Q9NQT8 (KI13B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.8
Subunit structure	Binds to DLG1 and DLG4. Interacts (when phosphorylated at Ser-1381 and Ser-1410) with 14-3-3. Ref.1 Ref.8
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.8
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.8
Sequence similarities	Belongs to the kinesin-like protein 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.

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 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.8. Source: UniProtKB signal transduction Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	axon Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro
Molecular_function	14-3-3 protein binding Inferred from direct assay Ref.8. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW microtubule motor activity Non-traceable author statement Ref.1. 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

1 – 278

278

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.9

Modified residue

1379

1

Phosphoserine Ref.6

Modified residue

1381

1

Phosphoserine; by MARK2 Ref.8

Modified residue

1382

1

Phosphoserine Ref.6

Modified residue

1410

1

Phosphoserine; by MARK2 Ref.7 Ref.8

Modified residue

1432

1

Phosphoserine Ref.6

Modified residue

1438

1

Phosphoserine Ref.6

Modified residue

1644

1

Phosphoserine Ref.5

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.8

Mutagenesis

1410

1

S → A: Abolishes phosphorylation by MARK2; when associated with A-1389. Ref.8

Sequence conflict

55

1

C → V in BAA31614. Ref.2

Sequence conflict

191

1

A → V in BAA31614. Ref.2

Sequence conflict

226

1

L → F in BAA31614. Ref.2

Sequence conflict

237

1

A → V in BAA31614. Ref.2

Sequence conflict

278

1

E → K in BAA31614. Ref.2

Sequence conflict

356

1

N → H in BAA31614. Ref.2

Sequence conflict

797

1

L → H in BAA31614. Ref.2

Sequence conflict

858

1

P → S in BAA31614. Ref.2

Secondary structure

1

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1826

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Helix

17 – 22

6

Beta strand

28 – 31

4

Beta strand

34 – 37

4

Beta strand

54 – 57

4

Beta strand

59 – 63

5

Turn

70 – 72

3

Helix

76 – 92

17

Beta strand

97 – 103

7

Helix

109 – 113

5

Beta strand

117 – 120

4

Helix

122 – 137

16

Beta strand

142 – 154

13

Beta strand

157 – 160

4

Beta strand

189 – 191

3

Helix

194 – 206

13

Beta strand

222 – 235

14

Beta strand

241 – 253

13

Helix

272 – 292

21

Helix

305 – 307

3

Helix

309 – 313

5

Helix

315 – 318

4

Beta strand

323 – 330

8

Helix

334 – 336

3

Helix

337 – 350

14

Beta strand

449 – 452

4

Turn

457 – 460

4

Beta strand

464 – 466

3

Beta strand

469 – 476

8

Beta strand

480 – 482

3

Beta strand

493 – 497

5

Beta strand

503 – 507

5

Beta strand

513 – 515

3

Beta strand

524 – 526

3

Beta strand

531 – 534

4

Turn

535 – 537

3

Beta strand

538 – 543

6

Beta strand

1706 – 1708

3

Beta strand

1710 – 1712

3

Beta strand

1714 – 1721

8

Beta strand

1724 – 1728

5

Beta strand

1730 – 1734

5

Beta strand

1736 – 1738

3

Beta strand

1743 – 1746

4

Beta strand

1760 – 1762

3

Helix

1764 – 1766

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NQT8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C614E7F3A89E89ED	FASTA	1,826	202,666
	10 20 30 40 50 60 MGDSKVKVAV RIRPMNRRET DLHTKCVVDV DANKVILNPV NTNLSKGDAR GQPKCFAYDH 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 ATSYKDIESL MSEGNKSRTV AATNMNEESS RSHAVLKITL THTLYDAKSG 250 260 270 280 290 300 TSGEKVGKLS LVDLAGSERA TKTGAAGDRL KEGSNINESL TTLGLVISAL ADQSAGKNKN 310 320 330 340 350 360 KFVPYRDSVL TWLLKDSLGG NSKTAMVATV SPAADNYDET LSTLRYADRA KHIVNNAVVN 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 YDEQENLSLI GVANVFLESL FYDVKLQYAV PIINQKGEVA GRLHVEVMRL 850 860 870 880 890 900 SGDVGERIAG GDEVAEVPFE 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

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]	"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.
[5]	"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, MASS SPECTROMETRY. Tissue: Platelet.
[6]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[8]	"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.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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.
AL583912 mRNA. Translation: CAC29496.1.

IPI

IPI00021753.

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.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34586N.

IntAct

Q9NQT8. 5 interactions.

STRING

9606.ENSP00000350459.

PTM databases

PhosphoSite

Q9NQT8.

Polymorphism databases

DMDM

23396625.

Proteomic databases

PaxDb

Q9NQT8.

PRIDE

Q9NQT8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

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

K10392.

OrthoDB

EOG4BG8V6.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6cyclingpathway. Arf6 signaling events.

Gene expression databases

CleanEx

HS_KIF13B.

Genevestigator

Q9NQT8.

GermOnline

ENSG00000197892. Homo sapiens.

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.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]

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

SSF74924. CAP-Gly_domain. 1 hit.
SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
PS50006. FHA_DOMAIN. False negative.
PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

KIF13B. human.

EvolutionaryTrace

Q9NQT8.

GenomeRNAi

23303.

NextBio

45145.

SOURCE

Search...

Entry information

Entry name

KI13B_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 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.