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TSP50_HUMAN
ID   TSP50_HUMAN             Reviewed;         385 AA.
AC   Q9UI38;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Probable threonine protease PRSS50;
DE            EC=3.4.25.- {ECO:0000269|PubMed:17283160};
DE   AltName: Full=Cancer/testis antigen 20;
DE   AltName: Full=Serine protease 50;
DE   AltName: Full=Testis-specific protease-like protein 50;
DE   Flags: Precursor;
GN   Name=PRSS50; Synonyms=CT20, TSP50;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary cancer;
RX   PubMed=10397268;
RA   Yuan L., Shan J., De Risi D., Broome J., Lovecchio J., Gal D.,
RA   Vinciguerra V., Xu H.-P.;
RT   "Isolation of a novel gene, TSP50, by a hypomethylated DNA fragment in
RT   human breast cancer.";
RL   Cancer Res. 59:3215-3221(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   THR-310.
RX   PubMed=17283160; DOI=10.1158/0008-5472.can-06-3688;
RA   Xu H., Shan J., Jurukovski V., Yuan L., Li J., Tian K.;
RT   "TSP50 encodes a testis-specific protease and is negatively regulated by
RT   p53.";
RL   Cancer Res. 67:1239-1245(2007).
CC   -!- FUNCTION: May be involved in proteolysis through its threonine
CC       endopeptidase activity. {ECO:0000269|PubMed:17283160}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000305|PubMed:17283160}. Note=May also localize to cytoplasmic
CC       membranes.
CC   -!- TISSUE SPECIFICITY: Testis specific. Differentially expressed in some
CC       breast cancer tissues.
CC   -!- MISCELLANEOUS: DNA hypomethylation is accompanied by the expression of
CC       the gene in the testis.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
CC   -!- CAUTION: Although related to peptidase S1 family, lacks the conserved
CC       active Ser residue in position 310 which is replaced by a Thr.
CC       {ECO:0000305}.
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DR   EMBL; AF100707; AAF22500.1; -; mRNA.
DR   EMBL; BC033016; AAH33016.1; -; mRNA.
DR   EMBL; BC037775; AAH37775.1; -; mRNA.
DR   CCDS; CCDS2745.1; -.
DR   RefSeq; NP_037402.1; NM_013270.4.
DR   AlphaFoldDB; Q9UI38; -.
DR   SMR; Q9UI38; -.
DR   BioGRID; 118887; 49.
DR   IntAct; Q9UI38; 18.
DR   MINT; Q9UI38; -.
DR   STRING; 9606.ENSP00000418875; -.
DR   MEROPS; S01.993; -.
DR   GlyGen; Q9UI38; 2 sites.
DR   iPTMnet; Q9UI38; -.
DR   PhosphoSitePlus; Q9UI38; -.
DR   BioMuta; PRSS50; -.
DR   DMDM; 37089988; -.
DR   MassIVE; Q9UI38; -.
DR   PaxDb; Q9UI38; -.
DR   PeptideAtlas; Q9UI38; -.
DR   PRIDE; Q9UI38; -.
DR   ProteomicsDB; 84468; -.
DR   Antibodypedia; 78661; 55 antibodies from 9 providers.
DR   DNASU; 29122; -.
DR   Ensembl; ENST00000315170.13; ENSP00000326598.7; ENSG00000283706.2.
DR   GeneID; 29122; -.
DR   KEGG; hsa:29122; -.
DR   MANE-Select; ENST00000315170.13; ENSP00000326598.7; NM_013270.5; NP_037402.1.
DR   UCSC; uc003cqe.2; human.
DR   CTD; 29122; -.
DR   DisGeNET; 29122; -.
DR   GeneCards; PRSS50; -.
DR   HGNC; HGNC:17910; PRSS50.
DR   HPA; ENSG00000283706; Group enriched (pituitary gland, testis, thyroid gland).
DR   MIM; 607950; gene.
DR   neXtProt; NX_Q9UI38; -.
DR   OpenTargets; ENSG00000206549; -.
DR   PharmGKB; PA165698443; -.
DR   VEuPathDB; HostDB:ENSG00000206549; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   GeneTree; ENSGT00940000162593; -.
DR   HOGENOM; CLU_006842_0_4_1; -.
DR   InParanoid; Q9UI38; -.
DR   OMA; EQFCYEL; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q9UI38; -.
DR   TreeFam; TF351676; -.
DR   PathwayCommons; Q9UI38; -.
DR   SignaLink; Q9UI38; -.
DR   BioGRID-ORCS; 29122; 41 hits in 1059 CRISPR screens.
DR   GenomeRNAi; 29122; -.
DR   Pharos; Q9UI38; Tbio.
DR   PRO; PR:Q9UI38; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9UI38; protein.
DR   Bgee; ENSG00000283706; Expressed in right testis and 88 other tissues.
DR   ExpressionAtlas; Q9UI38; baseline.
DR   Genevisible; Q9UI38; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IMP:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Threonine protease.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..385
FT                   /note="Probable threonine protease PRSS50"
FT                   /id="PRO_0000028492"
FT   DOMAIN          93..358
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        206
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        310
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        279
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..154
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        240..316
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        273..296
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        306..334
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   VARIANT         75
FT                   /note="Q -> P (in dbSNP:rs34788938)"
FT                   /id="VAR_051859"
FT   VARIANT         98
FT                   /note="V -> I (in dbSNP:rs35866901)"
FT                   /id="VAR_051860"
FT   MUTAGEN         310
FT                   /note="T->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:17283160"
SQ   SEQUENCE   385 AA;  43088 MW;  F5B39D6E12798AE5 CRC64;
     MGRWCQTVAR GQRPRTSAPS RAGALLLLLL LLRSAGCWGA GEAPGALSTA DPADQSVQCV
     PKATCPSSRP RLLWQTPTTQ TLPSTTMETQ FPVSEGKVDP YRSCGFSYEQ DPTLRDPEAV
     ARRWPWMVSV RANGTHICAG TIIASQWVLT VAHCLIWRDV IYSVRVGSPW IDQMTQTASD
     VPVLQVIMHS RYRAQRFWSW VGQANDIGLL KLKQELKYSN YVRPICLPGT DYVLKDHSRC
     TVTGWGLSKA DGMWPQFRTI QEKEVIILNN KECDNFYHNF TKIPTLVQII KSQMMCAEDT
     HREKFCYELT GEPLVCSMEG TWYLVGLVSW GAGCQKSEAP PIYLQVSSYQ HWIWDCLNGQ
     ALALPAPSRT LLLALPLPLS LLAAL
 
 
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