SENP2_HUMAN
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 03-AUG-2022, entry version 188.
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-23667468;
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; 163.
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; Q9HC62; -.
DR PeptideAtlas; Q9HC62; -.
DR PRIDE; Q9HC62; -.
DR ProteomicsDB; 4840; -.
DR ProteomicsDB; 81643; -. [Q9HC62-1]
DR Antibodypedia; 33840; 768 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 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; PGMYRWL; -.
DR OrthoDB; 1480705at2759; -.
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 BioGRID-ORCS; 59343; 20 hits in 1082 CRISPR screens.
DR ChiTaRS; SENP2; human.
DR EvolutionaryTrace; Q9HC62; -.
DR GeneWiki; SENP2; -.
DR GenomeRNAi; 59343; -.
DR Pharos; Q9HC62; Tbio.
DR PRO; PR:Q9HC62; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HC62; protein.
DR Bgee; ENSG00000163904; Expressed in calcaneal tendon and 183 other tissues.
DR ExpressionAtlas; Q9HC62; baseline and differential.
DR Genevisible; Q9HC62; HS.
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:0015031; P:protein transport; 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 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; 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
