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Q9H1H9 (KI13A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF13A
Alternative name(s):
Kinesin-like protein RBKIN
Gene names
Name:KIF13A
Synonyms:RBKIN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1805 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abcission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis. Ref.7 Ref.8

Subunit structure

Interacts with AP2B1 By similarity. Interacts with ZFYVE26. Interacts with AP1G1 and AP1G2. Ref.7 Ref.8

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Midbody. Endosome membrane. Golgi apparatus membrane By similarity. Note: Recruited to the midbody during cytokinesis. Ref.7 Ref.8

Tissue specificity

Widely expressed, with highest levels in heart, brain and skeletal muscle. Ref.1 Ref.2

Developmental stage

Expressed at very low level in most fetal tissues, but at higher levels in skeletal muscle and lung. Ref.2

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 FHA domain.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence CAI21670.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21671.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40947.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI40948.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Protein transport
Transport
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Golgi apparatus
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from sequence or structural similarity. Source: UniProtKB

cargo loading into vesicle

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

endosome to lysosome transport

Inferred from mutant phenotype Ref.7. Source: UniProtKB

melanosome organization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

plus-end-directed vesicle transport along microtubule

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

centrosome

Inferred from direct assay Ref.8. Source: UniProtKB

endosome membrane

Inferred from direct assay Ref.7. Source: UniProtKB

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.8. Source: UniProtKB

trans-Golgi network membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H1H9-1)

Also known as: RBKIN1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9H1H9-2)

Also known as: RBKIN2;

The sequence of this isoform differs from the canonical sequence as follows:
     1493-1527: Missing.
Isoform 3 (identifier: Q9H1H9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1071-1083: Missing.
     1493-1527: Missing.
     1792-1797: VIIPEA → GGTTSR
     1798-1805: Missing.
Isoform 4 (identifier: Q9H1H9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1071-1083: Missing.
     1493-1527: Missing.
Isoform 5 (identifier: Q9H1H9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     50-70: KPPKVFAFDYCFWSMDESNTT → LVTVAHISNSSTLGGQGKRIT
     71-1805: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18051805Kinesin-like protein KIF13A
PRO_0000125446

Regions

Domain1 – 277277Kinesin-motor
Domain469 – 51951FHA
Nucleotide binding102 – 1098ATP By similarity
Coiled coil359 – 43678 Potential
Coiled coil602 – 775174 Potential
Coiled coil1100 – 113839 Potential
Coiled coil1518 – 154730 Potential

Amino acid modifications

Modified residue12871Phosphoserine Ref.9

Natural variations

Alternative sequence50 – 7021KPPKV…ESNTT → LVTVAHISNSSTLGGQGKRI T in isoform 5.
VSP_045584
Alternative sequence71 – 18051735Missing in isoform 5.
VSP_045585
Alternative sequence1071 – 108313Missing in isoform 3 and isoform 4.
VSP_021724
Alternative sequence1493 – 152735Missing in isoform 2, isoform 3 and isoform 4.
VSP_002870
Alternative sequence1792 – 17976VIIPEA → GGTTSR in isoform 3.
VSP_021725
Alternative sequence1798 – 18058Missing in isoform 3.
VSP_021726
Natural variant14151M → V.
Corresponds to variant rs17689215 [ dbSNP | Ensembl ].
VAR_029389
Natural variant16001F → S.
Corresponds to variant rs12211658 [ dbSNP | Ensembl ].
VAR_049699

Experimental info

Sequence conflict6741S → G in AAG38890. Ref.2
Sequence conflict6741S → G in AAG38891. Ref.2
Sequence conflict9251T → A in AAG38890. Ref.2
Sequence conflict9251T → A in AAG38891. Ref.2
Sequence conflict11851L → P in AAG38890. Ref.2
Sequence conflict11851L → P in AAG38891. Ref.2
Sequence conflict15211S → N in AAG38890. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RBKIN1) [UniParc].

Last modified November 28, 2006. Version 2.
Checksum: 5E5A6C6941DC67CC

FASTA1,805202,308
        10         20         30         40         50         60 
MSDTKVKVAV RVRPMNRREL ELNTKCVVEM EGNQTVLHPP PSNTKQGERK PPKVFAFDYC 

        70         80         90        100        110        120 
FWSMDESNTT KYAGQEVVFK CLGEGILEKA FQGYNACIFA YGQTGSGKSF SMMGHAEQLG 

       130        140        150        160        170        180 
LIPRLCCALF KRISLEQNES QTFKVEVSYM EIYNEKVRDL LDPKGSRQSL KVREHKVLGP 

       190        200        210        220        230        240 
YVDGLSQLAV TSFEDIESLM SEGNKSRTVA ATNMNEESSR SHAVFNIIIT QTLYDLQSGN 

       250        260        270        280        290        300 
SGEKVSKVSL VDLAGSERVS KTGAAGERLK EGSNINKSLT TLGLVISSLA DQAAGKGKSK 

       310        320        330        340        350        360 
FVPYRDSVLT WLLKDNLGGN SQTSMIATIS PAADNYEETL STLRYADRAK RIVNHAVVNE 

       370        380        390        400        410        420 
DPNAKVIREL REEVEKLREQ LSQAEAMKAP ELKEKLEESE KLIKELTVTW EEKLRKTEEI 

       430        440        450        460        470        480 
AQERQRQLES MGISLEMSGI KVGDDKCYLV NLNADPALNE LLVYYLKDHT RVGADTSQDI 

       490        500        510        520        530        540 
QLFGIGIQPQ HCEIDIASDG DVTLTPKENA RSCVNGTLVC STTQLWHGDR ILWGNNHFFR 

       550        560        570        580        590        600 
INLPKRKRRD WLKDFEKETG PPEHDLDAAS EASSEPDYNY EFAQMEVIMK TLNSNDPVQN 

       610        620        630        640        650        660 
VVQVLEKQYL EEKRSALEEQ RLMYERELEQ LRQQLSPDRQ PQSSGPDRLA YSSQTAQQKV 

       670        680        690        700        710        720 
TQWAEERDEL FRQSLAKLRE QLVKANTLVR EANFLAEEMS KLTDYQVTLQ IPAANLSANR 

       730        740        750        760        770        780 
KRGAIVSEPA IQVRRKGKST QVWTIEKLEN KLIDMRDLYQ EWKEKVPEAK RLYGKRGDPF 

       790        800        810        820        830        840 
YEAQENHNLI GVANVFLECL FCDVKLQYAV PIISQQGEVA GRLHVEVMRV TGAVPERVVE 

       850        860        870        880        890        900 
DDSSENSSES GSLEVVDSSG EIIHRVKKLT CRVKIKEATG LPLNLSNFVF CQYTFWDQCE 

       910        920        930        940        950        960 
STVAAPVVDP EVPSPQSKDA QYTVTFSHCK DYVVNVTEEF LEFISDGALA IEVWGHRCAG 

       970        980        990       1000       1010       1020 
NGSSIWEVDS LHAKTRTLHD RWNEVTRRIE MWISILELNE LGEYAAVELH QAKDVNTGGI 

      1030       1040       1050       1060       1070       1080 
FQLRQGHSRR VQVTVKPVQH SGTLPLMVEA ILSVSIGCVT ARSTKLQRGL DSYQRDDEDG 

      1090       1100       1110       1120       1130       1140 
DDMDSYQEED LNCVRERWSD ALIKRREYLD EQIKKVSNKT EKTEDDVERE AQLVEQWVGL 

      1150       1160       1170       1180       1190       1200 
TEERNAVLVP APGSGIPGAP ADWIPPPGME THIPVLFLDL NADDLSANEQ LVGPHASGVN 

      1210       1220       1230       1240       1250       1260 
SILPKEHGSQ FFYLPIIKHS DDEVSATASW DSSVHDSVHL NRVTPQNERI YLIVKTTVQL 

      1270       1280       1290       1300       1310       1320 
SHPAAMELVL RKRIAANIYN KQSFTQSLKR RISLKNIFYS CGVTYEIVSN IPKATEEIED 

      1330       1340       1350       1360       1370       1380 
RETLALLAAR SENEGTSDGE TYIEKYTRGV LQVENILSLE RLRQAVTVKE ALSTKARHIR 

      1390       1400       1410       1420       1430       1440 
RSLSTPNVHN VSSSRPDLSG FDEDDKGWPE NQLDMSDYSS SYQDVACYGT LPRDSPRRNK 

      1450       1460       1470       1480       1490       1500 
EGCTSETPHA LTVSPFKAFS PQPPKFFKPL MPVKEEHKKR IALEARPLLS QESMPPPQAH 

      1510       1520       1530       1540       1550       1560 
NPGCIVPSGS NGSSMPVEHN SKREKKIDSE EEENELEAIN RKLISSQPYV PVEFADFSVY 

      1570       1580       1590       1600       1610       1620 
NASLENREWF SSKVDLSNSR VLEKEVSRSP TTSSITSGYF SHSASNATLS DMVVPSSDSS 

      1630       1640       1650       1660       1670       1680 
DQLAIQTKDA DSTEHSTPSL VHDFRPSSNK ELTEVEKGLV KDKIIVVPLK ENSALAKGSP 

      1690       1700       1710       1720       1730       1740 
SSQSIPEKNS KSLCRTGSCS ELDACPSKIS QPARGFCPRE VTVEHTTNIL EDHSFTEFMG 

      1750       1760       1770       1780       1790       1800 
VSEGKDFDGL TDSSAGELSS RRSLPNKTGG KTVSDGLHHP SQLHSKLEND QVIIPEAAFW 


VLCCQ 

« Hide

Isoform 2 (RBKIN2) [UniParc].

Checksum: 8117B6828ABF7193
Show »

FASTA1,770198,627
Isoform 3 [UniParc].

Checksum: F4C1C2E8435D578D
Show »

FASTA1,749196,070
Isoform 4 [UniParc].

Checksum: 92277256F8DDEF0F
Show »

FASTA1,757197,085
Isoform 5 [UniParc].

Checksum: A5457B8ACF8B75EE
Show »

FASTA707,726

References

« Hide 'large scale' references
[1]"Identification of the human KIF13A gene homologous to Drosophila kinesin-73 and candidate for schizophrenia."
Jamain S., Quach H., Fellous M., Bourgeron T.
Genomics 74:36-44(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"Genomic amplification in retinoblastoma narrowed to 0.6 megabase on chromosome 6p containing a kinesin-like gene, RBKIN."
Chen D., Pajovic S., Duckett A., Brown V.D., Squire J.A., Gallie B.L.
Cancer Res. 62:967-971(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Retina.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 2; 4 AND 5).
Tissue: Glioblastoma.
[5]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"AP-1 and KIF13A coordinate endosomal sorting and positioning during melanosome biogenesis."
Delevoye C., Hurbain I., Tenza D., Sibarita J.B., Uzan-Gafsou S., Ohno H., Geerts W.J., Verkleij A.J., Salamero J., Marks M.S., Raposo G.
J. Cell Biol. 187:247-264(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH AP1G1 AND AP1G2, SUBCELLULAR LOCATION.
[8]"PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody."
Sagona A.P., Nezis I.P., Pedersen N.M., Liestol K., Poulton J., Rusten T.E., Skotheim R.I., Raiborg C., Stenmark H.
Nat. Cell Biol. 12:362-371(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE26.
[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-1287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ291578 mRNA. Translation: CAC20442.1.
AJ291579 mRNA. Translation: CAC20443.1.
AY014403 mRNA. Translation: AAG38890.1.
AY014404 mRNA. Translation: AAG38891.1.
AL023807, AL138724 Genomic DNA. Translation: CAI21670.1. Sequence problems.
AL023807, AL138724 Genomic DNA. Translation: CAI21671.1. Sequence problems.
AL138724, AL023807 Genomic DNA. Translation: CAI40947.1. Sequence problems.
AL138724, AL023807 Genomic DNA. Translation: CAI40948.1. Sequence problems.
BC062673 mRNA. No translation available.
BC127115 mRNA. Translation: AAI27116.1.
BC127116 mRNA. Translation: AAI27117.1.
RefSeqNP_001099036.1. NM_001105566.2.
NP_001099037.1. NM_001105567.2.
NP_001099038.1. NM_001105568.2.
NP_001230352.1. NM_001243423.1.
NP_071396.4. NM_022113.5.
UniGeneHs.94499.

3D structure databases

ProteinModelPortalQ9H1H9.
SMRQ9H1H9. Positions 2-380, 391-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122019. 7 interactions.
DIPDIP-52276N.
IntActQ9H1H9. 4 interactions.
MINTMINT-1185433.
STRING9606.ENSP00000259711.

PTM databases

PhosphoSiteQ9H1H9.

Polymorphism databases

DMDM118572662.

Proteomic databases

PaxDbQ9H1H9.
PRIDEQ9H1H9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259711; ENSP00000259711; ENSG00000137177. [Q9H1H9-1]
ENST00000378814; ENSP00000368091; ENSG00000137177. [Q9H1H9-3]
ENST00000378826; ENSP00000368103; ENSG00000137177. [Q9H1H9-2]
ENST00000378843; ENSP00000368120; ENSG00000137177. [Q9H1H9-4]
ENST00000502704; ENSP00000425453; ENSG00000137177. [Q9H1H9-5]
GeneID63971.
KEGGhsa:63971.
UCSCuc003ncf.3. human. [Q9H1H9-3]
uc003ncg.4. human. [Q9H1H9-1]
uc003nch.4. human. [Q9H1H9-2]
uc003nci.4. human. [Q9H1H9-4]

Organism-specific databases

CTD63971.
GeneCardsGC06M017759.
HGNCHGNC:14566. KIF13A.
HPAHPA029253.
HPA029254.
MIM605433. gene.
neXtProtNX_Q9H1H9.
PharmGKBPA30098.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG052244.
InParanoidQ9H1H9.
KOK10392.
OrthoDBEOG72G16D.
TreeFamTF105221.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9H1H9.
BgeeQ9H1H9.
CleanExHS_KIF13A.
GenevestigatorQ9H1H9.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProIPR000253. 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.
PfamPF12473. DUF3694. 2 hits.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF13A. human.
GeneWikiKIF13A.
GenomeRNAi63971.
NextBio65762.
PROQ9H1H9.
SOURCESearch...

Entry information

Entry nameKI13A_HUMAN
AccessionPrimary (citable) accession number: Q9H1H9
Secondary accession number(s): A0JP21 expand/collapse secondary AC list , A0JP22, F2Z382, Q5THQ2, Q5THQ3, Q9H193, Q9H194, Q9H1H8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: November 28, 2006
Last modified: March 19, 2014
This is version 107 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

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 6

Human chromosome 6: entries, gene names and cross-references to MIM