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Q9UNL2

- SSRG_HUMAN

UniProt

Q9UNL2 - SSRG_HUMAN

Protein

Translocon-associated protein subunit gamma

Gene

SSR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    4. translation Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translocon-associated protein subunit gamma
    Short name:
    TRAP-gamma
    Alternative name(s):
    Signal sequence receptor subunit gamma
    Short name:
    SSR-gamma
    Gene namesi
    Name:SSR3
    Synonyms:TRAPG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11325. SSR3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of endoplasmic reticulum membrane Source: InterPro
    2. Sec61 translocon complex Source: InterPro

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36149.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Translocon-associated protein subunit gammaPRO_0000191690Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine2 Publications
    Modified residuei105 – 1051PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UNL2.
    PaxDbiQ9UNL2.
    PRIDEiQ9UNL2.

    PTM databases

    PhosphoSiteiQ9UNL2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UNL2.
    BgeeiQ9UNL2.
    CleanExiHS_SSR3.
    GenevestigatoriQ9UNL2.

    Organism-specific databases

    HPAiHPA014906.

    Interactioni

    Subunit structurei

    Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma.

    Protein-protein interaction databases

    BioGridi112625. 20 interactions.
    IntActiQ9UNL2. 3 interactions.
    MINTiMINT-1032208.
    STRINGi9606.ENSP00000265044.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UNL2.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727LumenalSequence AnalysisAdd
    BLAST
    Topological domaini49 – 546CytoplasmicSequence Analysis
    Topological domaini77 – 13559LumenalSequence AnalysisAdd
    BLAST
    Topological domaini158 – 1636CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei55 – 7622HelicalSequence AnalysisAdd
    BLAST
    Transmembranei136 – 15722HelicalSequence AnalysisAdd
    BLAST
    Transmembranei164 – 18421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the TRAP-gamma family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG255012.
    HOGENOMiHOG000007534.
    HOVERGENiHBG012424.
    InParanoidiQ9UNL2.
    KOiK13251.
    OrthoDBiEOG7W9RWF.
    PhylomeDBiQ9UNL2.
    TreeFamiTF314998.

    Family and domain databases

    InterProiIPR009779. TRAP-gamma.
    [Graphical view]
    PANTHERiPTHR13399. PTHR13399. 1 hit.
    PfamiPF07074. TRAP-gamma. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UNL2-1) [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

    MAPKGSSKQQ SEEDLLLQDF SRNLSAKSSA LFFGNAFIVS AIPIWLYWRI    50
    WHMDLIQSAV LYSVMTLVST YLVAFAYKNV KFVLKHKVAQ KREDAVSKEV 100
    TRKLSEADNR KMSRKEKDER ILWKKNEVAD YEATTFSIFY NNTLFLVVVI 150
    VASFFILKNF NPTVNYILSI SASSGLIALL STGSK 185
    Length:185
    Mass (Da):21,080
    Last modified:May 1, 2000 - v1
    Checksum:iDEE0B14BF524F62A
    GO
    Isoform 2 (identifier: Q9UNL2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         120-120: R → RFDSCLKYGHHKRG

    Note: No experimental confirmation available.

    Show »
    Length:198
    Mass (Da):22,610
    Checksum:iC66D0F4D32D36719
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei120 – 1201R → RFDSCLKYGHHKRG in isoform 2. 1 PublicationVSP_056195

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087907 mRNA. Translation: AAP97205.1.
    AF110647 mRNA. Translation: AAD48587.1.
    BT006669 mRNA. Translation: AAP35315.1.
    AK304364 mRNA. Translation: BAG65204.1.
    AK312935 mRNA. Translation: BAG35777.1.
    AC092927 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78730.1.
    CH471052 Genomic DNA. Translation: EAW78731.1.
    BC017203 mRNA. Translation: AAH17203.1.
    CCDSiCCDS3176.1.
    RefSeqiNP_009038.1. NM_007107.3.
    UniGeneiHs.518346.

    Genome annotation databases

    EnsembliENST00000265044; ENSP00000265044; ENSG00000114850.
    ENST00000467789; ENSP00000420641; ENSG00000114850.
    GeneIDi6747.
    KEGGihsa:6747.
    UCSCiuc003fau.3. human.

    Polymorphism databases

    DMDMi9087205.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087907 mRNA. Translation: AAP97205.1 .
    AF110647 mRNA. Translation: AAD48587.1 .
    BT006669 mRNA. Translation: AAP35315.1 .
    AK304364 mRNA. Translation: BAG65204.1 .
    AK312935 mRNA. Translation: BAG35777.1 .
    AC092927 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78730.1 .
    CH471052 Genomic DNA. Translation: EAW78731.1 .
    BC017203 mRNA. Translation: AAH17203.1 .
    CCDSi CCDS3176.1.
    RefSeqi NP_009038.1. NM_007107.3.
    UniGenei Hs.518346.

    3D structure databases

    ProteinModelPortali Q9UNL2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112625. 20 interactions.
    IntActi Q9UNL2. 3 interactions.
    MINTi MINT-1032208.
    STRINGi 9606.ENSP00000265044.

    PTM databases

    PhosphoSitei Q9UNL2.

    Polymorphism databases

    DMDMi 9087205.

    Proteomic databases

    MaxQBi Q9UNL2.
    PaxDbi Q9UNL2.
    PRIDEi Q9UNL2.

    Protocols and materials databases

    DNASUi 6747.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265044 ; ENSP00000265044 ; ENSG00000114850 .
    ENST00000467789 ; ENSP00000420641 ; ENSG00000114850 .
    GeneIDi 6747.
    KEGGi hsa:6747.
    UCSCi uc003fau.3. human.

    Organism-specific databases

    CTDi 6747.
    GeneCardsi GC03M156257.
    HGNCi HGNC:11325. SSR3.
    HPAi HPA014906.
    MIMi 606213. gene.
    neXtProti NX_Q9UNL2.
    PharmGKBi PA36149.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255012.
    HOGENOMi HOG000007534.
    HOVERGENi HBG012424.
    InParanoidi Q9UNL2.
    KOi K13251.
    OrthoDBi EOG7W9RWF.
    PhylomeDBi Q9UNL2.
    TreeFami TF314998.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi SSR3. human.
    GenomeRNAii 6747.
    NextBioi 26320.
    PROi Q9UNL2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNL2.
    Bgeei Q9UNL2.
    CleanExi HS_SSR3.
    Genevestigatori Q9UNL2.

    Family and domain databases

    InterProi IPR009779. TRAP-gamma.
    [Graphical view ]
    PANTHERi PTHR13399. PTHR13399. 1 hit.
    Pfami PF07074. TRAP-gamma. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel human cDNA homolog to R.norvegicus TRAP-complex gamma subunit mRNA."
      Huang H.B., Yu L., Yang J., Zhang H.L., Yang Y.M., Zhao S.Y.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Human translocon-associated protein, gamma subunit gene."
      Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Pituitary.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Prostate and Trachea.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin.
    8. "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-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSSRG_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNL2
    Secondary accession number(s): B2R7D0
    , B4E2P2, D3DNK5, Q549M4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 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 3
      Human chromosome 3: 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