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 27-MAR-2024, entry version 189. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 132. DR DIP; DIP-29252N; -. DR IntAct; Q9P0U3; 34. 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 SwissPalm; Q9P0U3; -. DR BioMuta; SENP1; -. DR DMDM; 215273882; -. DR EPD; Q9P0U3; -. DR jPOST; Q9P0U3; -. DR MassIVE; Q9P0U3; -. DR MaxQB; Q9P0U3; -. DR PaxDb; 9606-ENSP00000394791; -. DR PeptideAtlas; Q9P0U3; -. DR ProteomicsDB; 83598; -. [Q9P0U3-1] DR ProteomicsDB; 83599; -. [Q9P0U3-2] DR Pumba; Q9P0U3; -. DR Antibodypedia; 1710; 501 antibodies from 38 providers. DR DNASU; 29843; -. DR Ensembl; ENST00000448372.6; ENSP00000394791.2; ENSG00000079387.15. [Q9P0U3-1] DR Ensembl; ENST00000549518.6; ENSP00000447328.1; ENSG00000079387.15. [Q9P0U3-1] DR Ensembl; ENST00000549595.5; ENSP00000450076.1; ENSG00000079387.15. [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 AGR; HGNC:17927; -. 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; FPEITEX; -. DR OrthoDB; 1068193at2759; -. 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; 29 hits in 1170 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 153 other cell types or tissues. DR ExpressionAtlas; Q9P0U3; baseline and differential. 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; IDA:UniProtKB. 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:0016925; P:protein sumoylation; TAS:Reactome. DR GO; GO:0006508; P:proteolysis; TAS:ProtInc. DR GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProt. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR003653; Peptidase_C48_C. DR PANTHER; PTHR12606:SF30; SENTRIN-SPECIFIC PROTEASE 1; 1. DR PANTHER; PTHR12606; SENTRIN/SUMO-SPECIFIC PROTEASE; 1. DR Pfam; PF02902; Peptidase_C48; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS50600; ULP_PROTEASE; 1. DR Genevisible; Q9P0U3; HS. 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 //