SENP5_HUMAN
ID SENP5_HUMAN Reviewed; 755 AA.
AC Q96HI0; B4DY82; Q96SA5;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sentrin-specific protease 5;
DE EC=3.4.22.-;
DE AltName: Full=Sentrin/SUMO-specific protease SENP5;
GN Name=SENP5; ORFNames=FKSG45;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, and 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 305-755 (ISOFORM 1).
RA Wang Y.-G., Li T.;
RT "Identification of FKSG45, a novel gene located on human chromosome 3.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP REVIEW.
RX PubMed=10806345; DOI=10.1016/s0378-1119(00)00139-6;
RA Yeh E.T.H., Gong L., Kamitani T.;
RT "Ubiquitin-like proteins: new wines in new bottles.";
RL Gene 248:1-14(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-713.
RX PubMed=16608850; DOI=10.1074/jbc.m511658200;
RA Gong L., Yeh E.T.H.;
RT "Characterization of a family of nucleolar SUMO-specific proteases with
RT preference for SUMO-2 or SUMO-3.";
RL J. Biol. Chem. 281:15869-15877(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-713.
RX PubMed=16738315; DOI=10.1128/mcb.02301-05;
RA Di Bacco A., Ouyang J., Lee H.-Y., Catic A., Ploegh H., Gill G.;
RT "The SUMO-specific protease SENP5 is required for cell division.";
RL Mol. Cell. Biol. 26:4489-4498(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP INTERACTION WITH CCAR2.
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).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway: processing of full-length SUMO3 to its mature form and
CC deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak
CC proteolytic activity against full-length SUMO1 or SUMO1 conjugates.
CC Required for cell division. {ECO:0000269|PubMed:16608850,
CC ECO:0000269|PubMed:16738315}.
CC -!- SUBUNIT: Interacts with CCAR2. {ECO:0000269|PubMed:25406032}.
CC -!- INTERACTION:
CC Q96HI0; P03372: ESR1; NbExp=2; IntAct=EBI-3895753, EBI-78473;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16608850,
CC ECO:0000269|PubMed:16738315}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96HI0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HI0-2; Sequence=VSP_056415;
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK69630.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK302305; BAG63644.1; -; mRNA.
DR EMBL; AC011322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC127904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008589; AAH08589.1; -; mRNA.
DR EMBL; BC030705; AAH30705.1; -; mRNA.
DR EMBL; AF335474; AAK69630.1; ALT_INIT; mRNA.
DR CCDS; CCDS3322.1; -. [Q96HI0-1]
DR CCDS; CCDS77876.1; -. [Q96HI0-2]
DR RefSeq; NP_001294974.1; NM_001308045.1. [Q96HI0-2]
DR RefSeq; NP_689912.2; NM_152699.4. [Q96HI0-1]
DR RefSeq; XP_011510846.1; XM_011512544.2. [Q96HI0-1]
DR RefSeq; XP_016861359.1; XM_017005870.1.
DR AlphaFoldDB; Q96HI0; -.
DR SMR; Q96HI0; -.
DR BioGRID; 128497; 61.
DR DIP; DIP-62043N; -.
DR IntAct; Q96HI0; 15.
DR STRING; 9606.ENSP00000327197; -.
DR BindingDB; Q96HI0; -.
DR ChEMBL; CHEMBL4802012; -.
DR MEROPS; C48.008; -.
DR iPTMnet; Q96HI0; -.
DR PhosphoSitePlus; Q96HI0; -.
DR BioMuta; SENP5; -.
DR DMDM; 296452962; -.
DR EPD; Q96HI0; -.
DR jPOST; Q96HI0; -.
DR MassIVE; Q96HI0; -.
DR MaxQB; Q96HI0; -.
DR PaxDb; Q96HI0; -.
DR PeptideAtlas; Q96HI0; -.
DR PRIDE; Q96HI0; -.
DR ProteomicsDB; 5507; -.
DR ProteomicsDB; 76753; -. [Q96HI0-1]
DR Antibodypedia; 33951; 334 antibodies from 31 providers.
DR DNASU; 205564; -.
DR Ensembl; ENST00000323460.10; ENSP00000327197.5; ENSG00000119231.11. [Q96HI0-1]
DR Ensembl; ENST00000445299.6; ENSP00000390231.2; ENSG00000119231.11. [Q96HI0-2]
DR GeneID; 205564; -.
DR KEGG; hsa:205564; -.
DR MANE-Select; ENST00000323460.10; ENSP00000327197.5; NM_152699.5; NP_689912.2.
DR UCSC; uc003fwz.5; human. [Q96HI0-1]
DR CTD; 205564; -.
DR DisGeNET; 205564; -.
DR GeneCards; SENP5; -.
DR HGNC; HGNC:28407; SENP5.
DR HPA; ENSG00000119231; Low tissue specificity.
DR MIM; 612845; gene.
DR neXtProt; NX_Q96HI0; -.
DR OpenTargets; ENSG00000119231; -.
DR PharmGKB; PA134917083; -.
DR VEuPathDB; HostDB:ENSG00000119231; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000159865; -.
DR HOGENOM; CLU_021414_1_0_1; -.
DR InParanoid; Q96HI0; -.
DR OMA; QLRHFQC; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q96HI0; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B73; 2681.
DR PathwayCommons; Q96HI0; -.
DR Reactome; R-HSA-3065679; SUMO is proteolytically processed.
DR SignaLink; Q96HI0; -.
DR BioGRID-ORCS; 205564; 10 hits in 1083 CRISPR screens.
DR ChiTaRS; SENP5; human.
DR GenomeRNAi; 205564; -.
DR Pharos; Q96HI0; Tbio.
DR PRO; PR:Q96HI0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96HI0; protein.
DR Bgee; ENSG00000119231; Expressed in tendon of biceps brachii and 190 other tissues.
DR ExpressionAtlas; Q96HI0; baseline and differential.
DR Genevisible; Q96HI0; HS.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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; EXP:Reactome.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR045577; SENP3_5_cons_dom.
DR InterPro; IPR033465; SENP5.
DR PANTHER; PTHR12606:SF10; PTHR12606:SF10; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF19722; SENP3_5_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Hydrolase; Nucleus;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..755
FT /note="Sentrin-specific protease 5"
FT /id="PRO_0000101723"
FT REGION 268..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..724
FT /note="Protease"
FT ACT_SITE 646
FT /evidence="ECO:0000250"
FT ACT_SITE 663
FT /evidence="ECO:0000250"
FT ACT_SITE 713
FT /evidence="ECO:0000305"
FT VAR_SEQ 629..674
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056415"
FT VARIANT 83
FT /note="N -> S (in dbSNP:rs35434690)"
FT /id="VAR_057045"
FT VARIANT 340
FT /note="L -> F (in dbSNP:rs34251880)"
FT /id="VAR_061732"
FT MUTAGEN 713
FT /note="C->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16608850,
FT ECO:0000269|PubMed:16738315"
FT CONFLICT 75
FT /note="P -> H (in Ref. 3; AAH30705)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> C (in Ref. 4; AAK69630)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 86693 MW; 90D7B34B2853CEE4 CRC64;
MKKQRKILWR KGIHLAFSEK WNTGFGGFKK FYFHQHLCIL KAKLGRPVTW NRQLRHFQGR
KKALQIQKTW IKDEPLCAKT KFNVATQNVS TLSSKVKRKD AKHFISSSKT LLRLQAEKLL
SSAKNSDHEY CREKNLLKAV TDFPSNSALG QANGHRPRTD PQPSDFPMKF NGESQSPGES
GTIVVTLNNH KRKGFCYGCC QGPEHHRNGG PLIPKKFQLN QHRRIKLSPL MMYEKLSMIR
FRYRILRSQH FRTKSKVCKL RKAQRSWVQK VTGDHQETRR ENGEGGSCSP FPSPEPKDPS
CRHQPYFPDM DSSAVVKGTN SHVPDCHTKG SSFLGKELSL DEAFPDQQNG SATNAWDQSS
CSSPKWECTE LIHDIPLPEH RSNTMFISET EREIMTLGQE NQTSSVSDDR VKLSVSGADT
SVSSVDGPVS QKAVQNENSY QMEEDGSLKQ SILSSELLDH PYCKSPLEAP LVCSGLKLEN
QVGGGKNSQK ASPVDDEQLS VCLSGFLDEV MKKYGSLVPL SEKEVLGRLK DVFNEDFSNR
KPFINREITN YRARHQKCNF RIFYNKHMLD MDDLATLDGQ NWLNDQVINM YGELIMDAVP
DKVHFFNSFF HRQLVTKGYN GVKRWTKKVD LFKKSLLLIP IHLEVHWSLI TVTLSNRIIS
FYDSQGIHFK FCVENIRKYL LTEAREKNRP EFLQGWQTAV TKCIPQQKND SDCGVFVLQY
CKCLALEQPF QFSQEDMPRV RKRIYKELCE CRLMD
