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STALP_HUMAN
ID   STALP_HUMAN             Reviewed;         436 AA.
AC   Q96FJ0; B3KPA7; Q5T9N4; Q5T9N9; Q7Z420; Q9P2H4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=AMSH-like protease {ECO:0000303|PubMed:12810066};
DE            Short=AMSH-LP {ECO:0000303|PubMed:12810066};
DE            EC=3.4.19.- {ECO:0000269|PubMed:35114100};
DE   AltName: Full=STAM-binding protein-like 1;
GN   Name=STAMBPL1 {ECO:0000303|PubMed:35114100, ECO:0000312|HGNC:HGNC:24105};
GN   Synonyms=AMSHLP, KIAA1373;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Peripheral blood lymphocyte;
RX   PubMed=12810066; DOI=10.1016/s0006-291x(03)01009-x;
RA   Kikuchi K., Ishii N., Asano H., Sugamura K.;
RT   "Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme
RT   motif.";
RL   Biochem. Biophys. Res. Commun. 306:637-643(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVI. The
RT   complete sequences of 150 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:65-73(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas;
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-242, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF GLU-292 AND ASP-360.
RX   PubMed=35114100; DOI=10.1016/j.molcel.2022.01.002;
RA   Wang D., Xu C., Yang W., Chen J., Ou Y., Guan Y., Guan J., Liu Y.;
RT   "E3 ligase RNF167 and deubiquitinase STAMBPL1 modulate mTOR and cancer
RT   progression.";
RL   Mol. Cell 82:770-784(2022).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 263-436 IN COMPLEXES WITH ZINC
RP   IONS AND WITH LYS-63-LINKED DI-UBIQUITIN, FUNCTION, COFACTOR, AND
RP   MUTAGENESIS OF GLU-292; GLU-329; PHE-332; THR-353; PHE-355; SER-357;
RP   SER-358; ASP-360; MET-370; CYS-402 AND PHE-407.
RX   PubMed=18758443; DOI=10.1038/nature07254;
RA   Sato Y., Yoshikawa A., Yamagata A., Mimura H., Yamashita M., Ookata K.,
RA   Nureki O., Iwai K., Komada M., Fukai S.;
RT   "Structural basis for specific cleavage of Lys 63-linked polyubiquitin
RT   chains.";
RL   Nature 455:358-362(2008).
RN   [12]
RP   ERRATUM OF PUBMED:18758443.
RX   DOI=10.1038/nature07515;
RA   Sato Y., Yoshikawa A., Yamagata A., Mimura H., Yamashita M., Ookata K.,
RA   Nureki O., Iwai K., Komada M., Fukai S.;
RL   Nature 456:274-274(2008).
RN   [13] {ECO:0007744|PDB:7L97}
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 263-436 IN COMPLEX WITH ZINC AND
RP   UBIQUITIN VARIANT INHIBITOR UBVSP.1, AND ACTIVITY REGULATION.
RX   PubMed=34425109; DOI=10.1016/j.jbc.2021.101107;
RA   Guo Y., Liu Q., Mallette E., Caba C., Hou F., Fux J., LaPlante G., Dong A.,
RA   Zhang Q., Zheng H., Tong Y., Zhang W.;
RT   "Structural and functional characterization of ubiquitin variant inhibitors
RT   for the JAMM-family deubiquitinases STAMBP and STAMBPL1.";
RL   J. Biol. Chem. 297:101107-101107(2021).
CC   -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC       linked polyubiquitin chains (PubMed:18758443, PubMed:35114100). Acts as
CC       a positive regulator of the TORC1 signaling pathway by mediating 'Lys-
CC       63'-linked deubiquitination of SESN2, thereby inhibiting SESN2-
CC       interaction with the GATOR2 complex (PubMed:35114100). Does not cleave
CC       'Lys-48'-linked polyubiquitin chains (PubMed:18758443).
CC       {ECO:0000269|PubMed:18758443, ECO:0000269|PubMed:35114100}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:18758443};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:18758443};
CC   -!- ACTIVITY REGULATION: Inhibited by UbV(SP.1), an ubiquitin variant that
CC       also inhibits STAMBP. {ECO:0000269|PubMed:34425109}.
CC   -!- INTERACTION:
CC       Q96FJ0; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-745021, EBI-739580;
CC       Q96FJ0; Q9P209: CEP72; NbExp=8; IntAct=EBI-745021, EBI-739498;
CC       Q96FJ0; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-745021, EBI-17857617;
CC       Q96FJ0; Q3T906: GNPTAB; NbExp=3; IntAct=EBI-745021, EBI-1104907;
CC       Q96FJ0; Q08379: GOLGA2; NbExp=3; IntAct=EBI-745021, EBI-618309;
CC       Q96FJ0; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-745021, EBI-5916454;
CC       Q96FJ0; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-745021, EBI-747204;
CC       Q96FJ0; Q0VD86: INCA1; NbExp=3; IntAct=EBI-745021, EBI-6509505;
CC       Q96FJ0; Q8IWV1: LAX1; NbExp=3; IntAct=EBI-745021, EBI-10232942;
CC       Q96FJ0; P43357: MAGEA3; NbExp=4; IntAct=EBI-745021, EBI-5651459;
CC       Q96FJ0; P43360: MAGEA6; NbExp=6; IntAct=EBI-745021, EBI-1045155;
CC       Q96FJ0; Q5VZ52: MORN5; NbExp=3; IntAct=EBI-745021, EBI-12835568;
CC       Q96FJ0; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-745021, EBI-742388;
CC       Q96FJ0; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-745021, EBI-302345;
CC       Q96FJ0; P61019: RAB2A; NbExp=10; IntAct=EBI-745021, EBI-752037;
CC       Q96FJ0; Q8WUD1: RAB2B; NbExp=3; IntAct=EBI-745021, EBI-5542466;
CC       Q96FJ0; Q04864-2: REL; NbExp=3; IntAct=EBI-745021, EBI-10829018;
CC       Q96FJ0; Q9H0A6: RNF32; NbExp=2; IntAct=EBI-745021, EBI-724829;
CC       Q96FJ0; Q9BWJ5: SF3B5; NbExp=3; IntAct=EBI-745021, EBI-2555428;
CC       Q96FJ0; P15884: TCF4; NbExp=3; IntAct=EBI-745021, EBI-533224;
CC       Q96FJ0; P14373: TRIM27; NbExp=6; IntAct=EBI-745021, EBI-719493;
CC       Q96FJ0; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-745021, EBI-5667516;
CC       Q96FJ0; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-745021, EBI-527853;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96FJ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96FJ0-2; Sequence=VSP_014648;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:12810066}.
CC   -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC       {ECO:0000250|UniProtKB:O35864}.
CC   -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA92611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB010120; BAC77766.1; -; mRNA.
DR   EMBL; AB037794; BAA92611.1; ALT_INIT; mRNA.
DR   EMBL; AK056086; BAG51619.1; -; mRNA.
DR   EMBL; AL157394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW50156.1; -; Genomic_DNA.
DR   EMBL; BC010846; AAH10846.2; -; mRNA.
DR   CCDS; CCDS7391.1; -. [Q96FJ0-1]
DR   RefSeq; NP_065850.1; NM_020799.3. [Q96FJ0-1]
DR   RefSeq; XP_006717991.1; XM_006717928.2. [Q96FJ0-1]
DR   RefSeq; XP_006717993.1; XM_006717930.3. [Q96FJ0-1]
DR   RefSeq; XP_011538285.1; XM_011539983.1. [Q96FJ0-1]
DR   RefSeq; XP_011538287.1; XM_011539985.1. [Q96FJ0-1]
DR   RefSeq; XP_016871942.1; XM_017016453.1. [Q96FJ0-1]
DR   RefSeq; XP_016871943.1; XM_017016454.1.
DR   RefSeq; XP_016871944.1; XM_017016455.1. [Q96FJ0-1]
DR   RefSeq; XP_016871945.1; XM_017016456.1. [Q96FJ0-1]
DR   PDB; 2ZNR; X-ray; 1.20 A; A=264-436.
DR   PDB; 2ZNV; X-ray; 1.60 A; A/D=264-436.
DR   PDB; 7L97; X-ray; 2.01 A; A=263-436.
DR   PDBsum; 2ZNR; -.
DR   PDBsum; 2ZNV; -.
DR   PDBsum; 7L97; -.
DR   AlphaFoldDB; Q96FJ0; -.
DR   SMR; Q96FJ0; -.
DR   BioGRID; 121614; 66.
DR   IntAct; Q96FJ0; 58.
DR   MINT; Q96FJ0; -.
DR   STRING; 9606.ENSP00000360994; -.
DR   BindingDB; Q96FJ0; -.
DR   ChEMBL; CHEMBL4630848; -.
DR   MEROPS; M67.003; -.
DR   iPTMnet; Q96FJ0; -.
DR   PhosphoSitePlus; Q96FJ0; -.
DR   BioMuta; STAMBPL1; -.
DR   DMDM; 71153542; -.
DR   EPD; Q96FJ0; -.
DR   jPOST; Q96FJ0; -.
DR   MassIVE; Q96FJ0; -.
DR   MaxQB; Q96FJ0; -.
DR   PaxDb; Q96FJ0; -.
DR   PeptideAtlas; Q96FJ0; -.
DR   PRIDE; Q96FJ0; -.
DR   ProteomicsDB; 76533; -. [Q96FJ0-1]
DR   ProteomicsDB; 76534; -. [Q96FJ0-2]
DR   Antibodypedia; 45641; 106 antibodies from 20 providers.
DR   DNASU; 57559; -.
DR   Ensembl; ENST00000371924.5; ENSP00000360992.1; ENSG00000138134.12. [Q96FJ0-1]
DR   Ensembl; ENST00000371926.8; ENSP00000360994.3; ENSG00000138134.12. [Q96FJ0-1]
DR   Ensembl; ENST00000371927.7; ENSP00000360995.3; ENSG00000138134.12. [Q96FJ0-2]
DR   GeneID; 57559; -.
DR   KEGG; hsa:57559; -.
DR   MANE-Select; ENST00000371926.8; ENSP00000360994.3; NM_020799.4; NP_065850.1.
DR   UCSC; uc001kfk.5; human. [Q96FJ0-1]
DR   CTD; 57559; -.
DR   DisGeNET; 57559; -.
DR   GeneCards; STAMBPL1; -.
DR   HGNC; HGNC:24105; STAMBPL1.
DR   HPA; ENSG00000138134; Tissue enhanced (adrenal).
DR   MIM; 612352; gene.
DR   neXtProt; NX_Q96FJ0; -.
DR   OpenTargets; ENSG00000138134; -.
DR   PharmGKB; PA142670864; -.
DR   VEuPathDB; HostDB:ENSG00000138134; -.
DR   eggNOG; KOG2880; Eukaryota.
DR   GeneTree; ENSGT00940000153710; -.
DR   HOGENOM; CLU_023304_0_1_1; -.
DR   InParanoid; Q96FJ0; -.
DR   OMA; FGVQDQH; -.
DR   OrthoDB; 411229at2759; -.
DR   PhylomeDB; Q96FJ0; -.
DR   TreeFam; TF323215; -.
DR   PathwayCommons; Q96FJ0; -.
DR   Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR   SignaLink; Q96FJ0; -.
DR   BioGRID-ORCS; 57559; 11 hits in 1113 CRISPR screens.
DR   ChiTaRS; STAMBPL1; human.
DR   EvolutionaryTrace; Q96FJ0; -.
DR   GeneWiki; STAMBPL1; -.
DR   GenomeRNAi; 57559; -.
DR   Pharos; Q96FJ0; Tbio.
DR   PRO; PR:Q96FJ0; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96FJ0; protein.
DR   Bgee; ENSG00000138134; Expressed in ileal mucosa and 182 other tissues.
DR   Genevisible; Q96FJ0; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR   GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR   CDD; cd08066; MPN_AMSH_like; 1.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR   InterPro; IPR015063; USP8_dimer.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF08969; USP8_dimer; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   PROSITE; PS50249; MPN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Hydrolase; Metal-binding;
KW   Metalloprotease; Phosphoprotein; Protease; Reference proteome;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN           1..436
FT                   /note="AMSH-like protease"
FT                   /id="PRO_0000194874"
FT   DOMAIN          269..397
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           347..360
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182,
FT                   ECO:0000269|PubMed:18758443, ECO:0007744|PDB:2ZNR"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182,
FT                   ECO:0000269|PubMed:18758443, ECO:0007744|PDB:2ZNR"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182,
FT                   ECO:0000269|PubMed:18758443, ECO:0007744|PDB:2ZNR"
FT   BINDING         362
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:34425109, ECO:0007744|PDB:2ZNR,
FT                   ECO:0007744|PDB:7L97"
FT   BINDING         402
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:34425109, ECO:0007744|PDB:2ZNR,
FT                   ECO:0007744|PDB:7L97"
FT   BINDING         408
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:34425109, ECO:0007744|PDB:2ZNR,
FT                   ECO:0007744|PDB:7L97"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:34425109, ECO:0007744|PDB:2ZNR,
FT                   ECO:0007744|PDB:7L97"
FT   SITE            292
FT                   /note="Indirect zinc-binding"
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         420..436
FT                   /note="CKHVLVKDIKIIVLDLR -> QKFLSGIISGTALEMEPLKIGYGPNGFPLLG
FT                   ISRSSSPSEQL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10718198"
FT                   /id="VSP_014648"
FT   VARIANT         196
FT                   /note="S -> N (in dbSNP:rs12254856)"
FT                   /id="VAR_051817"
FT   VARIANT         204
FT                   /note="E -> K (in dbSNP:rs34270879)"
FT                   /id="VAR_051818"
FT   VARIANT         210
FT                   /note="A -> T (in dbSNP:rs9988723)"
FT                   /id="VAR_051819"
FT   MUTAGEN         292
FT                   /note="E->A: Complete loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:35114100"
FT   MUTAGEN         329
FT                   /note="E->A: 3-fold decrease in substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         332
FT                   /note="F->A: 12-fold decrease in substrate affinity, little
FT                   effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         353
FT                   /note="T->A: 19-fold decrease in activity, no change in
FT                   substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         355
FT                   /note="F->A: 161-fold decrease in activity, no change in
FT                   substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         357
FT                   /note="S->A: 34-fold decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         358
FT                   /note="S->A: 10-fold decrease in activity, no change in
FT                   substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         360
FT                   /note="D->A: Complete loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18758443,
FT                   ECO:0000269|PubMed:35114100"
FT   MUTAGEN         370
FT                   /note="M->A: 18-fold decrease in substrate affinity, little
FT                   effect on catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         402
FT                   /note="C->S: 402-fold decrease in activity, slight increase
FT                   in substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   MUTAGEN         407
FT                   /note="F->A: 35-fold decrease in activity, slight increase
FT                   in substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:18758443"
FT   STRAND          269..272
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   HELIX           275..287
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          294..302
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          305..313
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          316..319
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          322..325
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   HELIX           328..338
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          341..348
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   HELIX           358..370
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          375..380
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          385..391
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   HELIX           393..401
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          416..419
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          421..426
FT                   /evidence="ECO:0007829|PDB:2ZNR"
FT   STRAND          431..434
FT                   /evidence="ECO:0007829|PDB:2ZNR"
SQ   SEQUENCE   436 AA;  49783 MW;  722662C76A734102 CRC64;
     MDQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI TISEDITPRR YFRSGVEMER
     MASVYLEEGN LENAFVLYNK FITLFVEKLP NHRDYQQCAV PEKQDIMKKL KEIAFPRTDE
     LKNDLLKKYN VEYQEYLQSK NKYKAEILKK LEHQRLIEAE RKRIAQMRQQ QLESEQFLFF
     EDQLKKQELA RGQMRSQQTS GLSEQIDGSA LSCFSTHQNN SLLNVFADQP NKSDATNYAS
     HSPPVNRALT PAATLSAVQN LVVEGLRCVV LPEDLCHKFL QLAESNTVRG IETCGILCGK
     LTHNEFTITH VIVPKQSAGP DYCDMENVEE LFNVQDQHDL LTLGWIHTHP TQTAFLSSVD
     LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS ACKKKGFHPH TKEPRLFSIC
     KHVLVKDIKI IVLDLR
 
 
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