SENP1_HUMAN
ID SENP1_HUMAN Reviewed; 644 AA.
AC Q9P0U3; A8K7P5; Q86XC8;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Sentrin-specific protease 1;
DE EC=3.4.22.- {ECO:0000269|PubMed:24943844, ECO:0000269|PubMed:29506078};
DE AltName: Full=Sentrin/SUMO-specific protease SENP1;
GN Name=SENP1;
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 2), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Placenta;
RX PubMed=10652325; DOI=10.1074/jbc.275.5.3355;
RA Gong L., Millas S., Maul G.G., Yeh E.T.H.;
RT "Differential regulation of sentrinized proteins by a novel sentrin-
RT specific protease.";
RL J. Biol. Chem. 275:3355-3359(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Stomach;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS VAL-193
RP AND GLY-350.
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 [5]
RP NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-603.
RX PubMed=14563852; DOI=10.1074/jbc.m306195200;
RA Bailey D., O'Hare P.;
RT "Characterization of the localization and proteolytic activity of the SUMO-
RT specific protease, SENP1.";
RL J. Biol. Chem. 279:692-703(2004).
RN [6]
RP FUNCTION.
RX PubMed=15199155; DOI=10.1128/mcb.24.13.6021-6028.2004;
RA Cheng J., Wang D., Wang Z., Yeh E.T.H.;
RT "SENP1 enhances androgen receptor-dependent transcription through
RT desumoylation of histone deacetylase 1.";
RL Mol. Cell. Biol. 24:6021-6028(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15487983; DOI=10.1042/bj20041210;
RA Xu Z., Au S.W.N.;
RT "Mapping residues of SUMO precursors essential in differential maturation
RT by SUMO-specific protease, SENP1.";
RL Biochem. J. 386:325-330(2005).
RN [8]
RP NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=16253240; DOI=10.1016/j.febslet.2005.10.010;
RA Kim Y.H., Sung K.S., Lee S.-J., Kim Y.-O., Choi C.Y., Kim Y.;
RT "Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through
RT the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1.";
RL FEBS Lett. 579:6272-6278(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP 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 [10]
RP FUNCTION, AND INTERACTION WITH MTA1.
RX PubMed=21965678; DOI=10.1074/jbc.m111.267237;
RA Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.;
RT "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1
RT (MTA1) synergistically regulate its transcriptional repressor function.";
RL J. Biol. Chem. 286:43793-43808(2011).
RN [11]
RP FUNCTION.
RX PubMed=21829689; DOI=10.1371/journal.pone.0023046;
RA Hong Y., Xing X., Li S., Bi H., Yang C., Zhao F., Liu Y., Ao X.,
RA Chang A.K., Wu H.;
RT "SUMOylation of DEC1 protein regulates its transcriptional activity and
RT enhances its stability.";
RL PLoS ONE 6:E23046-E23046(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-117; SER-132 AND
RP SER-157, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [13]
RP FUNCTION.
RX PubMed=23160374; DOI=10.1038/onc.2012.518;
RA Li S., Wang M., Ao X., Chang A.K., Yang C., Zhao F., Bi H., Liu Y.,
RA Xiao L., Wu H.;
RT "CLOCK is a substrate of SUMO and sumoylation of CLOCK upregulates the
RT transcriptional activity of estrogen receptor-alpha.";
RL Oncogene 32:4883-4891(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24943844; DOI=10.1091/mbc.e13-12-0733;
RA Bi H., Li S., Wang M., Jia Z., Chang A.K., Pang P., Wu H.;
RT "SUMOylation of GPS2 protein regulates its transcription-suppressing
RT function.";
RL Mol. Biol. Cell 25:2499-2508(2014).
RN [16]
RP FUNCTION, INTERACTION WITH CCAR2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-603.
RX PubMed=25406032; DOI=10.1038/ncomms6483;
RA Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W., Ka S.H.,
RA Oh K.H., Jeon Y.J., Chung C.H.;
RT "Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in
RT response to DNA damage.";
RL Nat. Commun. 5:5483-5483(2014).
RN [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29506078; DOI=10.1093/nar/gky156;
RA Du Y., Hou G., Zhang H., Dou J., He J., Guo Y., Li L., Chen R., Wang Y.,
RA Deng R., Huang J., Jiang B., Xu M., Cheng J., Chen G.Q., Zhao X., Yu J.;
RT "SUMOylation of the m6A-RNA methyltransferase METTL3 modulates its
RT function.";
RL Nucleic Acids Res. 46:5195-5208(2018).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 419-644, X-RAY CRYSTALLOGRAPHY
RP (3.2 ANGSTROMS) OF 419-644 IN COMPLEX WITH SUMO3, MUTAGENESIS OF ASP-441;
RP TRP-465; ASP-468; PHE-496; ARG-511; TRP-512; HIS-529; VAL-532; HIS-533;
RP TRP-534; ASP-550; GLN-597 AND CYS-603, AND FUNCTION.
RX PubMed=16553580; DOI=10.1042/bj20052030;
RA Shen L.N., Dong C., Liu H., Naismith J.H., Hay R.T.;
RT "The structure of SENP1-SUMO-2 complex suggests a structural basis for
RT discrimination between SUMO paralogues during processing.";
RL Biochem. J. 397:279-288(2006).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 439-644 IN COMPLEX WITH SUMO1, AND
RP MUTAGENESIS OF CYS-603.
RX PubMed=16712526; DOI=10.1042/bj20060526;
RA Xu Z., Chau S.F., Lam K.H., Chan H.Y., Ng T.B., Au S.W.N.;
RT "Crystal structure of the SENP1 mutant C603S-SUMO complex reveals the
RT hydrolytic mechanism of SUMO-specific protease.";
RL Biochem. J. 398:345-352(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 439-644 IN COMPLEX WITH RANGAP1
RP AND SUMO1.
RX PubMed=17099698; DOI=10.1038/nsmb1172;
RA Shen L., Tatham M.H., Dong C., Zagorska A., Naismith J.H., Hay R.T.;
RT "SUMO protease SENP1 induces isomerization of the scissile peptide bond.";
RL Nat. Struct. Mol. Biol. 13:1069-1077(2006).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway (PubMed:10652325, PubMed:15199155, PubMed:16253240,
CC PubMed:16553580, PubMed:21829689, PubMed:21965678, PubMed:23160374,
CC PubMed:24943844, PubMed:25406032, PubMed:29506078). The first is the
CC hydrolysis of an alpha-linked peptide bond at the C-terminal end of the
CC small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and
CC SUMO3 leading to the mature form of the proteins. The second is the
CC deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by
CC cleaving an epsilon-linked peptide bond between the C-terminal glycine
CC of the mature SUMO and the lysine epsilon-amino group of the target
CC protein. Deconjugates SUMO1 from HIPK2 (PubMed:16253240). Deconjugates
CC SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional
CC repression activity (PubMed:21829689). Deconjugates SUMO1 from CLOCK,
CC which decreases its transcriptional activation activity
CC (PubMed:23160374). Deconjugates SUMO2 from MTA1 (PubMed:21965678).
CC Deconjugates SUMO1 from METTL3 (PubMed:29506078). Desumoylates CCAR2
CC which decreases its interaction with SIRT1 (PubMed:25406032).
CC Deconjugates SUMO1 from GPS2 (PubMed:24943844).
CC {ECO:0000269|PubMed:10652325, ECO:0000269|PubMed:15199155,
CC ECO:0000269|PubMed:16253240, ECO:0000269|PubMed:16553580,
CC ECO:0000269|PubMed:21829689, ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:23160374, ECO:0000269|PubMed:24943844,
CC ECO:0000269|PubMed:25406032, ECO:0000269|PubMed:29506078}.
CC -!- SUBUNIT: Interacts with MTA1. Interacts with CCAR2 (via N-terminus).
CC {ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:16712526,
CC ECO:0000269|PubMed:17099698, ECO:0000269|PubMed:21965678,
CC ECO:0000269|PubMed:25406032}.
CC -!- INTERACTION:
CC Q9P0U3; P63165: SUMO1; NbExp=11; IntAct=EBI-2822935, EBI-80140;
CC Q9P0U3; P61956: SUMO2; NbExp=6; IntAct=EBI-2822935, EBI-473220;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25406032}. Cytoplasm.
CC Note=Shuttles between cytoplasm and nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P0U3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0U3-2; Sequence=VSP_035777;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
CC levels in thymus, pancreas, spleen, liver, ovary and small intestine.
CC {ECO:0000269|PubMed:15487983}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AF149770; AAF31171.1; -; mRNA.
DR EMBL; AK292060; BAF84749.1; -; mRNA.
DR EMBL; AC074029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC045639; AAH45639.2; -; mRNA.
DR CCDS; CCDS44868.2; -. [Q9P0U3-1]
DR RefSeq; NP_001254523.1; NM_001267594.1. [Q9P0U3-1]
DR RefSeq; NP_001254524.1; NM_001267595.1. [Q9P0U3-1]
DR PDB; 2CKG; X-ray; 2.45 A; A/B=419-644.
DR PDB; 2CKH; X-ray; 3.20 A; A=419-644.
DR PDB; 2G4D; X-ray; 2.80 A; A/C=440-644.
DR PDB; 2IY0; X-ray; 2.77 A; A=419-644.
DR PDB; 2IY1; X-ray; 2.46 A; A/C=419-644.
DR PDB; 2IYC; X-ray; 2.45 A; A/B=419-644.
DR PDB; 2IYD; X-ray; 3.20 A; A=419-644.
DR PDB; 2XPH; X-ray; 2.40 A; A/B=415-644.
DR PDB; 2XRE; X-ray; 2.45 A; A/B=415-644.
DR PDB; 6NNQ; X-ray; 2.62 A; A=421-644.
DR PDBsum; 2CKG; -.
DR PDBsum; 2CKH; -.
DR PDBsum; 2G4D; -.
DR PDBsum; 2IY0; -.
DR PDBsum; 2IY1; -.
DR PDBsum; 2IYC; -.
DR PDBsum; 2IYD; -.
DR PDBsum; 2XPH; -.
DR PDBsum; 2XRE; -.
DR PDBsum; 6NNQ; -.
DR AlphaFoldDB; Q9P0U3; -.
DR BMRB; Q9P0U3; -.
DR SMR; Q9P0U3; -.
DR BioGRID; 118930; 121.
DR DIP; DIP-29252N; -.
DR IntAct; Q9P0U3; 32.
DR MINT; Q9P0U3; -.
DR STRING; 9606.ENSP00000394791; -.
DR BindingDB; Q9P0U3; -.
DR ChEMBL; CHEMBL1909484; -.
DR GuidetoPHARMACOLOGY; 2414; -.
DR MEROPS; C48.002; -.
DR iPTMnet; Q9P0U3; -.
DR PhosphoSitePlus; Q9P0U3; -.
DR BioMuta; SENP1; -.
DR DMDM; 215273882; -.
DR EPD; Q9P0U3; -.
DR jPOST; Q9P0U3; -.
DR MassIVE; Q9P0U3; -.
DR MaxQB; Q9P0U3; -.
DR PaxDb; Q9P0U3; -.
DR PeptideAtlas; Q9P0U3; -.
DR PRIDE; Q9P0U3; -.
DR ProteomicsDB; 83598; -. [Q9P0U3-1]
DR ProteomicsDB; 83599; -. [Q9P0U3-2]
DR Antibodypedia; 1710; 448 antibodies from 38 providers.
DR DNASU; 29843; -.
DR Ensembl; ENST00000448372.5; ENSP00000394791.2; ENSG00000079387.14. [Q9P0U3-1]
DR Ensembl; ENST00000549518.6; ENSP00000447328.1; ENSG00000079387.14. [Q9P0U3-1]
DR Ensembl; ENST00000549595.5; ENSP00000450076.1; ENSG00000079387.14. [Q9P0U3-2]
DR GeneID; 29843; -.
DR KEGG; hsa:29843; -.
DR MANE-Select; ENST00000549518.6; ENSP00000447328.1; NM_001267594.2; NP_001254523.1.
DR UCSC; uc001rqx.5; human. [Q9P0U3-1]
DR CTD; 29843; -.
DR DisGeNET; 29843; -.
DR GeneCards; SENP1; -.
DR HGNC; HGNC:17927; SENP1.
DR HPA; ENSG00000079387; Tissue enhanced (salivary gland, testis).
DR MIM; 612157; gene.
DR neXtProt; NX_Q9P0U3; -.
DR OpenTargets; ENSG00000079387; -.
DR PharmGKB; PA134947038; -.
DR VEuPathDB; HostDB:ENSG00000079387; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000155489; -.
DR HOGENOM; CLU_022541_0_0_1; -.
DR InParanoid; Q9P0U3; -.
DR OMA; MIWESEN; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q9P0U3; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B70; 2681.
DR PathwayCommons; Q9P0U3; -.
DR Reactome; R-HSA-3065679; SUMO is proteolytically processed.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9P0U3; -.
DR SIGNOR; Q9P0U3; -.
DR BioGRID-ORCS; 29843; 24 hits in 1090 CRISPR screens.
DR ChiTaRS; SENP1; human.
DR EvolutionaryTrace; Q9P0U3; -.
DR GeneWiki; SENP1; -.
DR GenomeRNAi; 29843; -.
DR Pharos; Q9P0U3; Tchem.
DR PRO; PR:Q9P0U3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9P0U3; protein.
DR Bgee; ENSG00000079387; Expressed in testis and 151 other tissues.
DR ExpressionAtlas; Q9P0U3; baseline and differential.
DR Genevisible; Q9P0U3; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016929; F:deSUMOylase activity; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; TAS:ProtInc.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; EXP:Reactome.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0016926; P:protein desumoylation; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..644
FT /note="Sentrin-specific protease 1"
FT /id="PRO_0000101716"
FT REGION 1..200
FT /note="Interaction with CCAR2"
FT /evidence="ECO:0000269|PubMed:25406032"
FT REGION 92..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..613
FT /note="Protease"
FT MOTIF 171..177
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:14563852"
FT MOTIF 574..577
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 628..634
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 635..644
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305"
FT ACT_SITE 533
FT ACT_SITE 550
FT ACT_SITE 603
FT /note="Nucleophile"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 593
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10652325"
FT /id="VSP_035777"
FT VARIANT 193
FT /note="I -> V (in dbSNP:rs17854369)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029648"
FT VARIANT 280
FT /note="A -> T (in dbSNP:rs35130318)"
FT /id="VAR_047547"
FT VARIANT 350
FT /note="D -> G (in dbSNP:rs17854368)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029649"
FT MUTAGEN 441
FT /note="D->A: No effect on SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 465
FT /note="W->A: Impairs SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 468
FT /note="D->A: Slightly impairs SUMO2 processing activity. No
FT effect on SUMO2 deconjugating activity."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 496
FT /note="F->A: Impairs SUMO2 processing activity. No effect
FT on SUMO2 deconjugating activity."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 511
FT /note="R->A: Impairs SUMO2 processing activity. No effect
FT on SUMO2 deconjugating activity."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 512
FT /note="W->A: Impairs SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 529
FT /note="H->A: Impairs SUMO2 processing activity. No effect
FT on SUMO2 deconjugating activity."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 532
FT /note="V->A: No effect on SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 533
FT /note="H->A: Abolishes SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 534
FT /note="W->A: Abolishes SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 550
FT /note="D->A: Abolishes SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 597
FT /note="Q->A: Abolishes SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:16553580"
FT MUTAGEN 603
FT /note="C->A,S: Abolishes SUMO2 processing and SUMO2
FT deconjugating activities."
FT /evidence="ECO:0000269|PubMed:14563852,
FT ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:16712526"
FT MUTAGEN 603
FT /note="C->S: Exclusively nuclear. Loss of CCAR2
FT desumoylation."
FT /evidence="ECO:0000269|PubMed:14563852,
FT ECO:0000269|PubMed:16553580, ECO:0000269|PubMed:16712526,
FT ECO:0000269|PubMed:25406032"
FT HELIX 425..434
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 454..458
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 468..481
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2IYD"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:2XPH"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 499..502
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:2XPH"
FT TURN 510..515
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 521..530
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 533..540
FT /evidence="ECO:0007829|PDB:2XPH"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 545..549
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 557..575
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:2XPH"
FT STRAND 591..594
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 624..626
FT /evidence="ECO:0007829|PDB:2XPH"
FT HELIX 627..640
FT /evidence="ECO:0007829|PDB:2XPH"
SQ SEQUENCE 644 AA; 73481 MW; 941951A8B341EC64 CRC64;
MDDIADRMRM DAGEVTLVNH NSVFKTHLLP QTGFPEDQLS LSDQQILSSR QGHLDRSFTC
STRSAAYNPS YYSDNPSSDS FLGSGDLRTF GQSANGQWRN STPSSSSSLQ KSRNSRSLYL
ETRKTSSGLS NSFAGKSNHH CHVSAYEKSF PIKPVPSPSW SGSCRRSLLS PKKTQRRHVS
TAEETVQEEE REIYRQLLQM VTGKQFTIAK PTTHFPLHLS RCLSSSKNTL KDSLFKNGNS
CASQIIGSDT SSSGSASILT NQEQLSHSVY SLSSYTPDVA FGSKDSGTLH HPHHHHSVPH
QPDNLAASNT QSEGSDSVIL LKVKDSQTPT PSSTFFQAEL WIKELTSVYD SRARERLRQI
EEQKALALQL QNQRLQEREH SVHDSVELHL RVPLEKEIPV TVVQETQKKG HKLTDSEDEF
PEITEEMEKE IKNVFRNGNQ DEVLSEAFRL TITRKDIQTL NHLNWLNDEI INFYMNMLME
RSKEKGLPSV HAFNTFFFTK LKTAGYQAVK RWTKKVDVFS VDILLVPIHL GVHWCLAVVD
FRKKNITYYD SMGGINNEAC RILLQYLKQE SIDKKRKEFD TNGWQLFSKK SQEIPQQMNG
SDCGMFACKY ADCITKDRPI NFTQQHMPYF RKRMVWEILH RKLL
