Q15629 (TRAM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translocating chain-associated membrane protein 1

Gene names

Name:	TRAM1
Synonyms:	TRAM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Host-virus interaction Protein transport Translocation Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome translation Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endoplasmic reticulum Traceable author statement Ref.1. Source: ProtInc endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	receptor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCAP31	P51572	5	EBI-1788852,EBI-77683

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 374	373	Translocating chain-associated membrane protein 1		PRO_0000185530
Regions
	Topological domain	2 – 29	28	Cytoplasmic Potential
	Transmembrane	30 – 50	21	Helical; Potential
	Topological domain	51 – 76	26	Lumenal Potential
	Transmembrane	77 – 97	21	Helical; Potential
	Topological domain	98 – 121	24	Cytoplasmic Potential
	Transmembrane	122 – 142	21	Helical; Potential
	Topological domain	143 – 159	17	Lumenal Potential
	Transmembrane	160 – 180	21	Helical; Potential
	Topological domain	181 – 192	12	Cytoplasmic Potential
	Transmembrane	193 – 213	21	Helical; Potential
	Topological domain	214 – 217	4	Lumenal Potential
	Transmembrane	218 – 238	21	Helical; Potential
	Topological domain	239 – 251	13	Cytoplasmic Potential
	Transmembrane	252 – 272	21	Helical; Potential
	Topological domain	273 – 297	25	Lumenal Potential
	Transmembrane	298 – 318	21	Helical; Potential
	Topological domain	319 – 374	56	Cytoplasmic Potential
	Domain	117 – 326	210	TLC
Amino acid modifications
	Modified residue	365	1	Phosphoserine Ref.3 Ref.4 Ref.5 Ref.7 Ref.8
	Glycosylation	56	1	N-linked (GlcNAc...) Probable

Sequences

	Sequence		Length	Mass (Da)
	Q15629 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9232ADA33DE20076	FASTA	374	43,072
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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.
IPI	IPI00219111.
PIR	S30034.
RefSeq	NP_055109.1. NM_014294.5.
UniGene	Hs.491988.
3D structure databases
ProteinModelPortal	Q15629.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-45978N.
IntAct	Q15629. 2 interactions.
STRING	9606.ENSP00000262213.
PTM databases
PhosphoSite	Q15629.
Polymorphism databases
DMDM	18202507.
Proteomic databases
PaxDb	Q15629.
PRIDE	Q15629.
Protocols and materials databases
DNASU	23471.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262213; ENSP00000262213; ENSG00000067167.
GeneID	23471.
KEGG	hsa:23471.
UCSC	uc003xyo.2. human.
Organism-specific databases
CTD	23471.
GeneCards	GC08M071535.
HGNC	HGNC:20568. TRAM1.
HPA	HPA023929.
MIM	605190. gene.
neXtProt	NX_Q15629.
PharmGKB	PA134955644.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG292300.
HOGENOM	HOG000007494.
HOVERGEN	HBG054402.
InParanoid	Q15629.
KO	K14010.
OMA	KSTKSPP.
OrthoDB	EOG4QVCC8.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q15629.
Bgee	Q15629.
CleanEx	HS_TRAM1.
Genevestigator	Q15629.
GermOnline	ENSG00000067167. Homo sapiens.
Family and domain databases
InterPro	IPR006634. TLC-dom. IPR013599. TRAM1. IPR016447. Translocation_assoc_membrane. [Graphical view]
Pfam	PF08390. TRAM1. 1 hit. PF03798. TRAM_LAG1_CLN8. 1 hit. [Graphical view]
PIRSF	PIRSF005449. Translocation_assoc_membrane. 1 hit.
SMART	SM00724. TLC. 1 hit. [Graphical view]
PROSITE	PS50922. TLC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TRAM1. human.
GenomeRNAi	23471.
NextBio	45801.
SOURCE	Search...

Entry information

Entry name

TRAM1_HUMAN

Accession

Primary (citable) accession number: Q15629

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.