83 interactions.
DIPiDIP-29244N.
IntActiP33176. 24 interactions.
MINTiMINT-4999704.
STRINGi9606.ENSP00000307078.

Chemistry

BindingDBiP33176.
ChEMBLiCHEMBL5864.

PTM databases

PhosphoSiteiP33176.

Polymorphism and mutation databases

BioMutaiKIF5B.
DMDMi417216.

Proteomic databases

PaxDbiP33176.
PRIDEiP33176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302418; ENSP00000307078; ENSG00000170759.
GeneIDi3799.
KEGGihsa:3799.
UCSCiuc001iwe.4. human.

Organism-specific databases

CTDi3799.
GeneCardsiGC10M032035.
HGNCiHGNC:6324. KIF5B.
HPAiCAB009846.
HPA037589.
HPA037590.
MIMi602809. gene.
neXtProtiNX_P33176.
PharmGKBiPA30108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5059.
HOVERGENiHBG006210.
InParanoidiP33176.
KOiK10396.
OMAiINMEDLM.
OrthoDBiEOG7T4MJD.
PhylomeDBiP33176.
TreeFamiTF105225.

Enzyme and pathway databases

ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-264876. Insulin processing.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-983189. Kinesins.

Miscellaneous databases

ChiTaRSiKIF5B. human.
EvolutionaryTraceiP33176.
GeneWikiiKIF5B.
GenomeRNAii3799.
NextBioi14917.
PROiP33176.
SOURCEiSearch...

Gene expression databases

BgeeiP33176.
CleanExiHS_KIF5B.
ExpressionAtlasiP33176. baseline and differential.
GenevisibleiP33176. HS.

Family and domain databases

Gene3Di3.40.850.10. 1 hit.
InterProiIPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells."
    Navone F., Niclas J., Hom-Booher N., Sparks L., Bernstein H.D., McCaffrey G., Vale R.D.
    J. Cell Biol. 117:1263-1275(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Syntabulin is a microtubule-associated protein implicated in syntaxin transport in neurons."
    Su Q., Cai Q., Gerwin C., Smith C.L., Sheng Z.-H.
    Nat. Cell Biol. 6:941-953(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYBU.
  5. "The intracellular fate of Salmonella depends on the recruitment of kinesin."
    Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.
    Science 308:1174-1178(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEKHM2.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton and regulate receptor transport."
    Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S., Couve A.
    Mol. Cell. Neurosci. 35:501-512(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH JAKMIP1.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components."
    Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M.
    J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM29.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Crystal structure of the kinesin motor domain reveals a structural similarity to myosin."
    Kull F.J., Sablin E.P., Lau R., Fletterick R.J., Vale R.D.
    Nature 380:550-555(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
  16. "Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy."
    Sindelar C.V., Budny M.J., Rice S., Naber N., Fletterick R., Cooke R.
    Nat. Struct. Biol. 9:844-848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-349 IN COMPLEX WITH ADP.
  17. "The beginning of kinesin's force-generating cycle visualized at 9-A resolution."
    Sindelar C.V., Downing K.H.
    J. Cell Biol. 177:377-385(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) OF 1-325.
+Additional computationally mapped references.

Entry informationi

Entry nameiKINH_HUMAN
AccessioniPrimary (citable) accession number: P33176
Secondary accession number(s): A0AVB2, Q5VZ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: September 16, 2015
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.