ID   SENP2_HUMAN             Reviewed;         589 AA.
AC   Q9HC62; B4DQ42; Q8IW97; Q96SR2; Q9P2L5;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Sentrin-specific protease 2 {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:21965678};
DE   AltName: Full=Axam2 {ECO:0000250|UniProtKB:Q91ZX6};
DE   AltName: Full=SMT3-specific isopeptidase 2 {ECO:0000250|UniProtKB:Q91ZX6};
DE            Short=Smt3ip2 {ECO:0000250|UniProtKB:Q91ZX6};
DE   AltName: Full=Sentrin/SUMO-specific protease SENP2 {ECO:0000303|Ref.1};
GN   Name=SENP2 {ECO:0000303|PubMed:10718198, ECO:0000312|HGNC:HGNC:23116};
GN   Synonyms=KIAA1331 {ECO:0000303|PubMed:10718198};
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), AND VARIANT LYS-301.
RA   Gong L., Yeh E.T.H.;
RT   "Cloning of SENP2, a novel member of sentrin-specific protease family.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-301.
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   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   LYS-301.
RC   TISSUE=Teratocarcinoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-589 (ISOFORM 1), AND VARIANT
RP   LYS-301.
RC   TISSUE=Melanoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NUP153, AND TOPOLOGY.
RC   TISSUE=Fetal brain;
RX   PubMed=12192048; DOI=10.1128/mcb.22.18.6498-6508.2002;
RA   Zhang H., Saitoh H., Matunis M.J.;
RT   "Enzymes of the SUMO modification pathway localize to filaments of the
RT   nuclear pore complex.";
RL   Mol. Cell. Biol. 22:6498-6508(2002).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NUP153.
RX   PubMed=11896061; DOI=10.1074/jbc.m201799200;
RA   Hang J., Dasso M.;
RT   "Association of the human SUMO-1 protease SENP2 with the nuclear pore.";
RL   J. Biol. Chem. 277:19961-19966(2002).
RN   [10]
RP   NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT SIGNAL, SUBCELLULAR LOCATION,
RP   AND UBIQUITINATION.
RX   PubMed=16738331; DOI=10.1128/mcb.01830-05;
RA   Itahana Y., Yeh E.T.H., Zhang Y.;
RT   "Nucleocytoplasmic shuttling modulates activity and ubiquitination-
RT   dependent turnover of SUMO-specific protease 2.";
RL   Mol. Cell. Biol. 26:4675-4689(2006).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   FUNCTION, AND MUTAGENESIS OF CYS-548 AND 576-ARG-LYS-577.
RX   PubMed=20194620; DOI=10.1128/mcb.00852-09;
RA   Chung S.S., Ahn B.Y., Kim M., Choi H.H., Park H.S., Kang S., Park S.G.,
RA   Kim Y.B., Cho Y.M., Lee H.K., Chung C.H., Park K.S.;
RT   "Control of adipogenesis by the SUMO-specific protease SENP2.";
RL   Mol. Cell. Biol. 30:2135-2146(2010).
RN   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-333 AND SER-344, AND
RP   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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, 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   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 364-589, X-RAY CRYSTALLOGRAPHY
RP   (2.8 ANGSTROMS) OF 364-589 IN COMPLEX WITH SUMO1, FUNCTION, ACTIVE SITE,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=15296745; DOI=10.1016/j.str.2004.05.023;
RA   Reverter D., Lima C.D.;
RT   "A basis for SUMO protease specificity provided by analysis of human Senp2
RT   and a Senp2-SUMO complex.";
RL   Structure 12:1519-1531(2004).
CC   -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC       pathway (PubMed:11896061, PubMed:12192048, PubMed:20194620,
CC       PubMed:21965678, PubMed:15296745). The first is the hydrolysis of an
CC       alpha-linked peptide bond at the C-terminal end of the small ubiquitin-
CC       like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the
CC       mature form of the proteins (PubMed:15296745). 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 (PubMed:20194620, PubMed:21965678, PubMed:15296745). May down-
CC       regulate CTNNB1 levels and thereby modulate the Wnt pathway (By
CC       similarity). Deconjugates SUMO2 from MTA1 (PubMed:21965678). Plays a
CC       dynamic role in adipogenesis by desumoylating and promoting the
CC       stabilization of CEBPB (PubMed:20194620). Acts as a regulator of the
CC       cGAS-STING pathway by catalyzing desumoylation of CGAS and STING1
CC       during the late phase of viral infection (By similarity).
CC       {ECO:0000250|UniProtKB:Q91ZX6, ECO:0000269|PubMed:11896061,
CC       ECO:0000269|PubMed:12192048, ECO:0000269|PubMed:15296745,
CC       ECO:0000269|PubMed:20194620, ECO:0000269|PubMed:21965678}.
CC   -!- SUBUNIT: Binds to SUMO2 and SUMO3 (PubMed:15296745). Interacts with the
CC       C-terminal domain of NUP153 via its N-terminus (PubMed:11896061,
CC       PubMed:12192048). Interacts with MTA1 (PubMed:21965678).
CC       {ECO:0000269|PubMed:11896061, ECO:0000269|PubMed:12192048,
CC       ECO:0000269|PubMed:15296745, ECO:0000269|PubMed:21965678}.
CC   -!- INTERACTION:
CC       Q9HC62; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-714881, EBI-2876502;
CC       Q9HC62; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-714881, EBI-741181;
CC       Q9HC62; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-714881, EBI-11522760;
CC       Q9HC62; P55056: APOC4; NbExp=3; IntAct=EBI-714881, EBI-18302142;
CC       Q9HC62; Q15041: ARL6IP1; NbExp=3; IntAct=EBI-714881, EBI-714543;
CC       Q9HC62; Q5T9G4-2: ARMC12; NbExp=3; IntAct=EBI-714881, EBI-36513937;
CC       Q9HC62; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-714881, EBI-3059266;
CC       Q9HC62; P53701: HCCS; NbExp=3; IntAct=EBI-714881, EBI-10763431;
CC       Q9HC62; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-714881, EBI-81279;
CC       Q9HC62; Q8N6L0: KASH5; NbExp=6; IntAct=EBI-714881, EBI-749265;
CC       Q9HC62; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-714881, EBI-10192441;
CC       Q9HC62; Q9NS64: RPRM; NbExp=3; IntAct=EBI-714881, EBI-1052363;
CC       Q9HC62; Q8N3Y7: SDR16C5; NbExp=3; IntAct=EBI-714881, EBI-3923480;
CC       Q9HC62; P63165: SUMO1; NbExp=2; IntAct=EBI-714881, EBI-80140;
CC       Q9HC62; P61956: SUMO2; NbExp=5; IntAct=EBI-714881, EBI-473220;
CC       Q9HC62; P55854: SUMO3; NbExp=6; IntAct=EBI-714881, EBI-474067;
CC       Q9HC62; Q8N205: SYNE4; NbExp=3; IntAct=EBI-714881, EBI-7131783;
CC       Q9HC62; Q8WW34: TMEM239; NbExp=3; IntAct=EBI-714881, EBI-9675724;
CC       Q9HC62; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-714881, EBI-11528917;
CC       Q9HC62; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-714881, EBI-1044859;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC       {ECO:0000269|PubMed:12192048}. Nucleus membrane
CC       {ECO:0000269|PubMed:12192048}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12192048}; Nucleoplasmic side
CC       {ECO:0000269|PubMed:12192048}. Cytoplasm {ECO:0000269|PubMed:16738331}.
CC       Note=Shuttles between cytoplasm and nucleus.
CC       {ECO:0000269|PubMed:16738331}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HC62-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HC62-2; Sequence=VSP_056697;
CC   -!- DOMAIN: The N-terminus is necessary and sufficient for nuclear envelope
CC       targeting. {ECO:0000269|PubMed:12192048}.
CC   -!- PTM: Polyubiquitinated; which leads to proteasomal degradation.
CC       {ECO:0000269|PubMed:16738331}.
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; AF151697; AAG15309.2; -; mRNA.
DR   EMBL; AB037752; BAA92569.2; -; mRNA.
DR   EMBL; AK027599; BAB55222.1; -; mRNA.
DR   EMBL; AK298628; BAG60804.1; -; mRNA.
DR   EMBL; AC016961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040609; AAH40609.1; -; mRNA.
DR   EMBL; AL834380; CAD39043.1; -; mRNA.
DR   CCDS; CCDS33902.1; -. [Q9HC62-1]
DR   RefSeq; NP_067640.2; NM_021627.2. [Q9HC62-1]
DR   PDB; 1TGZ; X-ray; 2.80 A; A=364-589.
DR   PDB; 1TH0; X-ray; 2.20 A; A/B=364-589.
DR   PDB; 2IO0; X-ray; 2.30 A; A=364-589.
DR   PDB; 2IO1; X-ray; 2.60 A; A/C/E=364-589.
DR   PDB; 2IO2; X-ray; 2.90 A; A=364-589.
DR   PDB; 2IO3; X-ray; 3.20 A; A=364-589.
DR   PDB; 3ZO5; X-ray; 2.15 A; A=363-589.
DR   PDB; 5AEK; X-ray; 3.00 A; A/C/E/G/I/K/M/O/Q/S/U/W=366-589.
DR   PDBsum; 1TGZ; -.
DR   PDBsum; 1TH0; -.
DR   PDBsum; 2IO0; -.
DR   PDBsum; 2IO1; -.
DR   PDBsum; 2IO2; -.
DR   PDBsum; 2IO3; -.
DR   PDBsum; 3ZO5; -.
DR   PDBsum; 5AEK; -.
DR   AlphaFoldDB; Q9HC62; -.
DR   SMR; Q9HC62; -.
DR   BioGRID; 121885; 176.
DR   DIP; DIP-29254N; -.
DR   IntAct; Q9HC62; 42.
DR   MINT; Q9HC62; -.
DR   STRING; 9606.ENSP00000296257; -.
DR   BindingDB; Q9HC62; -.
DR   ChEMBL; CHEMBL2176776; -.
DR   MEROPS; C48.007; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   iPTMnet; Q9HC62; -.
DR   PhosphoSitePlus; Q9HC62; -.
DR   BioMuta; SENP2; -.
DR   DMDM; 143811458; -.
DR   EPD; Q9HC62; -.
DR   jPOST; Q9HC62; -.
DR   MassIVE; Q9HC62; -.
DR   MaxQB; Q9HC62; -.
DR   PaxDb; 9606-ENSP00000296257; -.
DR   PeptideAtlas; Q9HC62; -.
DR   ProteomicsDB; 4840; -.
DR   ProteomicsDB; 81643; -. [Q9HC62-1]
DR   Pumba; Q9HC62; -.
DR   Antibodypedia; 33840; 865 antibodies from 35 providers.
DR   DNASU; 59343; -.
DR   Ensembl; ENST00000296257.10; ENSP00000296257.5; ENSG00000163904.13. [Q9HC62-1]
DR   GeneID; 59343; -.
DR   KEGG; hsa:59343; -.
DR   MANE-Select; ENST00000296257.10; ENSP00000296257.5; NM_021627.3; NP_067640.2.
DR   UCSC; uc003fpn.4; human. [Q9HC62-1]
DR   AGR; HGNC:23116; -.
DR   CTD; 59343; -.
DR   DisGeNET; 59343; -.
DR   GeneCards; SENP2; -.
DR   HGNC; HGNC:23116; SENP2.
DR   HPA; ENSG00000163904; Low tissue specificity.
DR   MIM; 608261; gene.
DR   neXtProt; NX_Q9HC62; -.
DR   OpenTargets; ENSG00000163904; -.
DR   PharmGKB; PA134955185; -.
DR   VEuPathDB; HostDB:ENSG00000163904; -.
DR   eggNOG; KOG0778; Eukaryota.
DR   GeneTree; ENSGT00940000154951; -.
DR   HOGENOM; CLU_024324_4_0_1; -.
DR   InParanoid; Q9HC62; -.
DR   OMA; CHWLNDE; -.
DR   OrthoDB; 1068193at2759; -.
DR   PhylomeDB; Q9HC62; -.
DR   TreeFam; TF316289; -.
DR   BRENDA; 3.4.22.B71; 2681.
DR   PathwayCommons; Q9HC62; -.
DR   Reactome; R-HSA-3065679; SUMO is proteolytically processed.
DR   SignaLink; Q9HC62; -.
DR   SIGNOR; Q9HC62; -.
DR   BioGRID-ORCS; 59343; 20 hits in 1160 CRISPR screens.
DR   ChiTaRS; SENP2; human.
DR   EvolutionaryTrace; Q9HC62; -.
DR   GeneWiki; SENP2; -.
DR   GenomeRNAi; 59343; -.
DR   Pharos; Q9HC62; Tchem.
DR   PRO; PR:Q9HC62; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9HC62; Protein.
DR   Bgee; ENSG00000163904; Expressed in calcaneal tendon and 185 other cell types or tissues.
DR   ExpressionAtlas; Q9HC62; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016929; F:deSUMOylase activity; IBA:GO_Central.
DR   GO; GO:0070139; F:SUMO-specific endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:CACAO.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:CACAO.
DR   GO; GO:0031648; P:protein destabilization; IMP:CACAO.
DR   GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003653; Peptidase_C48_C.
DR   PANTHER; PTHR12606:SF11; SENTRIN-SPECIFIC PROTEASE 2; 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; Q9HC62; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Membrane;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Protease;
KW   Protein transport; Reference proteome; Thiol protease; Translocation;
KW   Transport; Ubl conjugation; Ubl conjugation pathway; Wnt signaling pathway.
FT   CHAIN           1..589
FT                   /note="Sentrin-specific protease 2"
FT                   /id="PRO_0000101718"
FT   REGION          155..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..560
FT                   /note="Protease"
FT                   /evidence="ECO:0000269|PubMed:15296745"
FT   MOTIF           28..31
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:16738331"
FT   MOTIF           46..51
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:16738331"
FT   MOTIF           317..332
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000269|PubMed:16738331"
FT   ACT_SITE        478
FT                   /evidence="ECO:0000269|PubMed:15296745"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000269|PubMed:15296745"
FT   ACT_SITE        548
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:15296745"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         333
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..33
FT                   /note="MYRWLVRILGTIFRFCDRSVPPARALLKRRRSD -> MDSHPCLYCGPQDSE
FT                   GTNWQTSP (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056697"
FT   VARIANT         301
FT                   /note="T -> K (in dbSNP:rs6762208)"
FT                   /evidence="ECO:0000269|PubMed:10718198,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|Ref.1"
FT                   /id="VAR_029650"
FT   MUTAGEN         548
FT                   /note="C->S: Does not desumoylate CEBPB."
FT                   /evidence="ECO:0000269|PubMed:20194620"
FT   MUTAGEN         576..577
FT                   /note="RK->LM: Does not desumoylate CEBPB."
FT                   /evidence="ECO:0000269|PubMed:20194620"
FT   CONFLICT        39
FT                   /note="T -> TA (in Ref. 1; AAG15309)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        403
FT                   /note="Q -> H (in Ref. 4; BAB55222)"
FT                   /evidence="ECO:0000305"
FT   HELIX           370..380
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          381..383
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          388..392
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          396..398
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           399..402
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           403..405
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           413..430
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          435..437
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           442..454
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           455..458
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           463..465
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          466..474
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          479..485
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   TURN            486..489
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          490..494
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   STRAND          496..498
FT                   /evidence="ECO:0007829|PDB:2IO3"
FT   HELIX           502..520
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           526..528
FT                   /evidence="ECO:0007829|PDB:1TH0"
FT   STRAND          530..533
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   TURN            536..538
FT                   /evidence="ECO:0007829|PDB:1TH0"
FT   TURN            543..546
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           548..560
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           569..571
FT                   /evidence="ECO:0007829|PDB:3ZO5"
FT   HELIX           572..585
FT                   /evidence="ECO:0007829|PDB:3ZO5"
SQ   SEQUENCE   589 AA;  67855 MW;  712707DCC2C5431C CRC64;
     MYRWLVRILG TIFRFCDRSV PPARALLKRR RSDSTLFSTV DTDEIPAKRP RLDCFIHQVK
     NSLYNAASLF GFPFQLTTKP MVTSACNGTR NVAPSGEVFS NSSSCELTGS GSWNNMLKLG
     NKSPNGISDY PKIRVTVTRD QPRRVLPSFG FTLNSEGCNR RPGGRRHSKG NPESSLMWKP
     QEQAVTEMIS EESGKGLRRP HCTVEEGVQK EEREKYRKLL ERLKESGHGN SVCPVTSNYH
     SSQRSQMDTL KTKGWGEEQN HGVKTTQFVP KQYRLVETRG PLCSLRSEKR CSKGKITDTE
     TMVGIRFENE SRRGYQLEPD LSEEVSARLR LGSGSNGLLR RKVSIIETKE KNCSGKERDR
     RTDDLLELTE DMEKEISNAL GHGPQDEILS SAFKLRITRG DIQTLKNYHW LNDEVINFYM
     NLLVERNKKQ GYPALHVFST FFYPKLKSGG YQAVKRWTKG VNLFEQEIIL VPIHRKVHWS
     LVVIDLRKKC LKYLDSMGQK GHRICEILLQ YLQDESKTKR NSDLNLLEWT HHSMKPHEIP
     QQLNGSDCGM FTCKYADYIS RDKPITFTQH QMPLFRKKMV WEILHQQLL
//