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P43307

- SSRA_HUMAN

UniProt

P43307 - SSRA_HUMAN

Protein

Translocon-associated protein subunit alpha

Gene

SSR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (13 Aug 2002)
      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. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. cotranslational protein targeting to membrane Source: ProtInc
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. gene expression Source: Reactome
    6. positive regulation of cell proliferation Source: ProtInc
    7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    8. translation Source: Reactome

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_18273. XBP1(S) activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translocon-associated protein subunit alpha
    Short name:
    TRAP-alpha
    Alternative name(s):
    Signal sequence receptor subunit alpha
    Short name:
    SSR-alpha
    Gene namesi
    Name:SSR1
    Synonyms:TRAPA
    ORF Names:PSEC0262
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:11323. SSR1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: HPA
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36147.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 18181 PublicationAdd
    BLAST
    Chaini19 – 286268Translocon-associated protein subunit alphaPRO_0000033281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi136 – 1361N-linked (GlcNAc...)2 Publications
    Glycosylationi191 – 1911N-linked (GlcNAc...)1 Publication
    Modified residuei247 – 2471Phosphoserine1 Publication
    Modified residuei260 – 2601Phosphothreonine1 Publication
    Modified residuei268 – 2681Phosphoserine6 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP43307.
    PaxDbiP43307.
    PeptideAtlasiP43307.
    PRIDEiP43307.

    PTM databases

    PhosphoSiteiP43307.

    Expressioni

    Gene expression databases

    ArrayExpressiP43307.
    BgeeiP43307.
    GenevestigatoriP43307.

    Organism-specific databases

    HPAiHPA011276.
    HPA017062.

    Interactioni

    Subunit structurei

    Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and TRAP-gamma. Interacts with palmitoylated calnexin (CALX), the interaction is required for efficient folding of glycosylated proteins.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CANXP278245EBI-714168,EBI-355947
    SERPINA1P010094EBI-714168,EBI-986224

    Protein-protein interaction databases

    BioGridi112623. 35 interactions.
    IntActiP43307. 23 interactions.
    MINTiMINT-1379984.

    Structurei

    3D structure databases

    ProteinModelPortaliP43307.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 207189LumenalSequence AnalysisAdd
    BLAST
    Topological domaini229 – 28658CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei208 – 22821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domaini

    Shows a remarkable charge distribution with the N-terminus being highly negatively charged, and the cytoplasmic C-terminus positively charged.

    Sequence similaritiesi

    Belongs to the TRAP-alpha family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG127973.
    HOVERGENiHBG009736.
    KOiK13249.
    PhylomeDBiP43307.
    TreeFamiTF321074.

    Family and domain databases

    InterProiIPR005595. TRAP_alpha.
    [Graphical view]
    PfamiPF03896. TRAP_alpha. 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: P43307-1) [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

    MRLLPRLLLL LLLVFPATVL FRGGPRGLLA VAQDLTEDEE TVEDSIIEDE    50
    DDEAEVEEDE PTDLVEDKEE EDVSGEPEAS PSADTTILFV KGEDFPANNI 100
    VKFLVGFTNK GTEDFIVESL DASFRYPQDY QFYIQNFTAL PLNTVVPPQR 150
    QATFEYSFIP AEPMGGRPFG LVINLNYKDL NGNVFQDAVF NQTVTVIERE 200
    DGLDGETIFM YMFLAGLGLL VIVGLHQLLE SRKRKRPIQK VEMGTSSQND 250
    VDMSWIPQET LNQINKASPR RLPRKRAQKR SVGSDE 286
    Length:286
    Mass (Da):32,235
    Last modified:August 13, 2002 - v3
    Checksum:i2C631DC0CC3EB489
    GO
    Isoform 2 (identifier: P43307-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         68-94: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:259
    Mass (Da):29,373
    Checksum:iD79F40EE756B1CB5
    GO

    Sequence cautioni

    The sequence CAI16444.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61R → G in BAC11701. (PubMed:16303743)Curated
    Sequence conflicti37 – 371E → A in BAD96529. 1 PublicationCurated
    Sequence conflicti130 – 1301Y → H in CAA78290. (PubMed:8050590)Curated
    Sequence conflicti190 – 1901F → Y in BAF84239. (PubMed:14702039)Curated
    Sequence conflicti220 – 2201L → P in BAD96529. 1 PublicationCurated
    Sequence conflicti263 – 2631Q → R in BAF84239. (PubMed:14702039)Curated
    Sequence conflicti286 – 2861E → D in CAG33242. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281L → S.2 Publications
    Corresponds to variant rs10004 [ dbSNP | Ensembl ].
    VAR_022427

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei68 – 9427Missing in isoform 2. 1 PublicationVSP_013621Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12830 mRNA. Translation: CAA78290.1.
    AF156965 mRNA. Translation: AAD48778.1.
    BT007387 mRNA. Translation: AAP36051.1.
    AK291550 mRNA. Translation: BAF84239.1.
    CR456961 mRNA. Translation: CAG33242.1.
    AK222762 mRNA. Translation: BAD96482.1.
    AK222809 mRNA. Translation: BAD96529.1.
    AK075562 mRNA. Translation: BAC11701.1.
    AL139095 Genomic DNA. Translation: CAI16444.1. Sequence problems.
    BC007710 mRNA. Translation: AAH07710.1.
    CCDSiCCDS4499.1. [P43307-1]
    PIRiI38246.
    RefSeqiNP_003135.2. NM_003144.4. [P43307-1]
    UniGeneiHs.114033.

    Genome annotation databases

    EnsembliENST00000244763; ENSP00000244763; ENSG00000124783. [P43307-1]
    GeneIDi6745.
    KEGGihsa:6745.
    UCSCiuc003mxf.4. human. [P43307-1]

    Polymorphism databases

    DMDMi22261821.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z12830 mRNA. Translation: CAA78290.1 .
    AF156965 mRNA. Translation: AAD48778.1 .
    BT007387 mRNA. Translation: AAP36051.1 .
    AK291550 mRNA. Translation: BAF84239.1 .
    CR456961 mRNA. Translation: CAG33242.1 .
    AK222762 mRNA. Translation: BAD96482.1 .
    AK222809 mRNA. Translation: BAD96529.1 .
    AK075562 mRNA. Translation: BAC11701.1 .
    AL139095 Genomic DNA. Translation: CAI16444.1 . Sequence problems.
    BC007710 mRNA. Translation: AAH07710.1 .
    CCDSi CCDS4499.1. [P43307-1 ]
    PIRi I38246.
    RefSeqi NP_003135.2. NM_003144.4. [P43307-1 ]
    UniGenei Hs.114033.

    3D structure databases

    ProteinModelPortali P43307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112623. 35 interactions.
    IntActi P43307. 23 interactions.
    MINTi MINT-1379984.

    PTM databases

    PhosphoSitei P43307.

    Polymorphism databases

    DMDMi 22261821.

    Proteomic databases

    MaxQBi P43307.
    PaxDbi P43307.
    PeptideAtlasi P43307.
    PRIDEi P43307.

    Protocols and materials databases

    DNASUi 6745.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244763 ; ENSP00000244763 ; ENSG00000124783 . [P43307-1 ]
    GeneIDi 6745.
    KEGGi hsa:6745.
    UCSCi uc003mxf.4. human. [P43307-1 ]

    Organism-specific databases

    CTDi 6745.
    GeneCardsi GC06M007232.
    HGNCi HGNC:11323. SSR1.
    HPAi HPA011276.
    HPA017062.
    MIMi 600868. gene.
    neXtProti NX_P43307.
    PharmGKBi PA36147.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG127973.
    HOVERGENi HBG009736.
    KOi K13249.
    PhylomeDBi P43307.
    TreeFami TF321074.

    Enzyme and pathway databases

    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_18273. XBP1(S) activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi SSR1. human.
    GeneWikii SSR1.
    GenomeRNAii 6745.
    NextBioi 26310.
    PROi P43307.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P43307.
    Bgeei P43307.
    Genevestigatori P43307.

    Family and domain databases

    InterProi IPR005595. TRAP_alpha.
    [Graphical view ]
    Pfami PF03896. TRAP_alpha. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The N-terminal region of the alpha-subunit of the TRAP complex has a conserved cluster of negative charges."
      Hartmann E., Prehn S.
      FEBS Lett. 349:324-326(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-28.
    2. "Translocon-associated protein alpha transcripts are induced by granulocyte-macrophage colony-stimulating factor and exhibit complex alternative polyadenylation."
      Hirama T., Miller C.W., Koeffler H.P.
      FEBS Lett. 455:223-227(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
      Tissue: Placenta.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-28.
      Tissue: Liver.
    7. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
      Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
      , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
      DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Teratocarcinoma.
    8. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: B-cell.
    10. "HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides."
      Wei M.L., Cresswell P.
      Nature 356:443-446(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 19-31.
    11. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-136.
    12. "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-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-191.
      Tissue: Liver.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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 THR-260 AND SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Palmitoylated calnexin is a key component of the ribosome-translocon complex."
      Lakkaraju A.K., Abrami L., Lemmin T., Blaskovic S., Kunz B., Kihara A., Dal Peraro M., van der Goot F.G.
      EMBO J. 31:1823-1835(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CALNEXIN.

    Entry informationi

    Entry nameiSSRA_HUMAN
    AccessioniPrimary (citable) accession number: P43307
    Secondary accession number(s): A8K685
    , Q53GX2, Q53H19, Q5TAM3, Q6IB43, Q8NBH9, Q96IA2, Q9TNQ8, Q9UN49
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: August 13, 2002
    Last modified: October 1, 2014
    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

    Miscellaneous

    Seems to bind calcium.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

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