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O43896 (KIF1C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF1C
Gene names
Name:KIF1C
Synonyms:KIAA0706
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1103 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility. Ref.1

Subunit structure

Monomer Potential.

Subcellular location

Cytoplasmcytoskeleton Probable.

Tissue specificity

Expressed in all tissues examined, with most abundant expression in heart and skeletal muscle. Ref.1

Post-translational modification

Phosphorylated on tyrosine residues. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Sequence similarities

Belongs to the kinesin-like protein family. Unc-104 subfamily.

Contains 1 FHA domain.

Contains 1 kinesin-motor domain.

Sequence caution

The sequence BAA31681.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11031103Kinesin-like protein KIF1C
PRO_0000125410

Regions

Domain1 – 273273Kinesin-motor
Domain523 – 59068FHA
Nucleotide binding97 – 1048ATP By similarity
Coiled coil359 – 38830 Potential
Coiled coil438 – 47942 Potential
Coiled coil633 – 67442 Potential
Coiled coil828 – 87245 Potential
Compositional bias965 – 1085121Pro-rich

Amino acid modifications

Modified residue4941Phosphoserine Ref.5 Ref.10
Modified residue6741Phosphoserine By similarity
Modified residue6761Phosphoserine By similarity
Modified residue10331Phosphoserine Ref.6
Modified residue10821Phosphothreonine Ref.9
Modified residue10831Phosphothreonine Ref.7 Ref.8
Modified residue10921Phosphoserine Ref.6 Ref.8 Ref.10

Experimental info

Sequence conflict6691R → Q in AAC52117. Ref.1
Sequence conflict955 – 9628SGGRGGGL → LWGPGRGV in AAC52117. Ref.1
Sequence conflict976 – 9772KL → NV in AAC52117. Ref.1

Secondary structure

..................... 1103
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43896 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 5FDEEB8C91B3C46B

FASTA1,103122,947
        10         20         30         40         50         60 
MAGASVKVAV RVRPFNARET SQDAKCVVSM QGNTTSIINP KQSKDAPKSF TFDYSYWSHT 

        70         80         90        100        110        120 
STEDPQFASQ QQVYRDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGR QEPGQQGIVP 

       130        140        150        160        170        180 
QLCEDLFSRV SENQSAQLSY SVEVSYMEIY CERVRDLLNP KSRGSLRVRE HPILGPYVQD 

       190        200        210        220        230        240 
LSKLAVTSYA DIADLMDCGN KARTVAATNM NETSSRSHAV FTIVFTQRCH DQLTGLDSEK 

       250        260        270        280        290        300 
VSKISLVDLA GSERADSSGA RGMRLKEGAN INKSLTTLGK VISALADMQS KKRKSDFIPY 

       310        320        330        340        350        360 
RDSVLTWLLK ENLGGNSRTA MIAALSPADI NYEETLSTLR YADRTKQIRC NAIINEDPNA 

       370        380        390        400        410        420 
RLIRELQEEV ARLRELLMAQ GLSASALEGL KTEEGSVRGA LPAVSSPPAP VSPSSPTTHN 

       430        440        450        460        470        480 
GELEPSFSPN TESQIGPEEA MERLQETEKI IAELNETWEE KLRKTEALRM EREALLAEMG 

       490        500        510        520        530        540 
VAVREDGGTV GVFSPKKTPH LVNLNEDPLM SECLLYHIKD GVTRVGQVDM DIKLTGQFIR 

       550        560        570        580        590        600 
EQHCLFRSIP QPDGEVVVTL EPCEGAETYV NGKLVTEPLV LKSGNRIVMG KNHVFRFNHP 

       610        620        630        640        650        660 
EQARLERERG VPPPPGPPSE PVDWNFAQKE LLEQQGIDIK LEMEKRLQDL ENQYRKEKEE 

       670        680        690        700        710        720 
ADLLLEQQRL YADSDSGDDS DKRSCEESWR LISSLREQLP PTTVQTIVKR CGLPSSGKRR 

       730        740        750        760        770        780 
APRRVYQIPQ RRRLQGKDPR WATMADLKMQ AVKEICYEVA LADFRHGRAE IEALAALKMR 

       790        800        810        820        830        840 
ELCRTYGKPD GPGDAWRAVA RDVWDTVGEE EGGGAGSGGG SEEGARGAEV EDLRAHIDKL 

       850        860        870        880        890        900 
TGILQEVKLQ NSSKDRELQA LRDRMLRMER VIPLAQDHED ENEEGGEVPW APPEGSEAAE 

       910        920        930        940        950        960 
EAAPSDRMPS ARPPSPPLSS WERVSRLMEE DPAFRRGRLR WLKQEQLRLQ GLQGSGGRGG 

       970        980        990       1000       1010       1020 
GLRRPPARFV PPHDCKLRFP FKSNPQHRES WPGMGSGEAP TPLQPPEEVT PHPATPARRP 

      1030       1040       1050       1060       1070       1080 
PSPRRSHHPR RNSLDGGGRS RGAGSAQPEP QHFQPKKHNS YPQPPQPYPA QRPPGPRYPP 

      1090       1100 
YTTPPRMRRQ RSAPDLKESG AAV 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum."
Dorner C., Ciossek T., Mueller S., Moeller N.P.H., Ullrich A., Lammers R.
J. Biol. Chem. 273:20267-20275(1998) [PubMed: 9685376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, TISSUE SPECIFICITY.
Tissue: Hippocampus.
[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: 9734811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1033 AND SER-1092, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1083, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[8]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1083 AND SER-1092, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1082, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[10]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-1092, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Crystal structure of the FHA domain of human kinesin family member C."
Structural genomics consortium (SGC)
Submitted (FEB-2006) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 498-599.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U91329 mRNA. Translation: AAC52117.1.
AB014606 mRNA. Translation: BAA31681.2. Different initiation.
CH471108 Genomic DNA. Translation: EAW90366.1.
CH471108 Genomic DNA. Translation: EAW90367.1.
CH471108 Genomic DNA. Translation: EAW90368.1.
CH471108 Genomic DNA. Translation: EAW90369.1.
BC034993 mRNA. Translation: AAH34993.1.
IPIIPI00179757.
RefSeqNP_006603.2. NM_006612.5.
UniGeneHs.435120.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2G1LX-ray2.60A498-599[»]
ProteinModelPortalO43896.
SMRO43896. Positions 4-347, 498-599.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-40376N.
IntActO43896. 8 interactions.
STRINGO43896.

PTM databases

PhosphoSiteO43896.

Proteomic databases

PRIDEO43896.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320785; ENSP00000320821; ENSG00000129250.
GeneID10749.
KEGGhsa:10749.
UCSCuc002gan.1. human.

Organism-specific databases

CTD10749.
GeneCardsGC17P004901.
H-InvDBHIX0013460.
HGNCHGNC:6317. KIF1C.
HPAHPA021831.
HPA024602.
MIM603060. gene.
neXtProtNX_O43896.
PharmGKBPA30100.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG14745.
GeneTreeENSGT00570000078823.
HOGENOMHBG746568.
HOVERGENHBG057158.
InParanoidO43896.
OMAQSAQLSY.
OrthoDBEOG4W3SM7.
PhylomeDBO43896.

Gene expression databases

ArrayExpressO43896.
BgeeO43896.
CleanExHS_KIF1C.
GenevestigatorO43896.
GermOnlineENSG00000129250. Homo sapiens.

Family and domain databases

InterProIPR000253. FHA_dom.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
Gene3DG3DSA:2.60.200.20. FHA. 1 hit.
G3DSA:3.40.850.10. kinesin_motor. 1 hit.
KOK10392.
PfamPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF49879. SMAD_FHA. 1 hit.
PROSITEPS50006. FHA_DOMAIN. False negative.
PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio40821.
SOURCESearch...

Entry information

Entry nameKIF1C_HUMAN
AccessionPrimary (citable) accession number: O43896
Secondary accession number(s): D3DTL6, O75186, Q5U618
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 111 of the entry and version 3 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

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families