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Protein

Translocating chain-associated membrane protein 1

Gene

TRAM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • receptor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Translocating chain-associated membrane protein 1
Gene namesi
Name:TRAM1
Synonyms:TRAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:20568. TRAM1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2928CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei30 – 5021HelicalSequence AnalysisAdd
BLAST
Topological domaini51 – 7626LumenalSequence AnalysisAdd
BLAST
Transmembranei77 – 9721HelicalSequence AnalysisAdd
BLAST
Topological domaini98 – 12124CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Topological domaini143 – 15917LumenalSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Topological domaini181 – 19212CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei193 – 21321HelicalSequence AnalysisAdd
BLAST
Topological domaini214 – 2174LumenalSequence Analysis
Transmembranei218 – 23821HelicalSequence AnalysisAdd
BLAST
Topological domaini239 – 25113CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 29725LumenalSequence AnalysisAdd
BLAST
Transmembranei298 – 31821HelicalSequence AnalysisAdd
BLAST
Topological domaini319 – 37456CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134955644.

Polymorphism and mutation databases

BioMutaiTRAM1.
DMDMi18202507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 374373Translocating chain-associated membrane protein 1PRO_0000185530Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi56 – 561N-linked (GlcNAc...)Curated
Modified residuei365 – 3651Phosphoserine5 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ15629.
PaxDbiQ15629.
PRIDEiQ15629.

PTM databases

PhosphoSiteiQ15629.

Expressioni

Gene expression databases

BgeeiQ15629.
CleanExiHS_TRAM1.
ExpressionAtlasiQ15629. baseline and differential.
GenevisibleiQ15629. HS.

Organism-specific databases

HPAiHPA023929.

Interactioni

Subunit structurei

Interacts with human cytomegalovirus/HHV-5 protein US2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAP31P515725EBI-1788852,EBI-77683

Protein-protein interaction databases

BioGridi117032. 11 interactions.
DIPiDIP-45978N.
IntActiQ15629. 4 interactions.
MINTiMINT-4825850.
STRINGi9606.ENSP00000262213.

Structurei

3D structure databases

ProteinModelPortaliQ15629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 326210TLCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAM family.Curated
Contains 1 TLC (TRAM/LAG1/CLN8) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292300.
GeneTreeiENSGT00510000046470.
HOGENOMiHOG000007494.
HOVERGENiHBG054402.
InParanoidiQ15629.
KOiK14010.
OMAiLQLAYWF.
PhylomeDBiQ15629.
TreeFamiTF314319.

Family and domain databases

InterProiIPR006634. TLC-dom.
IPR013599. TRAM1.
IPR016447. Translocation_assoc_membrane.
[Graphical view]
PfamiPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFiPIRSF005449. Translocation_assoc_membrane. 1 hit.
SMARTiSM00724. TLC. 1 hit.
[Graphical view]
PROSITEiPS50922. TLC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15629-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF
60 70 80 90 100
VTLQYNVTLP ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY
110 120 130 140 150
MLDKINRRMH FSKTKHSKFN ESGQLSAFYL FACVWGTFIL ISENYISDPT
160 170 180 190 200
ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF PELYFQKTKK EDIPRQLVYI
210 220 230 240 250
GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY FSNEKYQKGF
260 270 280 290 300
SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
310 320 330 340 350
LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT
360 370
ENGVNGTLTS NVADSPRNKK EKSS
Length:374
Mass (Da):43,072
Last modified:January 23, 2007 - v3
Checksum:i9232ADA33DE20076
GO
Isoform 2 (identifier: Q15629-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Note: No experimental confirmation available.
Show »
Length:343
Mass (Da):39,683
Checksum:i14266BD8762EF466
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3131Missing in isoform 2. 1 PublicationVSP_056213Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63679 mRNA. Translation: CAA45218.1.
AK303411 mRNA. Translation: BAG64464.1.
AC022731 Genomic DNA. No translation available.
AC120194 Genomic DNA. No translation available.
BC000687 mRNA. Translation: AAH00687.1.
BC037738 mRNA. Translation: AAH37738.1.
CCDSiCCDS6207.1. [Q15629-1]
PIRiS30034.
RefSeqiNP_055109.1. NM_014294.5. [Q15629-1]
UniGeneiHs.491988.

Genome annotation databases

EnsembliENST00000262213; ENSP00000262213; ENSG00000067167.
GeneIDi23471.
KEGGihsa:23471.
UCSCiuc003xyo.2. human. [Q15629-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63679 mRNA. Translation: CAA45218.1.
AK303411 mRNA. Translation: BAG64464.1.
AC022731 Genomic DNA. No translation available.
AC120194 Genomic DNA. No translation available.
BC000687 mRNA. Translation: AAH00687.1.
BC037738 mRNA. Translation: AAH37738.1.
CCDSiCCDS6207.1. [Q15629-1]
PIRiS30034.
RefSeqiNP_055109.1. NM_014294.5. [Q15629-1]
UniGeneiHs.491988.

3D structure databases

ProteinModelPortaliQ15629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117032. 11 interactions.
DIPiDIP-45978N.
IntActiQ15629. 4 interactions.
MINTiMINT-4825850.
STRINGi9606.ENSP00000262213.

PTM databases

PhosphoSiteiQ15629.

Polymorphism and mutation databases

BioMutaiTRAM1.
DMDMi18202507.

Proteomic databases

MaxQBiQ15629.
PaxDbiQ15629.
PRIDEiQ15629.

Protocols and materials databases

DNASUi23471.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262213; ENSP00000262213; ENSG00000067167.
GeneIDi23471.
KEGGihsa:23471.
UCSCiuc003xyo.2. human. [Q15629-1]

Organism-specific databases

CTDi23471.
GeneCardsiGC08M071535.
HGNCiHGNC:20568. TRAM1.
HPAiHPA023929.
MIMi605190. gene.
neXtProtiNX_Q15629.
PharmGKBiPA134955644.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292300.
GeneTreeiENSGT00510000046470.
HOGENOMiHOG000007494.
HOVERGENiHBG054402.
InParanoidiQ15629.
KOiK14010.
OMAiLQLAYWF.
PhylomeDBiQ15629.
TreeFamiTF314319.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

Miscellaneous databases

ChiTaRSiTRAM1. human.
GenomeRNAii23471.
NextBioi35476779.
PROiQ15629.
SOURCEiSearch...

Gene expression databases

BgeeiQ15629.
CleanExiHS_TRAM1.
ExpressionAtlasiQ15629. baseline and differential.
GenevisibleiQ15629. HS.

Family and domain databases

InterProiIPR006634. TLC-dom.
IPR013599. TRAM1.
IPR016447. Translocation_assoc_membrane.
[Graphical view]
PfamiPF08390. TRAM1. 1 hit.
PF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
PIRSFiPIRSF005449. Translocation_assoc_membrane. 1 hit.
SMARTiSM00724. TLC. 1 hit.
[Graphical view]
PROSITEiPS50922. TLC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(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 1).
    Tissue: Brain and Kidney.
  5. "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.
  6. "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.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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.
  9. "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.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTRAM1_HUMAN
AccessioniPrimary (citable) accession number: Q15629
Secondary accession number(s): B4E0K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.