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Sentrin-specific protease 5 (EC 3.4.22.68) (Sentrin/SUMO-specific protease SENP5)

 SENP5_HUMAN             Reviewed;         755 AA.
Q96HI0; B4DY82; Q96SA5;
28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 129.
RecName: Full=Sentrin-specific protease 5;
EC=3.4.22.-;
AltName: Full=Sentrin/SUMO-specific protease SENP5;
Name=SENP5; ORFNames=FKSG45;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 305-755 (ISOFORM 1).
Wang Y.-G., Li T.;
"Identification of FKSG45, a novel gene located on human chromosome
3.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[5]
REVIEW.
PubMed=10806345; DOI=10.1016/S0378-1119(00)00139-6;
Yeh E.T.H., Gong L., Kamitani T.;
"Ubiquitin-like proteins: new wines in new bottles.";
Gene 248:1-14(2000).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-713.
PubMed=16608850; DOI=10.1074/jbc.M511658200;
Gong L., Yeh E.T.H.;
"Characterization of a family of nucleolar SUMO-specific proteases
with preference for SUMO-2 or SUMO-3.";
J. Biol. Chem. 281:15869-15877(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-713.
PubMed=16738315; DOI=10.1128/MCB.02301-05;
Di Bacco A., Ouyang J., Lee H.-Y., Catic A., Ploegh H., Gill G.;
"The SUMO-specific protease SENP5 is required for cell division.";
Mol. Cell. Biol. 26:4489-4498(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[9]
INTERACTION WITH CCAR2.
PubMed=25406032; DOI=10.1038/ncomms6483;
Park J.H., Lee S.W., Yang S.W., Yoo H.M., Park J.M., Seong M.W.,
Ka S.H., Oh K.H., Jeon Y.J., Chung C.H.;
"Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis
in response to DNA damage.";
Nat. Commun. 5:5483-5483(2014).
-!- FUNCTION: Protease that catalyzes two essential functions in the
SUMO pathway: processing of full-length SUMO3 to its mature form
and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has
weak proteolytic activity against full-length SUMO1 or SUMO1
conjugates. Required for cell division.
{ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:16738315}.
-!- SUBUNIT: Interacts with CCAR2. {ECO:0000269|PubMed:25406032}.
-!- INTERACTION:
P03372:ESR1; NbExp=2; IntAct=EBI-3895753, EBI-78473;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:16608850, ECO:0000269|PubMed:16738315}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96HI0-1; Sequence=Displayed;
Name=2;
IsoId=Q96HI0-2; Sequence=VSP_056415;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK69630.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK302305; BAG63644.1; -; mRNA.
EMBL; AC011322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008589; AAH08589.1; -; mRNA.
EMBL; BC030705; AAH30705.1; -; mRNA.
EMBL; AF335474; AAK69630.1; ALT_INIT; mRNA.
CCDS; CCDS3322.1; -. [Q96HI0-1]
CCDS; CCDS77876.1; -. [Q96HI0-2]
RefSeq; NP_001294974.1; NM_001308045.1. [Q96HI0-2]
RefSeq; NP_689912.2; NM_152699.4. [Q96HI0-1]
RefSeq; XP_011510846.1; XM_011512544.2. [Q96HI0-1]
RefSeq; XP_016861359.1; XM_017005870.1. [Q96HI0-2]
UniGene; Hs.240770; -.
ProteinModelPortal; Q96HI0; -.
SMR; Q96HI0; -.
BioGrid; 128497; 23.
DIP; DIP-62043N; -.
IntAct; Q96HI0; 2.
STRING; 9606.ENSP00000327197; -.
MEROPS; C48.008; -.
iPTMnet; Q96HI0; -.
PhosphoSitePlus; Q96HI0; -.
BioMuta; SENP5; -.
DMDM; 296452962; -.
EPD; Q96HI0; -.
MaxQB; Q96HI0; -.
PaxDb; Q96HI0; -.
PeptideAtlas; Q96HI0; -.
PRIDE; Q96HI0; -.
DNASU; 205564; -.
Ensembl; ENST00000323460; ENSP00000327197; ENSG00000119231. [Q96HI0-1]
Ensembl; ENST00000445299; ENSP00000390231; ENSG00000119231. [Q96HI0-2]
GeneID; 205564; -.
KEGG; hsa:205564; -.
UCSC; uc003fwz.5; human. [Q96HI0-1]
CTD; 205564; -.
DisGeNET; 205564; -.
EuPathDB; HostDB:ENSG00000119231.10; -.
GeneCards; SENP5; -.
H-InvDB; HIX0018042; -.
HGNC; HGNC:28407; SENP5.
MIM; 612845; gene.
neXtProt; NX_Q96HI0; -.
OpenTargets; ENSG00000119231; -.
PharmGKB; PA134917083; -.
eggNOG; KOG0778; Eukaryota.
eggNOG; COG5160; LUCA.
GeneTree; ENSGT00530000062941; -.
HOGENOM; HOG000070166; -.
HOVERGEN; HBG062231; -.
InParanoid; Q96HI0; -.
KO; K08594; -.
OMA; WRKGIHL; -.
OrthoDB; EOG091G092N; -.
PhylomeDB; Q96HI0; -.
TreeFam; TF316289; -.
BRENDA; 3.4.22.B73; 2681.
Reactome; R-HSA-3065679; SUMO is proteolytically processed.
ChiTaRS; SENP5; human.
GenomeRNAi; 205564; -.
PRO; PR:Q96HI0; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000119231; -.
CleanEx; HS_SENP5; -.
ExpressionAtlas; Q96HI0; baseline and differential.
Genevisible; Q96HI0; HS.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0070139; F:SUMO-specific endopeptidase activity; EXP:Reactome.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
GO; GO:0016925; P:protein sumoylation; TAS:Reactome.
InterPro; IPR003653; Peptidase_C48_C.
InterPro; IPR033465; SENP5.
PANTHER; PTHR12606:SF10; PTHR12606:SF10; 1.
Pfam; PF02902; Peptidase_C48; 1.
PROSITE; PS50600; ULP_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Complete proteome;
Hydrolase; Nucleus; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation pathway.
CHAIN 1 755 Sentrin-specific protease 5.
/FTId=PRO_0000101723.
REGION 567 724 Protease.
ACT_SITE 646 646 {ECO:0000250}.
ACT_SITE 663 663 {ECO:0000250}.
ACT_SITE 713 713 {ECO:0000305}.
VAR_SEQ 629 674 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056415.
VARIANT 83 83 N -> S (in dbSNP:rs35434690).
/FTId=VAR_057045.
VARIANT 340 340 L -> F (in dbSNP:rs34251880).
/FTId=VAR_061732.
MUTAGEN 713 713 C->A: Abolishes enzymatic activity.
{ECO:0000269|PubMed:16608850,
ECO:0000269|PubMed:16738315}.
CONFLICT 75 75 P -> H (in Ref. 3; AAH30705).
{ECO:0000305}.
CONFLICT 538 538 S -> C (in Ref. 4; AAK69630).
{ECO:0000305}.
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


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