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Q9UPV9 (TRAK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Trafficking kinesin-binding protein 1
Alternative name(s):
106 kDa O-GlcNAc transferase-interacting protein
Gene names
Name:TRAK1
Synonyms:KIAA1042, OIP106
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the regulation of endosome-to-lysosome trafficking, including endocytic trafficking of EGF-EGFR complexes and GABA-A receptors. Ref.10

Subunit structure

Interacts with O-GlcNAc transferase. Interacts with RHOT1/Miro-1 and RHOT2/Miro-2. Interacts with HGS. Interacts with GABRA1 By similarity. Interacts with KIF5C. Ref.5 Ref.6 Ref.7 Ref.10

Subcellular location

Cytoplasm. Nucleus. Mitochondrion. Early endosome. Endosome. Note: Predominantly associated with early endosome. The localization to early endosomes depends on its interaction with HRS. Colocalizes with MGARP at the mitochondria. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11

Tissue specificity

High expression in spinal cord and moderate expression in all other tissues and specific brain regions examined. Expressed in all cell lines examined. Ref.9

Domain

The C-terminal region is required for the early endosomal and mitochondrial localization.

Post-translational modification

O-glycosylated. Ref.5

Miscellaneous

Over-expressed in all investigated carcinomas, especially in gastric adenocarcinoma and signet-ring carcinoma and may serve as a marker of gastric cancer.

Sequence similarities

Contains 1 HAP1 N-terminal domain.

Sequence caution

The sequence BAA82994.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RHOT1Q8IXI23EBI-1105048,EBI-1396430

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UPV9-1)

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: Q9UPV9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: MALVFQFGQP...QIEETLKYFL → MSLRDKGGEE...HDTQDLLEEV
     655-744: AHHPGKCMSQ...STSLGLVWLL → GERSQARVTV...LSVASARLCG
     745-953: Missing.
Note: 4 (AAH15922) sequence is in conflict in position: 631:E->EEE.
Isoform 3 (identifier: Q9UPV9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: MALVFQFGQP...IEETLKYFLL → MQKFIEADYYELDWYYEECSDVL
     583-630: SATLHHWQQL...EVYCLNDFEE → DHAGPRPLSV...SHPRCWFEFL
     631-953: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Trafficking kinesin-binding protein 1
PRO_0000058037

Regions

Domain47 – 354308HAP1 N-terminal
Region359 – 509151Interaction with HGS
Coiled coil104 – 356253 Potential
Coiled coil492 – 53241 Potential
Compositional bias200 – 2034Poly-Ser

Natural variations

Alternative sequence1 – 9797MALVF…KYFLL → MQKFIEADYYELDWYYEECS DVL in isoform 3.
VSP_045558
Alternative sequence1 – 9696MALVF…LKYFL → MSLRDKGGEEECFEYDCQDE ERKPTHRQHDTQDLLEEV in isoform 2.
VSP_010839
Alternative sequence583 – 63048SATLH…NDFEE → DHAGPRPLSVLLGDSLWSLI HLRKAGHLCHAYSFFFRDSH PRCWFEFL in isoform 3.
VSP_045559
Alternative sequence631 – 953323Missing in isoform 3.
VSP_045560
Alternative sequence655 – 74490AHHPG…LVWLL → GERSQARVTVSGSRSYPSRP QASPEEMQEPPAATEEEEEE EEEEGSGEGTTISPVNLAPF PEAEFWAILTSVPGTIRSGS LSVASARLCG in isoform 2.
VSP_010840
Alternative sequence745 – 953209Missing in isoform 2.
VSP_010841

Experimental info

Sequence conflict5031S → P in CAH56169. Ref.2
Sequence conflict6381S → F in CAH56169. Ref.2
Isoform 2:
Sequence conflict6311E → EE in CAH56169. Ref.2

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: E834BE07CF41D9A4

FASTA953106,040
        10         20         30         40         50         60 
MALVFQFGQP VRAQPLPGLC HGKLIRTNAC DVCNSTDLPE VEIISLLEEQ LPHYKLRADT 

        70         80         90        100        110        120 
IYGYDHDDWL HTPLISPDAN IDLTTEQIEE TLKYFLLCAE RVGQMTKTYN DIDAVTRLLE 

       130        140        150        160        170        180 
EKERDLELAA RIGQSLLKKN KTLTERNELL EEQVEHIREE VSQLRHELSM KDELLQFYTS 

       190        200        210        220        230        240 
AAEESEPESV CSTPLKRNES SSSVQNYFHL DSLQKKLKDL EEENVVLRSE ASQLKTETIT 

       250        260        270        280        290        300 
YEEKEQQLVN DCVKELRDAN VQIASISEEL AKKTEDAARQ QEEITHLLSQ IVDLQKKAKA 

       310        320        330        340        350        360 
CAVENEELVQ HLGAAKDAQR QLTAELRELE DKYAECMEML HEAQEELKNL RNKTMPNTTS 

       370        380        390        400        410        420 
RRYHSLGLFP MDSLAAEIEG TMRKELQLEE AESPDITHQK RVFETVRNIN QVVKQRSLTP 

       430        440        450        460        470        480 
SPMNIPGSNQ SSAMNSLLSS CVSTPRSSFY GSDIGNVVLD NKTNSIILET EAADLGNDER 

       490        500        510        520        530        540 
SKKPGTPGTP GSHDLETALR RLSLRRENYL SERRFFEEEQ ERKLQELAEK GELRSGSLTP 

       550        560        570        580        590        600 
TESIMSLGTH SRFSEFTGFS GMSFSSRSYL PEKLQIVKPL EGSATLHHWQ QLAQPHLGGI 

       610        620        630        640        650        660 
LDPRPGVVTK GFRTLDVDLD EVYCLNDFEE DDTGDHISLP RLATSTPVQH PETSAHHPGK 

       670        680        690        700        710        720 
CMSQTNSTFT FTTCRILHPS DELTRVTPSL NSAPTPACGS TSHLKSTPVA TPCTPRRLSL 

       730        740        750        760        770        780 
AESFTNTRES TTTMSTSLGL VWLLKERGIS AAVYDPQSWD RAGRGSLLHS YTPKMAVIPS 

       790        800        810        820        830        840 
TPPNSPMQTP TSSPPSFEFK CTSPPYDNFL ASKPASSILR EVREKNVRSS ESQTDVSVSN 

       850        860        870        880        890        900 
LNLVDKVRRF GVAKVVNSGR AHVPTLTEEQ GPLLCGPPGP APALVPRGLV PEGLPLRCPT 

       910        920        930        940        950 
VTSAIGGLQL NSGIRRNRSF PTMVGSSMQM KAPVTLTSGI LMGAKLSKQT SLR 

« Hide

Isoform 2 [UniParc].

Checksum: E14EC7B6B460E042
Show »

FASTA68677,256
Isoform 3 [UniParc].

Checksum: 9837FDB279C91758
Show »

FASTA55663,642

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-508 (ISOFORM 3).
Tissue: Kidney and Salivary gland.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [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] (ISOFORM 2).
Tissue: Kidney.
[5]"Identification and cloning of a novel family of coiled-coil domain proteins that interact with O-GlcNAc transferase."
Iyer S.P.N., Akimoto Y., Hart G.W.
J. Biol. Chem. 278:5399-5409(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH O-GLCNAC TRANSFERASE, GLYCOSYLATION.
[6]"GRIF-1 and OIP106, members of a novel gene family of coiled-coil domain proteins: association in vivo and in vitro with kinesin."
Brickley K., Smith M.J., Beck M., Stephenson F.A.
J. Biol. Chem. 280:14723-14732(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIF5C, SUBCELLULAR LOCATION.
[7]"The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking."
Fransson S., Ruusala A., Aspenstroem P.
Biochem. Biophys. Res. Commun. 344:500-510(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RHOT1 AND RHOT2.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Identification of TRAK1 (Trafficking protein, kinesin-binding 1) as MGb2-Ag: a novel cancer biomarker."
Zhang F., Ren G., Lu Y., Jin B., Wang J., Chen X., Liu Z., Li K., Nie Y., Wang X., Fan D.
Cancer Lett. 274:250-258(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MARKER FOR GASTRIC CANCER.
[10]"Hypertonia-associated protein Trak1 is a novel regulator of endosome-to-lysosome trafficking."
Webber E., Li L., Chin L.S.
J. Mol. Biol. 382:638-651(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HGS.
[11]"HUMMR, a hypoxia- and HIF-1alpha-inducible protein, alters mitochondrial distribution and transport."
Li Y., Lim S., Hoffman D., Aspenstrom P., Federoff H.J., Rempe D.A.
J. Cell Biol. 185:1065-1081(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028965 mRNA. Translation: BAA82994.2. Different initiation.
BX647199 mRNA. Translation: CAH56169.1.
AL713787 mRNA. Translation: CAH56394.1.
AC018358 Genomic DNA. No translation available.
AC093414 Genomic DNA. No translation available.
AC137935 Genomic DNA. No translation available.
BC015922 mRNA. Translation: AAH15922.1.
CCDSCCDS43072.1. [Q9UPV9-1]
CCDS58826.1. [Q9UPV9-3]
RefSeqNP_001036111.1. NM_001042646.2. [Q9UPV9-1]
NP_001252537.1. NM_001265608.1.
NP_001252539.1. NM_001265610.1. [Q9UPV9-3]
NP_055780.2. NM_014965.4. [Q9UPV9-2]
UniGeneHs.535711.

3D structure databases

ProteinModelPortalQ9UPV9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116570. 7 interactions.
IntActQ9UPV9. 8 interactions.
MINTMINT-1195439.
STRING9606.ENSP00000328998.

PTM databases

PhosphoSiteQ9UPV9.

Polymorphism databases

DMDM13124654.

Proteomic databases

MaxQBQ9UPV9.
PaxDbQ9UPV9.
PRIDEQ9UPV9.

Protocols and materials databases

DNASU22906.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327628; ENSP00000328998; ENSG00000182606. [Q9UPV9-1]
ENST00000341421; ENSP00000340702; ENSG00000182606.
ENST00000449246; ENSP00000410717; ENSG00000182606. [Q9UPV9-3]
GeneID22906.
KEGGhsa:22906.
UCSCuc003cky.4. human. [Q9UPV9-1]

Organism-specific databases

CTD22906.
GeneCardsGC03P042108.
HGNCHGNC:29947. TRAK1.
HPAHPA005853.
MIM608112. gene.
neXtProtNX_Q9UPV9.
PharmGKBPA128394593.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG246318.
HOGENOMHOG000143414.
HOVERGENHBG069248.
InParanoidQ9UPV9.
KOK15369.
OMANSCDVCN.
OrthoDBEOG7CRTSM.
PhylomeDBQ9UPV9.
TreeFamTF323495.

Gene expression databases

ArrayExpressQ9UPV9.
BgeeQ9UPV9.
CleanExHS_TRAK1.
GenevestigatorQ9UPV9.

Family and domain databases

InterProIPR006933. HAP1_N.
IPR022154. Traffickng_kinesin-bd_prot_dom.
[Graphical view]
PfamPF04849. HAP1_N. 1 hit.
PF12448. Milton. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRAK1. human.
GeneWikiTRAK1.
GenomeRNAi22906.
NextBio35534989.
PROQ9UPV9.
SOURCESearch...

Entry information

Entry nameTRAK1_HUMAN
AccessionPrimary (citable) accession number: Q9UPV9
Secondary accession number(s): E9PDS2 expand/collapse secondary AC list , J3KNT7, Q63HR0, Q659B5, Q96B69
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 111 of the entry and version 1 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 chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM