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Q15629 (TRAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Translocating chain-associated membrane protein 1
Gene names
Name:TRAM1
Synonyms:TRAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulatory or required for the translocation of secretory proteins across the ER membrane.

Subunit structure

Interacts with human cytomegalovirus/HHV-5 protein US2. Ref.6

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the TRAM family.

Contains 1 TLC (TRAM/LAG1/CLN8) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCAP31P515725EBI-1788852,EBI-77683

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 374373Translocating chain-associated membrane protein 1
PRO_0000185530

Regions

Topological domain2 – 2928Cytoplasmic Potential
Transmembrane30 – 5021Helical; Potential
Topological domain51 – 7626Lumenal Potential
Transmembrane77 – 9721Helical; Potential
Topological domain98 – 12124Cytoplasmic Potential
Transmembrane122 – 14221Helical; Potential
Topological domain143 – 15917Lumenal Potential
Transmembrane160 – 18021Helical; Potential
Topological domain181 – 19212Cytoplasmic Potential
Transmembrane193 – 21321Helical; Potential
Topological domain214 – 2174Lumenal Potential
Transmembrane218 – 23821Helical; Potential
Topological domain239 – 25113Cytoplasmic Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 29725Lumenal Potential
Transmembrane298 – 31821Helical; Potential
Topological domain319 – 37456Cytoplasmic Potential
Domain117 – 326210TLC

Amino acid modifications

Modified residue3651Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
Glycosylation561N-linked (GlcNAc...) Probable

Sequences

Sequence LengthMass (Da)Tools
Q15629 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9232ADA33DE20076

FASTA37443,072
        10         20         30         40         50         60 
MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP 

        70         80         90        100        110        120 
ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY MLDKINRRMH FSKTKHSKFN 

       130        140        150        160        170        180 
ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF 

       190        200        210        220        230        240 
PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY 

       250        260        270        280        290        300 
FSNEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV 

       310        320        330        340        350        360 
LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT ENGVNGTLTS 

       370 
NVADSPRNKK EKSS 

« Hide

References

« Hide 'large scale' references
[1]"A protein of the endoplasmic reticulum involved early in polypeptide translocation."
Goerlich D., Hartmann E., Prehn S., Rapoport T.A.
Nature 357:47-52(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Brain and Kidney.
[3]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein."
Oresic K., Ng C.L., Tortorella D.
J. Biol. Chem. 284:5905-5914(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN US2.
[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-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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
X63679 mRNA. Translation: CAA45218.1.
BC000687 mRNA. Translation: AAH00687.1.
BC037738 mRNA. Translation: AAH37738.1.
PIRS30034.
RefSeqNP_055109.1. NM_014294.5.
UniGeneHs.491988.

3D structure databases

ProteinModelPortalQ15629.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117032. 13 interactions.
DIPDIP-45978N.
IntActQ15629. 3 interactions.
MINTMINT-4825850.
STRING9606.ENSP00000262213.

PTM databases

PhosphoSiteQ15629.

Polymorphism databases

DMDM18202507.

Proteomic databases

PaxDbQ15629.
PRIDEQ15629.

Protocols and materials databases

DNASU23471.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262213; ENSP00000262213; ENSG00000067167.
GeneID23471.
KEGGhsa:23471.
UCSCuc003xyo.2. human.

Organism-specific databases

CTD23471.
GeneCardsGC08M071535.
HGNCHGNC:20568. TRAM1.
HPAHPA023929.
MIM605190. gene.
neXtProtNX_Q15629.
PharmGKBPA134955644.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292300.
HOGENOMHOG000007494.
HOVERGENHBG054402.
InParanoidQ15629.
KOK14010.
OMAWREHSAF.
PhylomeDBQ15629.
TreeFamTF314319.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ15629.
BgeeQ15629.
CleanExHS_TRAM1.
GenevestigatorQ15629.

Family and domain databases

InterProIPR006634. TLC-dom.
IPR013599. TRAM1.
IPR016447. Translocation_assoc_membrane.
[Graphical view]
PfamPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFPIRSF005449. Translocation_assoc_membrane. 1 hit.
SMARTSM00724. TLC. 1 hit.
[Graphical view]
PROSITEPS50922. TLC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRAM1. human.
GenomeRNAi23471.
NextBio45801.
PROQ15629.
SOURCESearch...

Entry information

Entry nameTRAM1_HUMAN
AccessionPrimary (citable) accession number: Q15629
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 121 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

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 8

Human chromosome 8: entries, gene names and cross-references to MIM