SENP6_HUMAN
ID SENP6_HUMAN Reviewed; 1112 AA.
AC Q9GZR1; A6NNY9; O94891; Q5VUL3; Q5VUL4; Q8TBY4; Q9UJV5;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Sentrin-specific protease 6;
DE EC=3.4.22.- {ECO:0000269|PubMed:18799455};
DE AltName: Full=SUMO-1-specific protease 1;
DE AltName: Full=Sentrin/SUMO-specific protease SENP6;
GN Name=SENP6; Synonyms=KIAA0797, SSP1, SUSP1; ORFNames=FKSG6;
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).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-121 AND CYS-1106, AND
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=10799485; DOI=10.1074/jbc.275.19.14102;
RA Kim K.I., Baek S.H., Jeon Y.-J., Nishimori S., Suzuki T., Uchida S.,
RA Shimbara N., Saitoh H., Tanaka K., Chung C.H.;
RT "A new SUMO-1-specific protease, SUSP1, that is highly expressed in
RT reproductive organs.";
RL J. Biol. Chem. 275:14102-14106(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang Y.-G.;
RT "Identification of FKSG6, a novel protein with protease activity.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-121
RP AND CYS-1106.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692 (ISOFORM 2).
RC TISSUE=Tongue;
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 [10]
RP INTERACTION WITH RXRA, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF
RP CYS-1030.
RX PubMed=16912044; DOI=10.1074/jbc.m604033200;
RA Choi S.J., Chung S.S., Rho E.J., Lee H.W., Lee M.H., Choi H.S., Seol J.H.,
RA Baek S.H., Bang O.S., Chung C.H.;
RT "Negative modulation of RXRalpha transcriptional activity by small
RT ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-
RT specific protease SUSP1.";
RL J. Biol. Chem. 281:30669-30677(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17000875; DOI=10.1083/jcb.200510103;
RA Mukhopadhyay D., Ayaydin F., Kolli N., Tan S.-H., Anan T., Kametaka A.,
RA Azuma Y., Wilkinson K.D., Dasso M.;
RT "SUSP1 antagonizes formation of highly SUMO2/3-conjugated species.";
RL J. Cell Biol. 174:939-949(2006).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18799455; DOI=10.1074/jbc.m805655200;
RA Lima C.D., Reverter D.;
RT "Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation
RT activities for SENP6 and SENP7.";
RL J. Biol. Chem. 283:32045-32055(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION OF KAT5-UBE2I-SENP6
RP COMPLEX.
RX PubMed=17704809; DOI=10.1038/sj.onc.1210710;
RA Cheng Z., Ke Y., Ding X., Wang F., Wang H., Wang W., Ahmed K., Liu Z.,
RA Xu Y., Aikhionbare F., Yan H., Liu J., Xue Y., Yu J., Powell M., Liang S.,
RA Wu Q., Reddy S.E., Hu R., Huang H., Jin C., Yao X.;
RT "Functional characterization of TIP60 sumoylation in UV-irradiated DNA
RT damage response.";
RL Oncogene 27:931-941(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-350 AND
RP SER-352, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
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 [16]
RP FUNCTION.
RX PubMed=20212317; DOI=10.1083/jcb.200909008;
RA Mukhopadhyay D., Arnaoutov A., Dasso M.;
RT "The SUMO protease SENP6 is essential for inner kinetochore assembly.";
RL J. Cell Biol. 188:681-692(2010).
RN [17]
RP FUNCTION, AND INTERACTION WITH RPA1.
RX PubMed=20705237; DOI=10.1016/j.molcel.2010.07.021;
RA Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T.;
RT "Regulation of DNA repair through desumoylation and sumoylation of
RT replication protein A complex.";
RL Mol. Cell 39:333-345(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP FUNCTION.
RX PubMed=21148299; DOI=10.1091/mbc.e10-06-0504;
RA Hattersley N., Shen L., Jaffray E.G., Hay R.T.;
RT "The SUMO protease SENP6 is a direct regulator of PML nuclear bodies.";
RL Mol. Biol. Cell 22:78-90(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416; SER-919 AND SER-1111,
RP AND 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 [22]
RP IDENTIFICATION BY 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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-628, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Protease that deconjugates SUMO1, SUMO2 and SUMO3 from
CC targeted proteins. Processes preferentially poly-SUMO2 and poly-SUMO3
CC chains, but does not efficiently process SUMO1, SUMO2 and SUMO3
CC precursors. Deconjugates SUMO1 from RXRA, leading to transcriptional
CC activation. Involved in chromosome alignment and spindle assembly, by
CC regulating the kinetochore CENPH-CENPI-CENPK complex. Desumoylates PML
CC and CENPI, protecting them from degradation by the ubiquitin ligase
CC RNF4, which targets polysumoylated proteins for proteasomal
CC degradation. Desumoylates also RPA1, thus preventing recruitment of
CC RAD51 to the DNA damage foci to initiate DNA repair through homologous
CC recombination. {ECO:0000269|PubMed:16912044,
CC ECO:0000269|PubMed:17000875, ECO:0000269|PubMed:18799455,
CC ECO:0000269|PubMed:20212317, ECO:0000269|PubMed:20705237,
CC ECO:0000269|PubMed:21148299}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with RXRA. Forms a complex with KAT5-TIP60 and UBE2I
CC in response to UV irradiation. Interacts with RPA1 to maintain it in
CC hyposumoylated state during S phase preventing DNA repair initiation.
CC {ECO:0000269|PubMed:16912044, ECO:0000269|PubMed:20705237}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16912044,
CC ECO:0000269|PubMed:17000875}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZR1-2; Sequence=VSP_005274;
CC -!- TISSUE SPECIFICITY: Highly expressed in reproductive organs, such as
CC testis, ovary and prostate.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34517.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF196304; AAF04852.1; -; mRNA.
DR EMBL; AF307849; AAG29831.1; -; mRNA.
DR EMBL; AF306508; AAG30253.1; -; mRNA.
DR EMBL; AB018340; BAA34517.2; ALT_INIT; mRNA.
DR EMBL; AL109897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48734.1; -; Genomic_DNA.
DR EMBL; BC028583; AAH28583.1; -; mRNA.
DR EMBL; AK096455; BAC04794.1; -; mRNA.
DR CCDS; CCDS43483.1; -. [Q9GZR1-2]
DR CCDS; CCDS47454.1; -. [Q9GZR1-1]
DR RefSeq; NP_001093879.1; NM_001100409.2. [Q9GZR1-2]
DR RefSeq; NP_001291721.1; NM_001304792.1.
DR RefSeq; NP_056386.2; NM_015571.3. [Q9GZR1-1]
DR AlphaFoldDB; Q9GZR1; -.
DR SMR; Q9GZR1; -.
DR BioGRID; 117517; 41.
DR IntAct; Q9GZR1; 11.
DR STRING; 9606.ENSP00000402527; -.
DR BindingDB; Q9GZR1; -.
DR ChEMBL; CHEMBL1741215; -.
DR MEROPS; C48.004; -.
DR GlyGen; Q9GZR1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9GZR1; -.
DR PhosphoSitePlus; Q9GZR1; -.
DR BioMuta; SENP6; -.
DR DMDM; 119370526; -.
DR EPD; Q9GZR1; -.
DR jPOST; Q9GZR1; -.
DR MassIVE; Q9GZR1; -.
DR MaxQB; Q9GZR1; -.
DR PaxDb; Q9GZR1; -.
DR PeptideAtlas; Q9GZR1; -.
DR PRIDE; Q9GZR1; -.
DR ProteomicsDB; 80116; -. [Q9GZR1-1]
DR ProteomicsDB; 80117; -. [Q9GZR1-2]
DR Antibodypedia; 7742; 420 antibodies from 32 providers.
DR DNASU; 26054; -.
DR Ensembl; ENST00000370010.6; ENSP00000359027.2; ENSG00000112701.18. [Q9GZR1-2]
DR Ensembl; ENST00000447266.7; ENSP00000402527.2; ENSG00000112701.18. [Q9GZR1-1]
DR GeneID; 26054; -.
DR KEGG; hsa:26054; -.
DR MANE-Select; ENST00000447266.7; ENSP00000402527.2; NM_015571.4; NP_056386.2.
DR UCSC; uc003pid.5; human. [Q9GZR1-1]
DR CTD; 26054; -.
DR DisGeNET; 26054; -.
DR GeneCards; SENP6; -.
DR HGNC; HGNC:20944; SENP6.
DR HPA; ENSG00000112701; Low tissue specificity.
DR MIM; 605003; gene.
DR neXtProt; NX_Q9GZR1; -.
DR OpenTargets; ENSG00000112701; -.
DR PharmGKB; PA134893291; -.
DR VEuPathDB; HostDB:ENSG00000112701; -.
DR eggNOG; KOG0779; Eukaryota.
DR GeneTree; ENSGT00940000155724; -.
DR HOGENOM; CLU_009561_0_0_1; -.
DR InParanoid; Q9GZR1; -.
DR OMA; RKEYPAH; -.
DR PhylomeDB; Q9GZR1; -.
DR TreeFam; TF350136; -.
DR BRENDA; 3.4.22.B74; 2681.
DR PathwayCommons; Q9GZR1; -.
DR SignaLink; Q9GZR1; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 26054; 695 hits in 1084 CRISPR screens.
DR ChiTaRS; SENP6; human.
DR GeneWiki; SENP6; -.
DR GenomeRNAi; 26054; -.
DR Pharos; Q9GZR1; Tchem.
DR PRO; PR:Q9GZR1; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9GZR1; protein.
DR Bgee; ENSG00000112701; Expressed in calcaneal tendon and 202 other tissues.
DR ExpressionAtlas; Q9GZR1; baseline and differential.
DR Genevisible; Q9GZR1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; IMP:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IMP:UniProtKB.
DR GO; GO:0070646; P:protein modification by small protein removal; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0090234; P:regulation of kinetochore assembly; IMP:UniProtKB.
DR GO; GO:0090169; P:regulation of spindle assembly; IMP:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..1112
FT /note="Sentrin-specific protease 6"
FT /id="PRO_0000101725"
FT REGION 26..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..1112
FT /note="Protease"
FT REGION 870..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 765
FT /evidence="ECO:0000250"
FT ACT_SITE 917
FT /evidence="ECO:0000250"
FT ACT_SITE 1030
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 153..159
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005274"
FT VARIANT 121
FT /note="T -> M (in dbSNP:rs17414086)"
FT /evidence="ECO:0000269|PubMed:10799485,
FT ECO:0000269|PubMed:9872452"
FT /id="VAR_029653"
FT VARIANT 637
FT /note="E -> K (in dbSNP:rs1061347)"
FT /id="VAR_029654"
FT VARIANT 717
FT /note="R -> P (in dbSNP:rs12195603)"
FT /id="VAR_029655"
FT VARIANT 820
FT /note="A -> V (in dbSNP:rs34045941)"
FT /id="VAR_051545"
FT VARIANT 1106
FT /note="Y -> C (in dbSNP:rs9250)"
FT /evidence="ECO:0000269|PubMed:10799485,
FT ECO:0000269|PubMed:9872452"
FT /id="VAR_016096"
FT MUTAGEN 1030
FT /note="C->S: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16912044"
FT CONFLICT 293
FT /note="D -> V (in Ref. 9; BAC04794)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="E -> Q (in Ref. 1; AAG29831 and 3; AAG30253)"
FT /evidence="ECO:0000305"
SQ 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
