Full text data of SPCS2
SPCS2
(KIAA0102, SPC25)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Signal peptidase complex subunit 2; 3.4.-.- (Microsomal signal peptidase 25 kDa subunit; SPase 25 kDa subunit)
Signal peptidase complex subunit 2; 3.4.-.- (Microsomal signal peptidase 25 kDa subunit; SPase 25 kDa subunit)
UniProt
Q15005
ID SPCS2_HUMAN Reviewed; 226 AA.
AC Q15005; Q15507; Q3KQT0; Q641R4; Q6FG65; Q6IRX0; Q6P1P4; Q96HU9;
read moreDT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Signal peptidase complex subunit 2;
DE EC=3.4.-.-;
DE AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE Short=SPase 25 kDa subunit;
GN Name=SPCS2; Synonyms=KIAA0102, SPC25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Pancreas, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
RA Hartmann E.;
RT "5'-end of human signal peptidase 25kDa subunit mRNA.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-226.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [4]
RP PROTEIN SEQUENCE OF 2-10; 174-180 AND 196-214, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Lao L., Ryan K.M.;
RL Submitted (MAY-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-226.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169 AND LYS-191, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the microsomal signal peptidase complex
CC which removes signal peptides from nascent proteins as they are
CC translocated into the lumen of the endoplasmic reticulum (By
CC similarity).
CC -!- SUBUNIT: Component of the microsomal signal peptidase complex
CC which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and
CC SPCS3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane
CC protein (By similarity). Endoplasmic reticulum membrane; Multi-
CC pass membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the SPCS2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08063.3; Type=Erroneous initiation;
CC Sequence=AAH70276.2; Type=Erroneous initiation;
CC Sequence=AAH82231.2; Type=Erroneous initiation;
CC Sequence=BAA03492.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BC008063; AAH08063.3; ALT_INIT; mRNA.
DR EMBL; BC064957; AAH64957.1; -; mRNA.
DR EMBL; BC070276; AAH70276.2; ALT_INIT; mRNA.
DR EMBL; BC082231; AAH82231.2; ALT_INIT; mRNA.
DR EMBL; BC106066; AAI06067.1; -; mRNA.
DR EMBL; L38950; AAA60992.1; -; mRNA.
DR EMBL; D14658; BAA03492.1; ALT_INIT; mRNA.
DR EMBL; CR542233; CAG47029.1; -; mRNA.
DR EMBL; CR542243; CAG47039.1; -; mRNA.
DR RefSeq; NP_055567.2; NM_014752.2.
DR UniGene; Hs.282700; -.
DR UniGene; Hs.719927; -.
DR ProteinModelPortal; Q15005; -.
DR DIP; DIP-47276N; -.
DR IntAct; Q15005; 5.
DR MINT; MINT-1382200; -.
DR STRING; 9606.ENSP00000263672; -.
DR PhosphoSite; Q15005; -.
DR DMDM; 6648110; -.
DR PaxDb; Q15005; -.
DR PRIDE; Q15005; -.
DR DNASU; 9789; -.
DR Ensembl; ENST00000263672; ENSP00000263672; ENSG00000118363.
DR GeneID; 9789; -.
DR KEGG; hsa:9789; -.
DR UCSC; uc001ovu.2; human.
DR CTD; 9789; -.
DR GeneCards; GC11P074660; -.
DR H-InvDB; HIX0028705; -.
DR HGNC; HGNC:28962; SPCS2.
DR HPA; HPA013386; -.
DR neXtProt; NX_Q15005; -.
DR PharmGKB; PA128394559; -.
DR eggNOG; NOG150008; -.
DR HOVERGEN; HBG093979; -.
DR InParanoid; Q15005; -.
DR KO; K12947; -.
DR OrthoDB; EOG7X6M1N; -.
DR BRENDA; 3.4.21.89; 2681.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR GenomeRNAi; 9789; -.
DR NextBio; 36862; -.
DR PRO; PR:Q15005; -.
DR ArrayExpress; Q15005; -.
DR Bgee; Q15005; -.
DR CleanEx; HS_SPC25; -.
DR CleanEx; HS_SPCS2; -.
DR Genevestigator; Q15005; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR009582; SigPept_cplx_su2.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Membrane; Microsome; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 Signal peptidase complex subunit 2.
FT /FTId=PRO_0000221158.
FT TOPO_DOM 2 86 Cytoplasmic (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 111 Lumenal (Potential).
FT TRANSMEM 112 132 Helical; (Potential).
FT TOPO_DOM 133 226 Cytoplasmic (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 169 169 N6-acetyllysine.
FT MOD_RES 191 191 N6-acetyllysine.
FT CONFLICT 64 64 A -> V (in Ref. 1; AAH64957).
SQ SEQUENCE 226 AA; 25003 MW; C1EDF687E9F7A57A CRC64;
MAAAAVQGGR SGGSGGCSGA GGASNCGTGS GRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA IERKIK
//
ID SPCS2_HUMAN Reviewed; 226 AA.
AC Q15005; Q15507; Q3KQT0; Q641R4; Q6FG65; Q6IRX0; Q6P1P4; Q96HU9;
read moreDT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Signal peptidase complex subunit 2;
DE EC=3.4.-.-;
DE AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE Short=SPase 25 kDa subunit;
GN Name=SPCS2; Synonyms=KIAA0102, SPC25;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Pancreas, Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
RA Hartmann E.;
RT "5'-end of human signal peptidase 25kDa subunit mRNA.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-226.
RC TISSUE=Bone marrow;
RX PubMed=7788527; DOI=10.1093/dnares/2.1.37;
RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S.,
RA Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. III.
RT The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:37-43(1995).
RN [4]
RP PROTEIN SEQUENCE OF 2-10; 174-180 AND 196-214, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Lao L., Ryan K.M.;
RL Submitted (MAY-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-226.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169 AND LYS-191, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the microsomal signal peptidase complex
CC which removes signal peptides from nascent proteins as they are
CC translocated into the lumen of the endoplasmic reticulum (By
CC similarity).
CC -!- SUBUNIT: Component of the microsomal signal peptidase complex
CC which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and
CC SPCS3 (By similarity).
CC -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane
CC protein (By similarity). Endoplasmic reticulum membrane; Multi-
CC pass membrane protein (By similarity).
CC -!- SIMILARITY: Belongs to the SPCS2 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08063.3; Type=Erroneous initiation;
CC Sequence=AAH70276.2; Type=Erroneous initiation;
CC Sequence=AAH82231.2; Type=Erroneous initiation;
CC Sequence=BAA03492.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; BC008063; AAH08063.3; ALT_INIT; mRNA.
DR EMBL; BC064957; AAH64957.1; -; mRNA.
DR EMBL; BC070276; AAH70276.2; ALT_INIT; mRNA.
DR EMBL; BC082231; AAH82231.2; ALT_INIT; mRNA.
DR EMBL; BC106066; AAI06067.1; -; mRNA.
DR EMBL; L38950; AAA60992.1; -; mRNA.
DR EMBL; D14658; BAA03492.1; ALT_INIT; mRNA.
DR EMBL; CR542233; CAG47029.1; -; mRNA.
DR EMBL; CR542243; CAG47039.1; -; mRNA.
DR RefSeq; NP_055567.2; NM_014752.2.
DR UniGene; Hs.282700; -.
DR UniGene; Hs.719927; -.
DR ProteinModelPortal; Q15005; -.
DR DIP; DIP-47276N; -.
DR IntAct; Q15005; 5.
DR MINT; MINT-1382200; -.
DR STRING; 9606.ENSP00000263672; -.
DR PhosphoSite; Q15005; -.
DR DMDM; 6648110; -.
DR PaxDb; Q15005; -.
DR PRIDE; Q15005; -.
DR DNASU; 9789; -.
DR Ensembl; ENST00000263672; ENSP00000263672; ENSG00000118363.
DR GeneID; 9789; -.
DR KEGG; hsa:9789; -.
DR UCSC; uc001ovu.2; human.
DR CTD; 9789; -.
DR GeneCards; GC11P074660; -.
DR H-InvDB; HIX0028705; -.
DR HGNC; HGNC:28962; SPCS2.
DR HPA; HPA013386; -.
DR neXtProt; NX_Q15005; -.
DR PharmGKB; PA128394559; -.
DR eggNOG; NOG150008; -.
DR HOVERGEN; HBG093979; -.
DR InParanoid; Q15005; -.
DR KO; K12947; -.
DR OrthoDB; EOG7X6M1N; -.
DR BRENDA; 3.4.21.89; 2681.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR GenomeRNAi; 9789; -.
DR NextBio; 36862; -.
DR PRO; PR:Q15005; -.
DR ArrayExpress; Q15005; -.
DR Bgee; Q15005; -.
DR CleanEx; HS_SPC25; -.
DR CleanEx; HS_SPCS2; -.
DR Genevestigator; Q15005; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR009582; SigPept_cplx_su2.
DR Pfam; PF06703; SPC25; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Membrane; Microsome; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 226 Signal peptidase complex subunit 2.
FT /FTId=PRO_0000221158.
FT TOPO_DOM 2 86 Cytoplasmic (Potential).
FT TRANSMEM 87 107 Helical; (Potential).
FT TOPO_DOM 108 111 Lumenal (Potential).
FT TRANSMEM 112 132 Helical; (Potential).
FT TOPO_DOM 133 226 Cytoplasmic (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 169 169 N6-acetyllysine.
FT MOD_RES 191 191 N6-acetyllysine.
FT CONFLICT 64 64 A -> V (in Ref. 1; AAH64957).
SQ SEQUENCE 226 AA; 25003 MW; C1EDF687E9F7A57A CRC64;
MAAAAVQGGR SGGSGGCSGA GGASNCGTGS GRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA IERKIK
//