Kinesin-like protein KIF13B - KIF13B

Preferred order of sections

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIF13B

Alternative name(s):
Kinesin-like protein GAKIN

Gene names

Name:	KIF13B
Synonyms:	GAKIN, KIAA0639

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1826 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes. Ref.9
Subunit structure	Binds to DLG1 and DLG4. Interacts (when phosphorylated at Ser-1381 and Ser-1410) with 14-3-3. Ref.1 Ref.9
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › axon. Note: accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites. Ref.9
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting interaction with 14-3-3 and inhibiting microtubule-dependent accumulation and formation of axons. Ref.9
Sequence similarities	Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Contains 1 CAP-Gly domain. Contains 1 FHA domain. Contains 1 kinesin motor domain.
Sequence caution	The sequence BAA31614.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cell projection Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Non-traceable author statement PubMed 12496241. Source: UniProtKB metabolic process Non-traceable author statement Ref.1. Source: GOC microtubule-based movement Traceable author statement Ref.1. Source: UniProtKB protein targeting Traceable author statement Ref.1. Source: UniProtKB regulation of axonogenesis Inferred from direct assay Ref.9. Source: UniProtKB signal transduction Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	axon Inferred from direct assay Ref.9. Source: UniProtKB cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB kinesin complex Inferred from electronic annotation. Source: InterPro microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	14-3-3 protein binding Inferred from direct assay Ref.9. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Non-traceable author statement Ref.1. Source: UniProtKB protein binding Inferred from physical interaction Ref.1. Source: UniProtKB protein kinase binding Inferred from physical interaction Ref.1 Ref.9. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DLG1	Q12959-2	3	EBI-766408,EBI-357500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1826

1826

Kinesin-like protein KIF13B

PRO_0000125448

Regions

Domain

5 – 353

349

Kinesin motor

Domain

471 – 535

65

FHA

Domain

1721 – 1763

43

CAP-Gly

Nucleotide binding

103 – 110

8

ATP By similarity

Coiled coil

364 – 439

76

Potential

Coiled coil

607 – 710

104

Potential

Coiled coil

752 – 772

21

Potential

Coiled coil

1096 – 1143

48

Potential

Amino acid modifications

Modified residue

661

1

Phosphoserine Ref.10

Modified residue

1379

1

Phosphoserine Ref.7

Modified residue

1381

1

Phosphoserine; by MARK2 Ref.9

Modified residue

1382

1

Phosphoserine Ref.7

Modified residue

1410

1

Phosphoserine; by MARK2 Ref.8 Ref.9

Modified residue

1432

1

Phosphoserine Ref.7

Modified residue

1438

1

Phosphoserine Ref.7

Modified residue

1644

1

Phosphoserine Ref.6

Natural variations

Natural variant

1471

1

V → I.
Corresponds to variant rs17526980 [ dbSNP | Ensembl ].

VAR_055982

Experimental info

Mutagenesis

1381

1

S → A: Abolishes phosphorylation by MARK2; when associated with A-1410. Ref.9

Mutagenesis

1410

1

S → A: Abolishes phosphorylation by MARK2; when associated with A-1389. Ref.9

Sequence conflict

55

1

V → C in AAF81263. Ref.1

Sequence conflict

191

1

V → A in AAF81263. Ref.1

Sequence conflict

226

1

F → L in AAF81263. Ref.1

Sequence conflict

237

1

V → A in AAF81263. Ref.1

Sequence conflict

278

1

K → E in AAF81263. Ref.1

Sequence conflict

356

1

H → N in AAF81263. Ref.1

Sequence conflict

797

1

H → L in AAF81263. Ref.1

Sequence conflict

858

1

S → P in AAF81263. Ref.1

Secondary structure

1

.

1826

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9NQT8 [UniParc].

Last modified June 26, 2013. Version 2.
Checksum: 7A336B3C5BDA21E6
Show »

FASTA

1,826

202,789

        10         20         30         40         50         60 
MGDSKVKVAV RIRPMNRRET DLHTKCVVDV DANKVILNPV NTNLSKGDAR GQPKVFAYDH 

        70         80         90        100        110        120 
CFWSMDESVK EKYAGQDIVF KCLGENILQN AFDGYNACIF AYGQTGSGKS YTMMGTADQP 

       130        140        150        160        170        180 
GLIPRLCSGL FERTQKEENE EQSFKVEVSY MEIYNEKVRD LLDPKGSRQT LKVREHSVLG 

       190        200        210        220        230        240 
PYVDGLSKLA VTSYKDIESL MSEGNKSRTV AATNMNEESS RSHAVFKITL THTLYDVKSG 

       250        260        270        280        290        300 
TSGEKVGKLS LVDLAGSERA TKTGAAGDRL KEGSNINKSL TTLGLVISAL ADQSAGKNKN 

       310        320        330        340        350        360 
KFVPYRDSVL TWLLKDSLGG NSKTAMVATV SPAADNYDET LSTLRYADRA KHIVNHAVVN 

       370        380        390        400        410        420 
EDPNARIIRD LREEVEKLRE QLTKAEAMKS PELKDRLEES EKLIQEMTVT WEEKLRKTEE 

       430        440        450        460        470        480 
IAQERQKQLE SLGISLQSSG IKVGDDKCFL VNLNADPALN ELLVYYLKEH TLIGSANSQD 

       490        500        510        520        530        540 
IQLCGMGILP EHCIIDITSE GQVMLTPQKN TRTFVNGSSV SSPIQLHHGD RILWGNNHFF 

       550        560        570        580        590        600 
RLNLPKKKKK AEREDEDQDP SMKNENSSEQ LDVDGDSSSE VSSEVNFNYE YAQMEVTMKA 

       610        620        630        640        650        660 
LGSNDPMQSI LNSLEQQHEE EKRSALERQR LMYEHELEQL RRRLSPEKQN CRSMDRFSFH 

       670        680        690        700        710        720 
SPSAQQRLRQ WAEEREATLN NSLMRLREQI VKANLLVREA NYIAEELDKR TEYKVTLQIP 

       730        740        750        760        770        780 
ASSLDANRKR GSLLSEPAIQ VRRKGKGKQI WSLEKLDNRL LDMRDLYQEW KECEEDNPVI 

       790        800        810        820        830        840 
RSYFKRADPF YDEQENHSLI GVANVFLESL FYDVKLQYAV PIINQKGEVA GRLHVEVMRL 

       850        860        870        880        890        900 
SGDVGERIAG GDEVAEVSFE KETQENKLVC MVKILQATGL PQHLSHFVFC KYSFWDQQEP 

       910        920        930        940        950        960 
VIVAPEVDTS SSSVSKEPHC MVVFDHCNEF SVNITEDFIE HLSEGALAIE VYGHKINDPR 

       970        980        990       1000       1010       1020 
KNPALWDLGI IQAKTRSLRD RWSEVTRKLE FWVQILEQNE NGEYCPVEVI SAKDVPTGGI 

      1030       1040       1050       1060       1070       1080 
FQLRQGQSRR VQVEVKSVQE SGTLPLMEEC ILSVGIGCVK VRPLRAPRTH ETFHEEEEDM 

      1090       1100       1110       1120       1130       1140 
DSYQDRDLER LRRKWLNALT KRQEYLDQQL QKLVSKRDKT EDDADREAQL LEMRLTLTEE 

      1150       1160       1170       1180       1190       1200 
RNAVMVPSAG SGIPGAPAEW TPVPGMETHI PVIFLDLNAD DFSSQDNLDD PEAGGWDATL 

      1210       1220       1230       1240       1250       1260 
TGEEEEEFFE LQIVKQHDGE VKAEASWDSA VHGCPQLSRG TPVDERLFLI VRVTVQLSHP 

      1270       1280       1290       1300       1310       1320 
ADMQLVLRKR ICVNVHGRQG FAQSLLKKMS HRSSIPGCGV TFEIVSNIPE DAQGVEEREA 

      1330       1340       1350       1360       1370       1380 
LARMAANVEN PASADSEAYI EKYLRSVLAV ENLLTLDRLR QEVAVKEQLT GKGKLSRRSI 

      1390       1400       1410       1420       1430       1440 
SSPNVNRLSG SRQDLIPSYS LGSNKGRWES QQDVSQTTVS RGIAPAPALS VSPQNNHSPD 

      1450       1460       1470       1480       1490       1500 
PGLSNLAASY LNPVKSFVPQ MPKLLKSLFP VRDEKRGKRP SPLAHQPVPR IMVQSASPDI 

      1510       1520       1530       1540       1550       1560 
RVTRMEEAQP EMGPDVLVQT MGAPALKICD KPAKVPSPPP VIAVTAVTPA PEAQDGPPSP 

      1570       1580       1590       1600       1610       1620 
LSEASSGYFS HSVSTATLSD ALGPGLDAAA PPGSMPTAPE AEPEAPISHP PPPTAVPAEE 

      1630       1640       1650       1660       1670       1680 
PPGPQQLVSP GRERPDLEAP APGSPFRVRR VRASELRSFS RMLAGDPGCS PGAEGNAPAP 

      1690       1700       1710       1720       1730       1740 
GAGGQALASD SEEADEVPEW LREGEFVTVG AHKTGVVRYV GPADFQEGTW VGVELDLPSG 

      1750       1760       1770       1780       1790       1800 
KNDGSIGGKQ YFRCNPGYGL LVRPSRVRRA TGPVRRRSTG LRLGAPEARR SATLSGSATN 

      1810       1820 
LASLTAALAK ADRSHKNPEN RKSWAS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes." Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H. J. Biol. Chem. 275:28774-28784(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH DLG1 AND DLG4.
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	Ohara O., Suyama M., Nagase T., Ishikawa K. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1096-1826. Tissue: Amygdala.
[6]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1379; SER-1382; SER-1432 AND SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[9]	"Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B to regulate axon formation." Yoshimura Y., Terabayashi T., Miki H. Mol. Cell. Biol. 30:2206-2219(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF SER-1381 AND SER-1410, PHOSPHORYLATION AT SER-1381 AND SER-1410.
[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-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"Solution structure of the CAP-Gly domain in human kinesin-like protein KIF13B." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1684-1771.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF279865 mRNA. Translation: AAF81263.1.
AB014539 mRNA. Translation: BAA31614.3. Different initiation.
AC084262 Genomic DNA. No translation available.
AC103830 Genomic DNA. No translation available.
AC108449 Genomic DNA. No translation available.
AL583912 mRNA. Translation: CAC29496.1.

CCDS

CCDS55217.1.

RefSeq

NP_056069.2. NM_015254.3.

UniGene

Hs.444767.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2COW	NMR	-	A	1685-1771	[»]
3FM8	X-ray	2.30	A/B	440-545	[»]
3GBJ	X-ray	2.10	A/B/C	4-352	[»]
3MDB	X-ray	2.95	A/B	440-545	[»]

ProteinModelPortal

Q9NQT8.

SMR

Q9NQT8. Positions 5-351, 448-545, 1679-1773.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

116895. 8 interactions.

DIP

DIP-34586N.

IntAct

Q9NQT8. 5 interactions.

STRING

9606.ENSP00000350459.

PTM databases

PhosphoSite

Q9NQT8.

Polymorphism databases

DMDM

519668668.

Proteomic databases

MaxQB

Q9NQT8.

PaxDb

Q9NQT8.

PRIDE

Q9NQT8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000524189; ENSP00000427900; ENSG00000197892.

GeneID

23303.

KEGG

hsa:23303.

Organism-specific databases

CTD

23303.

GeneCards

GC08M028924.

H-InvDB

HIX0021580.

HGNC

HGNC:14405. KIF13B.

HPA

HPA025023.

MIM

607350. gene.

neXtProt

NX_Q9NQT8.

PharmGKB

PA30099.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5244.

HOGENOM

HOG000230729.

HOVERGEN

HBG052244.

KO

K17914.

OMA

MKALGSN.

OrthoDB

EOG72G16D.

PhylomeDB

Q9NQT8.

TreeFam

TF105221.

Gene expression databases

CleanEx

HS_KIF13B.

Genevestigator

Q9NQT8.

Family and domain databases

Gene3D

2.30.30.190. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.

InterPro

IPR000938. CAP-Gly_domain.
IPR000253. FHA_dom.
IPR022140. KIF1B.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]

PANTHER

PTHR24115. PTHR24115. 1 hit.

Pfam

PF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 2 hits.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM01052. CAP_GLY. 1 hit.
SM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]

SUPFAM

SSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF74924. SSF74924. 1 hit.

PROSITE

PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KIF13B. human.

EvolutionaryTrace

Q9NQT8.

GenomeRNAi

23303.

NextBio

45145.

PRO

Q9NQT8.

SOURCE

Search...

Entry information

Entry name

KI13B_HUMAN

Accession

Primary (citable) accession number: Q9NQT8
Secondary accession number(s): F8VPJ2, O75134, Q9BYJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	June 26, 2013
Last modified:	July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents