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Q15005

- SPCS2_HUMAN

UniProt

Q15005 - SPCS2_HUMAN

Protein

Signal peptidase complex subunit 2

Gene

SPCS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (30 May 2000)
      Previous versions | rss
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    Functioni

    Component of the microsomal signal peptidase complex which removes signal peptides from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum.By similarity

    GO - Molecular functioni

    1. peptidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. regulation of insulin secretion Source: Reactome
    4. signal peptide processing Source: InterPro
    5. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    6. translation Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease

    Enzyme and pathway databases

    BRENDAi3.4.21.89. 2681.
    ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    REACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal peptidase complex subunit 2 (EC:3.4.-.-)
    Alternative name(s):
    Microsomal signal peptidase 25 kDa subunit
    Short name:
    SPase 25 kDa subunit
    Gene namesi
    Name:SPCS2
    Synonyms:KIAA0102, SPC25
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:28962. SPCS2.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. signal peptidase complex Source: InterPro

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394559.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 226225Signal peptidase complex subunit 2PRO_0000221158Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei169 – 1691N6-acetyllysine1 Publication
    Modified residuei191 – 1911N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ15005.
    PaxDbiQ15005.
    PRIDEiQ15005.

    PTM databases

    PhosphoSiteiQ15005.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15005.
    BgeeiQ15005.
    CleanExiHS_SPC25.
    HS_SPCS2.
    GenevestigatoriQ15005.

    Organism-specific databases

    HPAiHPA013386.

    Interactioni

    Subunit structurei

    Component of the microsomal signal peptidase complex which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and SPCS3.By similarity

    Protein-protein interaction databases

    BioGridi115133. 13 interactions.
    DIPiDIP-47276N.
    IntActiQ15005. 6 interactions.
    MINTiMINT-1382200.
    STRINGi9606.ENSP00000263672.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15005.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 8685CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini108 – 1114LumenalSequence Analysis
    Topological domaini133 – 22694CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei112 – 13221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the SPCS2 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG150008.
    HOVERGENiHBG093979.
    InParanoidiQ15005.
    KOiK12947.
    OrthoDBiEOG7X6M1N.
    PhylomeDBiQ15005.
    TreeFamiTF314545.

    Family and domain databases

    InterProiIPR009582. SigPept_cplx_su2.
    [Graphical view]
    PfamiPF06703. SPC25. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q15005-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAAVQGGR SGGSGGCSGA GGASNCGTGS GRSGLLDKWK IDDKPVKIDK    50
    WDGSAVKNSL DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI 100
    WDYMHPFPES KPVLALCVIS YFVMMGILTI YTSYKEKSIF LVAHRKDPTG 150
    MDPDDIWQLS SSLKRFDDKY TLKLTFISGR TKQQREAEFT KSIAKFFDHS 200
    GTLVMDAYEP EISRLHDSLA IERKIK 226
    Length:226
    Mass (Da):25,003
    Last modified:May 30, 2000 - v3
    Checksum:iC1EDF687E9F7A57A
    GO

    Sequence cautioni

    The sequence AAH08063.3 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH70276.2 differs from that shown. Reason: Erroneous initiation.
    The sequence AAH82231.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA03492.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641A → V in AAH64957. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC008063 mRNA. Translation: AAH08063.3. Different initiation.
    BC064957 mRNA. Translation: AAH64957.1.
    BC070276 mRNA. Translation: AAH70276.2. Different initiation.
    BC082231 mRNA. Translation: AAH82231.2. Different initiation.
    BC106066 mRNA. Translation: AAI06067.1.
    L38950 mRNA. Translation: AAA60992.1.
    D14658 mRNA. Translation: BAA03492.1. Different initiation.
    CR542233 mRNA. Translation: CAG47029.1.
    CR542243 mRNA. Translation: CAG47039.1.
    CCDSiCCDS44681.1.
    RefSeqiNP_055567.2. NM_014752.2.
    UniGeneiHs.282700.
    Hs.719927.

    Genome annotation databases

    EnsembliENST00000263672; ENSP00000263672; ENSG00000118363.
    GeneIDi9789.
    KEGGihsa:9789.
    UCSCiuc001ovu.2. human.

    Polymorphism databases

    DMDMi6648110.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC008063 mRNA. Translation: AAH08063.3 . Different initiation.
    BC064957 mRNA. Translation: AAH64957.1 .
    BC070276 mRNA. Translation: AAH70276.2 . Different initiation.
    BC082231 mRNA. Translation: AAH82231.2 . Different initiation.
    BC106066 mRNA. Translation: AAI06067.1 .
    L38950 mRNA. Translation: AAA60992.1 .
    D14658 mRNA. Translation: BAA03492.1 . Different initiation.
    CR542233 mRNA. Translation: CAG47029.1 .
    CR542243 mRNA. Translation: CAG47039.1 .
    CCDSi CCDS44681.1.
    RefSeqi NP_055567.2. NM_014752.2.
    UniGenei Hs.282700.
    Hs.719927.

    3D structure databases

    ProteinModelPortali Q15005.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115133. 13 interactions.
    DIPi DIP-47276N.
    IntActi Q15005. 6 interactions.
    MINTi MINT-1382200.
    STRINGi 9606.ENSP00000263672.

    PTM databases

    PhosphoSitei Q15005.

    Polymorphism databases

    DMDMi 6648110.

    Proteomic databases

    MaxQBi Q15005.
    PaxDbi Q15005.
    PRIDEi Q15005.

    Protocols and materials databases

    DNASUi 9789.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263672 ; ENSP00000263672 ; ENSG00000118363 .
    GeneIDi 9789.
    KEGGi hsa:9789.
    UCSCi uc001ovu.2. human.

    Organism-specific databases

    CTDi 9789.
    GeneCardsi GC11P074660.
    H-InvDB HIX0028705.
    HGNCi HGNC:28962. SPCS2.
    HPAi HPA013386.
    neXtProti NX_Q15005.
    PharmGKBi PA128394559.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150008.
    HOVERGENi HBG093979.
    InParanoidi Q15005.
    KOi K12947.
    OrthoDBi EOG7X6M1N.
    PhylomeDBi Q15005.
    TreeFami TF314545.

    Enzyme and pathway databases

    BRENDAi 3.4.21.89. 2681.
    Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
    REACT_23824. Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP).
    REACT_24019. Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).

    Miscellaneous databases

    GenomeRNAii 9789.
    NextBioi 36862.
    PROi Q15005.

    Gene expression databases

    ArrayExpressi Q15005.
    Bgeei Q15005.
    CleanExi HS_SPC25.
    HS_SPCS2.
    Genevestigatori Q15005.

    Family and domain databases

    InterProi IPR009582. SigPept_cplx_su2.
    [Graphical view ]
    Pfami PF06703. SPC25. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Lung, Pancreas, Skin and Testis.
    2. "5'-end of human signal peptidase 25kDa subunit mRNA."
      Hartmann E.
      Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
    3. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
      DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-226.
      Tissue: Bone marrow.
    4. Bienvenut W.V., Lao L., Ryan K.M.
      Submitted (MAY-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 174-180 AND 196-214, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    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] OF 104-226.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169 AND LYS-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSPCS2_HUMAN
    AccessioniPrimary (citable) accession number: Q15005
    Secondary accession number(s): Q15507
    , Q3KQT0, Q641R4, Q6FG65, Q6IRX0, Q6P1P4, Q96HU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 119 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3