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Sentrin-specific protease 6 (EC 3.4.22.68) (SUMO-1-specific protease 1) (Sentrin/SUMO-specific protease SENP6)

 SENP6_HUMAN             Reviewed;        1112 AA.
Q9GZR1; A6NNY9; O94891; Q5VUL3; Q5VUL4; Q8TBY4; Q9UJV5;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 2.
25-OCT-2017, entry version 153.
RecName: Full=Sentrin-specific protease 6;
EC=3.4.22.- {ECO:0000269|PubMed:18799455};
AltName: Full=SUMO-1-specific protease 1;
AltName: Full=Sentrin/SUMO-specific protease SENP6;
Name=SENP6; Synonyms=KIAA0797, SSP1, SUSP1; ORFNames=FKSG6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-121 AND CYS-1106,
AND CHARACTERIZATION.
TISSUE=Brain;
PubMed=10799485; DOI=10.1074/jbc.275.19.14102;
Kim K.I., Baek S.H., Jeon Y.-J., Nishimori S., Suzuki T., Uchida S.,
Shimbara N., Saitoh H., Tanaka K., Chung C.H.;
"A new SUMO-1-specific protease, SUSP1, that is highly expressed in
reproductive organs.";
J. Biol. Chem. 275:14102-14106(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang Y.-G.;
"Identification of FKSG6, a novel protein with protease activity.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
MET-121 AND CYS-1106.
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[5]
SEQUENCE REVISION.
Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692 (ISOFORM 2).
TISSUE=Tongue;
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).
[10]
INTERACTION WITH RXRA, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS
OF CYS-1030.
PubMed=16912044; DOI=10.1074/jbc.M604033200;
Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S.,
Seol J.H., Baek S.H., Bang O.S., Chung C.H.;
"Negative modulation of RXRalpha transcriptional activity by small
ubiquitin-related modifier (SUMO) modification and its reversal by
SUMO-specific protease SUSP1.";
J. Biol. Chem. 281:30669-30677(2006).
[11]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17000875; DOI=10.1083/jcb.200510103;
Mukhopadhyay D., Ayaydin F., Kolli N., Tan S.-H., Anan T.,
Kametaka A., Azuma Y., Wilkinson K.D., Dasso M.;
"SUSP1 antagonizes formation of highly SUMO2/3-conjugated species.";
J. Cell Biol. 174:939-949(2006).
[12]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18799455; DOI=10.1074/jbc.M805655200;
Lima C.D., Reverter D.;
"Structure of the human SENP7 catalytic domain and poly-SUMO
deconjugation activities for SENP6 and SENP7.";
J. Biol. Chem. 283:32045-32055(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION OF
KAT5-UBE2I-SENP6 COMPLEX.
PubMed=17704809; DOI=10.1038/sj.onc.1210710;
Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z.,
Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M.,
Liang S., Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.;
"Functional characterization of TIP60 sumoylation in UV-irradiated DNA
damage response.";
Oncogene 27:931-941(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-350
AND SER-352, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
FUNCTION.
PubMed=20212317; DOI=10.1083/jcb.200909008;
Mukhopadhyay D., Arnaoutov A., Dasso M.;
"The SUMO protease SENP6 is essential for inner kinetochore
assembly.";
J. Cell Biol. 188:681-692(2010).
[17]
FUNCTION, AND INTERACTION WITH RPA1.
PubMed=20705237; DOI=10.1016/j.molcel.2010.07.021;
Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.;
"Regulation of DNA repair through desumoylation and sumoylation of
replication protein A complex.";
Mol. Cell 39:333-345(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
FUNCTION.
PubMed=21148299; DOI=10.1091/mbc.E10-06-0504;
Hattersley N., Shen L., Jaffray E.G., Hay R.T.;
"The SUMO protease SENP6 is a direct regulator of PML nuclear
bodies.";
Mol. Biol. Cell 22:78-90(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416; SER-919 AND
SER-1111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-628, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from
targeted proteins. Processes preferentially poly-SUMO2 and poly-
SUMO3 chains, but does not efficiently process SUMO1, SUMO2 and
SUMO3 precursors. Deconjugates SUMO1 from RXRA, leading to
transcriptional activation. Involved in chromosome alignment and
spindle assembly, by regulating the kinetochore CENPH-CENPI-CENPK
complex. Desumoylates PML and CENPI, protecting them from
degradation by the ubiquitin ligase RNF4, which targets
polysumoylated proteins for proteasomal degradation. Desumoylates
also RPA1, thus preventing recruitment of RAD51 to the DNA damage
foci to initiate DNA repair through homologous recombination.
{ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:17000875,
ECO:0000269|PubMed:18799455, ECO:0000269|PubMed:20212317,
ECO:0000269|PubMed:20705237, ECO:0000269|PubMed:21148299}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Interacts with RXRA. Forms a complex with KAT5-TIP60 and
UBE2I in response to UV irradiation. Interacts with RPA1 to
maintain it in hyposumoylated state during S phase preventing DNA
repair initiation. {ECO:0000269|PubMed:16912044,
ECO:0000269|PubMed:20705237}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16912044,
ECO:0000269|PubMed:17000875}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9GZR1-1; Sequence=Displayed;
Name=2;
IsoId=Q9GZR1-2; Sequence=VSP_005274;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in reproductive organs, such
as testis, ovary and prostate.
-!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34517.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAH72480.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH72481.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH74168.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH74170.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI19523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI23575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI23576.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF196304; AAF04852.1; -; mRNA.
EMBL; AF307849; AAG29831.1; -; mRNA.
EMBL; AF306508; AAG30253.1; -; mRNA.
EMBL; AB018340; BAA34517.2; ALT_INIT; mRNA.
EMBL; AL589656; CAH72480.1; ALT_SEQ; Genomic_DNA.
EMBL; AL109897; CAH72480.1; JOINED; Genomic_DNA.
EMBL; AL355797; CAH72480.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAH72480.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAH72481.1; ALT_SEQ; Genomic_DNA.
EMBL; AL355797; CAH72481.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAH72481.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAH74168.1; ALT_SEQ; Genomic_DNA.
EMBL; AL109897; CAH74168.1; JOINED; Genomic_DNA.
EMBL; AL355797; CAH74168.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAH74168.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAH74170.1; ALT_SEQ; Genomic_DNA.
EMBL; AL355797; CAH74170.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAH74170.1; JOINED; Genomic_DNA.
EMBL; AL109897; CAI19523.1; ALT_SEQ; Genomic_DNA.
EMBL; AL355797; CAI19523.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAI19523.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAI19523.1; JOINED; Genomic_DNA.
EMBL; AL355797; CAI23575.1; ALT_SEQ; Genomic_DNA.
EMBL; AL109897; CAI23575.1; JOINED; Genomic_DNA.
EMBL; AL356057; CAI23575.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAI23575.1; JOINED; Genomic_DNA.
EMBL; AL355797; CAI23576.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356057; CAI23576.1; JOINED; Genomic_DNA.
EMBL; AL589656; CAI23576.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48734.1; -; Genomic_DNA.
EMBL; BC028583; AAH28583.1; -; mRNA.
EMBL; AK096455; BAC04794.1; -; mRNA.
CCDS; CCDS43483.1; -. [Q9GZR1-2]
CCDS; CCDS47454.1; -. [Q9GZR1-1]
RefSeq; NP_001093879.1; NM_001100409.2. [Q9GZR1-2]
RefSeq; NP_001291721.1; NM_001304792.1.
RefSeq; NP_056386.2; NM_015571.3. [Q9GZR1-1]
UniGene; Hs.485784; -.
ProteinModelPortal; Q9GZR1; -.
SMR; Q9GZR1; -.
BioGrid; 117517; 14.
IntAct; Q9GZR1; 5.
STRING; 9606.ENSP00000402527; -.
BindingDB; Q9GZR1; -.
ChEMBL; CHEMBL1741215; -.
MEROPS; C48.004; -.
iPTMnet; Q9GZR1; -.
PhosphoSitePlus; Q9GZR1; -.
BioMuta; SENP6; -.
DMDM; 119370526; -.
MaxQB; Q9GZR1; -.
PaxDb; Q9GZR1; -.
PeptideAtlas; Q9GZR1; -.
PRIDE; Q9GZR1; -.
Ensembl; ENST00000370010; ENSP00000359027; ENSG00000112701. [Q9GZR1-2]
Ensembl; ENST00000447266; ENSP00000402527; ENSG00000112701. [Q9GZR1-1]
GeneID; 26054; -.
KEGG; hsa:26054; -.
UCSC; uc003pid.5; human. [Q9GZR1-1]
CTD; 26054; -.
DisGeNET; 26054; -.
EuPathDB; HostDB:ENSG00000112701.17; -.
GeneCards; SENP6; -.
HGNC; HGNC:20944; SENP6.
HPA; HPA024376; -.
MIM; 605003; gene.
neXtProt; NX_Q9GZR1; -.
OpenTargets; ENSG00000112701; -.
PharmGKB; PA134893291; -.
eggNOG; KOG0779; Eukaryota.
eggNOG; COG5160; LUCA.
GeneTree; ENSGT00530000063531; -.
HOVERGEN; HBG059746; -.
InParanoid; Q9GZR1; -.
KO; K08595; -.
OMA; YPPHVQK; -.
OrthoDB; EOG091G012K; -.
PhylomeDB; Q9GZR1; -.
TreeFam; TF350136; -.
BRENDA; 3.4.22.B74; 2681.
UniPathway; UPA00886; -.
ChiTaRS; SENP6; human.
GeneWiki; SENP6; -.
GenomeRNAi; 26054; -.
PRO; PR:Q9GZR1; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112701; -.
CleanEx; HS_SENP6; -.
ExpressionAtlas; Q9GZR1; baseline and differential.
Genevisible; Q9GZR1; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016929; F:SUMO-specific protease activity; IMP:UniProtKB.
GO; GO:0016926; P:protein desumoylation; IMP:UniProtKB.
GO; GO:0070646; P:protein modification by small protein removal; IDA:UniProtKB.
GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
GO; GO:0090234; P:regulation of kinetochore assembly; IMP:UniProtKB.
GO; GO:0090169; P:regulation of spindle assembly; IMP:UniProtKB.
InterPro; IPR003653; Peptidase_C48_C.
Pfam; PF02902; Peptidase_C48; 2.
PROSITE; PS50600; ULP_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Hydrolase; Isopeptide bond;
Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 1112 Sentrin-specific protease 6.
/FTId=PRO_0000101725.
REGION 666 1112 Protease.
ACT_SITE 765 765 {ECO:0000250}.
ACT_SITE 917 917 {ECO:0000250}.
ACT_SITE 1030 1030 {ECO:0000250}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 350 350 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 416 416 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 919 919 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1111 1111 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 628 628 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 153 159 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005274.
VARIANT 121 121 T -> M (in dbSNP:rs17414086).
{ECO:0000269|PubMed:10799485,
ECO:0000269|PubMed:9872452}.
/FTId=VAR_029653.
VARIANT 637 637 E -> K (in dbSNP:rs1061347).
/FTId=VAR_029654.
VARIANT 717 717 R -> P (in dbSNP:rs12195603).
/FTId=VAR_029655.
VARIANT 820 820 A -> V (in dbSNP:rs34045941).
/FTId=VAR_051545.
VARIANT 1106 1106 Y -> C (in dbSNP:rs9250).
{ECO:0000269|PubMed:10799485,
ECO:0000269|PubMed:9872452}.
/FTId=VAR_016096.
MUTAGEN 1030 1030 C->S: Abolishes enzymatic activity.
{ECO:0000269|PubMed:16912044}.
CONFLICT 293 293 D -> V (in Ref. 9; BAC04794).
{ECO:0000305}.
CONFLICT 1043 1043 E -> Q (in Ref. 1; AAG29831 and 3;
AAG30253). {ECO:0000305}.
SEQUENCE 1112 AA; 126146 MW; A7B07C75C39EE786 CRC64;
MAAGKSGGSA GEITFLEALA RSESKRDGGF KNNWSFDHEE ESEGDTDKDG TNLLSVDEDE
DSETSKGKKL NRRSEIVANS SGEFILKTYV RRNKSESFKT LKGNPIGLNM LSNNKKLSEN
TQNTSLCSGT VVHGRRFHHA HAQIPVVKTA AQSSLDRKER KEYPPHVQKV EINPVRLSRL
QGVERIMKKT EESESQVEPE IKRKVQQKRH CSTYQPTPPL SPASKKCLTH LEDLQRNCRQ
AITLNESTGP LLRTSIHQNS GGQKSQNTGL TTKKFYGNNV EKVPIDIIVN CDDSKHTYLQ
TNGKVILPGA KIPKITNLKE RKTSLSDLND PIILSSDDDD DNDRTNRRES ISPQPADSAC
SSPAPSTGKV EAALNENTCR AERELRSIPE DSELNTVTLP RKARMKDQFG NSIINTPLKR
RKVFSQEPPD ALALSCQSSF DSVILNCRSI RVGTLFRLLI EPVIFCLDFI KIQLDEPDHD
PVEIILNTSD LTKCEWCNVR KLPVVFLQAI PAVYQKLSIQ LQMNKEDKVW NDCKGVNKLT
NLEEQYIILI FQNGLDPPAN MVFESIINEI GIKNNISNFF AKIPFEEANG RLVACTRTYE
ESIKGSCGQK ENKIKTVSFE SKIQLRSKQE FQFFDEEEET GENHTIFIGP VEKLIVYPPP
PAKGGISVTN EDLHCLNEGE FLNDVIIDFY LKYLVLEKLK KEDADRIHIF SSFFYKRLNQ
RERRNHETTN LSIQQKRHGR VKTWTRHVDI FEKDFIFVPL NEAAHWFLAV VCFPGLEKPK
YEPNPHYHEN AVIQKCSTVE DSCISSSASE MESCSQNSSA KPVIKKMLNK KHCIAVIDSN
PGQEESDPRY KRNICSVKYS VKKINHTASE NEEFNKGEST SQKVADRTKS ENGLQNESLS
STHHTDGLSK IRLNYSDESP EAGKMLEDEL VDFSEDQDNQ DDSSDDGFLA DDNCSSEIGQ
WHLKPTICKQ PCILLMDSLR GPSRSNVVKI LREYLEVEWE VKKGSKRSFS KDVMKGSNPK
VPQQNNFSDC GVYVLQYVES FFENPILSFE LPMNLANWFP PPRMRTKREE IRNIILKLQE
DQSKEKRKHK DTYSTEAPLG EGTEQYVNSI SD


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