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Q9NQT8 (KI13B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF13B
Alternative name(s):
Kinesin-like protein GAKIN
Gene names
Name:KIF13B
Synonyms:GAKIN, KIAA0639
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1826 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytoskeleton. Cell projectionaxon. 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 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. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DLG1Q12959-23EBI-766408,EBI-357500

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18261826Kinesin-like protein KIF13B
PRO_0000125448

Regions

Domain1 – 278278Kinesin-motor
Domain471 – 53565FHA
Domain1721 – 176343CAP-Gly
Nucleotide binding103 – 1108ATP By similarity
Coiled coil364 – 43976 Potential
Coiled coil607 – 710104 Potential
Coiled coil752 – 77221 Potential
Coiled coil1096 – 114348 Potential

Amino acid modifications

Modified residue6611Phosphoserine Ref.10
Modified residue13791Phosphoserine Ref.7
Modified residue13811Phosphoserine; by MARK2 Ref.9
Modified residue13821Phosphoserine Ref.7
Modified residue14101Phosphoserine; by MARK2 Ref.8 Ref.9
Modified residue14321Phosphoserine Ref.7
Modified residue14381Phosphoserine Ref.7
Modified residue16441Phosphoserine Ref.6

Natural variations

Natural variant14711V → I.
Corresponds to variant rs17526980 [ dbSNP | Ensembl ].
VAR_055982

Experimental info

Mutagenesis13811S → A: Abolishes phosphorylation by MARK2; when associated with A-1410. Ref.9
Mutagenesis14101S → A: Abolishes phosphorylation by MARK2; when associated with A-1389. Ref.9
Sequence conflict551V → C in AAF81263. Ref.1
Sequence conflict1911V → A in AAF81263. Ref.1
Sequence conflict2261F → L in AAF81263. Ref.1
Sequence conflict2371V → A in AAF81263. Ref.1
Sequence conflict2781K → E in AAF81263. Ref.1
Sequence conflict3561H → N in AAF81263. Ref.1
Sequence conflict7971H → L in AAF81263. Ref.1
Sequence conflict8581S → P in AAF81263. Ref.1

Secondary structure

.......................................................................................... 1826
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NQT8 [UniParc].

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

FASTA1,826202,789
        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' 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. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., 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.
RefSeqNP_056069.2. NM_015254.3.
UniGeneHs.444767.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COWNMR-A1685-1771[»]
3FM8X-ray2.30A/B440-545[»]
3GBJX-ray2.10A/B/C4-352[»]
3MDBX-ray2.95A/B440-545[»]
ProteinModelPortalQ9NQT8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116895. 8 interactions.
DIPDIP-34586N.
IntActQ9NQT8. 5 interactions.
STRING9606.ENSP00000350459.

PTM databases

PhosphoSiteQ9NQT8.

Polymorphism databases

DMDM519668668.

Proteomic databases

PaxDbQ9NQT8.
PRIDEQ9NQT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000524189; ENSP00000427900; ENSG00000197892.
GeneID23303.
KEGGhsa:23303.

Organism-specific databases

CTD23303.
GeneCardsGC08M028924.
H-InvDBHIX0021580.
HGNCHGNC:14405. KIF13B.
HPAHPA025023.
MIM607350. gene.
neXtProtNX_Q9NQT8.
PharmGKBPA30099.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5244.
HOGENOMHOG000230729.
HOVERGENHBG052244.
KOK17914.
OMAGSNKGRW.
OrthoDBEOG72G16D.
TreeFamTF105221.

Gene expression databases

CleanExHS_KIF13B.
GenevestigatorQ9NQT8.

Family and domain databases

Gene3D2.30.30.190. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProIPR000938. 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]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 2 hits.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM01052. CAP_GLY. 1 hit.
SM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF13B. human.
EvolutionaryTraceQ9NQT8.
GenomeRNAi23303.
NextBio45145.
PROQ9NQT8.
SOURCESearch...

Entry information

Entry nameKI13B_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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