Details for: TRAM1

Gene ID: 23471

Symbol: TRAM1

Ensembl ID: ENSG00000067167

Description: translocation associated membrane protein 1

Associated with

Other Information

Genular Protein ID: 2261373217

Symbol: TRAM1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 1315422

Title: A protein of the endoplasmic reticulum involved early in polypeptide translocation.

PubMed ID: 1315422

DOI: 10.1038/357047a0

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16421571

Title: DNA sequence and analysis of human chromosome 8.

PubMed ID: 16421571

DOI: 10.1038/nature04406

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8616892

Title: The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process.

PubMed ID: 8616892

DOI: 10.1016/s0092-8674(00)81115-0

PubMed ID: 9506517

Title: TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum.

PubMed ID: 9506517

DOI: 10.1016/s0092-8674(00)81130-7

PubMed ID: 12475939

Title: Different transmembrane domains associate with distinct endoplasmic reticulum components during membrane integration of a polytopic protein.

PubMed ID: 12475939

DOI: 10.1091/mbc.e02-04-0198

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19121997

Title: TRAM1 participates in human cytomegalovirus US2- and US11-mediated dislocation of an endoplasmic reticulum membrane glycoprotein.

PubMed ID: 19121997

DOI: 10.1074/jbc.m807568200

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20430023

Title: TRAM1 is involved in disposal of ER membrane degradation substrates.

PubMed ID: 20430023

DOI: 10.1016/j.yexcr.2010.04.010

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 32013668

Title: TRAM1 protein may support ER protein import by modulating the phospholipid bilayer near the lateral gate of the Sec61-channel.

PubMed ID: 32013668

DOI: 10.1080/19336950.2020.1724759

Sequence Information:

  • Length: 374
  • Mass: 43072
  • Checksum: 9232ADA33DE20076
  • Sequence:
  • MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP 
    ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY MLDKINRRMH FSKTKHSKFN 
    ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF 
    PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY 
    FSNEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV 
    LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT ENGVNGTLTS 
    NVADSPRNKK EKSS

Genular Protein ID: 793995512

Symbol: G3XAN4_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16421571

Title: DNA sequence and analysis of human chromosome 8.

PubMed ID: 16421571

DOI: 10.1038/nature04406

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

Sequence Information:

  • Length: 288
  • Mass: 33435
  • Checksum: 3B8E80AD4EFFA9FA
  • Sequence:
  • MLVAIIIHAV IQEYMLDKIN RRMHFSKTKH SKFNESGQLS AFYLFACVWG TFILISENYI 
    SDPTILWRAY PHNLMTFQMK FFYISQLAYW LHAFPELYFQ KTKKEDIPRQ LVYIGLYLFH 
    IAGAYLLNLN HLGLVLLVLH YFVEFLFHIS RLFYFSNEKY QKGFSLWAVL FVLGRLLTLI 
    LSVLTVGFGL ARAENQKLDF STGNFNVLAV RIAVLASICV TQAFMMWKFI NFQLRRWREH 
    SAFQAPAVKK KPTVTKGRSS KKGTENGVNG TLTSNVADSP RNKKEKSS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.