Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15629

- TRAM1_HUMAN

UniProt

Q15629 - TRAM1_HUMAN

Protein

Translocating chain-associated membrane protein 1

Gene

TRAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. receptor activity Source: ProtInc

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cotranslational protein targeting to membrane Source: ProtInc
    3. gene expression Source: Reactome
    4. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    5. translation Source: Reactome
    6. viral process Source: UniProtKB-KW

    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:20568. TRAM1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134955644.

    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

    ArrayExpressiQ15629.
    BgeeiQ15629.
    CleanExiHS_TRAM1.
    GenevestigatoriQ15629.

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ15629.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 2928CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini51 – 7626LumenalSequence AnalysisAdd
    BLAST
    Topological domaini98 – 12124CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini143 – 15917LumenalSequence AnalysisAdd
    BLAST
    Topological domaini181 – 19212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini214 – 2174LumenalSequence Analysis
    Topological domaini239 – 25113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini273 – 29725LumenalSequence AnalysisAdd
    BLAST
    Topological domaini319 – 37456CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei30 – 5021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei77 – 9721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei122 – 14221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei160 – 18021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei193 – 21321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei218 – 23821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei252 – 27221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei298 – 31821HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF    50
    VTLQYNVTLP ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY 100
    MLDKINRRMH FSKTKHSKFN ESGQLSAFYL FACVWGTFIL ISENYISDPT 150
    ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF PELYFQKTKK EDIPRQLVYI 200
    GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY FSNEKYQKGF 250
    SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV 300
    LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT 350
    ENGVNGTLTS NVADSPRNKK EKSS 374
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiS30034.
    RefSeqiNP_055109.1. NM_014294.5.
    UniGeneiHs.491988.

    Genome annotation databases

    EnsembliENST00000262213; ENSP00000262213; ENSG00000067167.
    ENST00000536748; ENSP00000439359; ENSG00000067167.
    GeneIDi23471.
    KEGGihsa:23471.
    UCSCiuc003xyo.2. human.

    Polymorphism databases

    DMDMi18202507.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6207.1.
    PIRi S30034.
    RefSeqi NP_055109.1. NM_014294.5.
    UniGenei Hs.491988.

    3D structure databases

    ProteinModelPortali Q15629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117032. 13 interactions.
    DIPi DIP-45978N.
    IntActi Q15629. 4 interactions.
    MINTi MINT-4825850.
    STRINGi 9606.ENSP00000262213.

    PTM databases

    PhosphoSitei Q15629.

    Polymorphism databases

    DMDMi 18202507.

    Proteomic databases

    MaxQBi Q15629.
    PaxDbi Q15629.
    PRIDEi Q15629.

    Protocols and materials databases

    DNASUi 23471.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262213 ; ENSP00000262213 ; ENSG00000067167 .
    ENST00000536748 ; ENSP00000439359 ; ENSG00000067167 .
    GeneIDi 23471.
    KEGGi hsa:23471.
    UCSCi uc003xyo.2. human.

    Organism-specific databases

    CTDi 23471.
    GeneCardsi GC08M071535.
    HGNCi HGNC:20568. TRAM1.
    HPAi HPA023929.
    MIMi 605190. gene.
    neXtProti NX_Q15629.
    PharmGKBi PA134955644.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292300.
    HOGENOMi HOG000007494.
    HOVERGENi HBG054402.
    InParanoidi Q15629.
    KOi K14010.
    OMAi LQLAYWF.
    PhylomeDBi Q15629.
    TreeFami TF314319.

    Enzyme and pathway databases

    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.

    Miscellaneous databases

    ChiTaRSi TRAM1. human.
    GenomeRNAii 23471.
    NextBioi 45801.
    PROi Q15629.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15629.
    Bgeei Q15629.
    CleanExi HS_TRAM1.
    Genevestigatori Q15629.

    Family and domain databases

    InterProi IPR006634. TLC-dom.
    IPR013599. TRAM1.
    IPR016447. Translocation_assoc_membrane.
    [Graphical view ]
    Pfami PF08390. TRAM1. 1 hit.
    PF03798. TRAM_LAG1_CLN8. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005449. Translocation_assoc_membrane. 1 hit.
    SMARTi SM00724. TLC. 1 hit.
    [Graphical view ]
    PROSITEi PS50922. TLC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 126 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