Q9GZR1 (SENP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sentrin-specific protease 6
EC=3.4.22.-

Alternative name(s):
SUMO-1-specific protease 1
Sentrin/SUMO-specific protease SENP6

Gene names

Name:	SENP6
Synonyms:	KIAA0797, SSP1, SUSP1
ORF Names:	FKSG6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1112 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 recombinaison. Ref.12 Ref.13 Ref.14 Ref.19 Ref.20 Ref.22
Pathway	Protein modification; protein sumoylation.
Subunit structure	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. Ref.12 Ref.20
Subcellular location	Nucleus Ref.12 Ref.13.
Tissue specificity	Highly expressed in reproductive organs, such as testis, ovary and prostate.
Sequence similarities	Belongs to the peptidase C48 family.
Sequence caution	The sequence BAA34517.2 differs from that shown. Reason: Erroneous initiation. The sequence CAH72480.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH72481.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH74168.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAH74170.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI19523.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI23575.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI23576.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase Protease Thiol protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein desumoylation Inferred from mutant phenotype Ref.19. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW regulation of kinetochore assembly Inferred from mutant phenotype Ref.19. Source: UniProtKB regulation of spindle assembly Inferred from mutant phenotype Ref.19. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular function	SUMO-specific protease activity Inferred from mutant phenotype Ref.19. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9GZR1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9GZR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     153-159: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1112	1112	Sentrin-specific protease 6		PRO_0000101725
Regions
	Region	666 – 1112	447	Protease
Sites
	Active site	765	1	By similarity
	Active site	917	1	By similarity
	Active site	1030	1	By similarity
Amino acid modifications
	Modified residue	6	1	Phosphoserine By similarity
	Modified residue	9	1	Phosphoserine By similarity
	Modified residue	335	1	Phosphoserine Ref.11 Ref.16
	Modified residue	336	1	Phosphoserine Ref.11 Ref.16
	Modified residue	350	1	Phosphoserine Ref.16
	Modified residue	352	1	Phosphoserine Ref.16 Ref.17
	Modified residue	361	1	Phosphoserine Ref.16
	Modified residue	919	1	Phosphoserine Ref.10 Ref.18
Natural variations
	Alternative sequence	153 – 159	7	Missing in isoform 2.		VSP_005274
	Natural variant	121	1	T → M. Ref.2 Ref.4 Corresponds to variant rs17414086 [ dbSNP | Ensembl ].		VAR_029653
	Natural variant	637	1	E → K. Corresponds to variant rs1061347 [ dbSNP | Ensembl ].		VAR_029654
	Natural variant	717	1	R → P. Corresponds to variant rs12195603 [ dbSNP | Ensembl ].		VAR_029655
	Natural variant	820	1	A → V. Corresponds to variant rs34045941 [ dbSNP | Ensembl ].		VAR_051545
	Natural variant	1106	1	Y → C. Ref.2 Ref.4 Corresponds to variant rs9250 [ dbSNP | Ensembl ].		VAR_016096
Experimental info
	Mutagenesis	1030	1	C → S: Abolishes enzymatic activity. Ref.12
	Sequence conflict	293	1	D → V in BAC04794. Ref.9
	Sequence conflict	1043	1	E → Q in AAG29831. Ref.1
	Sequence conflict	1043	1	E → Q in AAG30253. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 12, 2006. Version 2. Checksum: A7B07C75C39EE786	FASTA	1,112	126,146
	10 20 30 40 50 60 MAAGKSGGSA GEITFLEALA RSESKRDGGF KNNWSFDHEE ESEGDTDKDG TNLLSVDEDE 70 80 90 100 110 120 DSETSKGKKL NRRSEIVANS SGEFILKTYV RRNKSESFKT LKGNPIGLNM LSNNKKLSEN 130 140 150 160 170 180 TQNTSLCSGT VVHGRRFHHA HAQIPVVKTA AQSSLDRKER KEYPPHVQKV EINPVRLSRL 190 200 210 220 230 240 QGVERIMKKT EESESQVEPE IKRKVQQKRH CSTYQPTPPL SPASKKCLTH LEDLQRNCRQ 250 260 270 280 290 300 AITLNESTGP LLRTSIHQNS GGQKSQNTGL TTKKFYGNNV EKVPIDIIVN CDDSKHTYLQ 310 320 330 340 350 360 TNGKVILPGA KIPKITNLKE RKTSLSDLND PIILSSDDDD DNDRTNRRES ISPQPADSAC 370 380 390 400 410 420 SSPAPSTGKV EAALNENTCR AERELRSIPE DSELNTVTLP RKARMKDQFG NSIINTPLKR 430 440 450 460 470 480 RKVFSQEPPD ALALSCQSSF DSVILNCRSI RVGTLFRLLI EPVIFCLDFI KIQLDEPDHD 490 500 510 520 530 540 PVEIILNTSD LTKCEWCNVR KLPVVFLQAI PAVYQKLSIQ LQMNKEDKVW NDCKGVNKLT 550 560 570 580 590 600 NLEEQYIILI FQNGLDPPAN MVFESIINEI GIKNNISNFF AKIPFEEANG RLVACTRTYE 610 620 630 640 650 660 ESIKGSCGQK ENKIKTVSFE SKIQLRSKQE FQFFDEEEET GENHTIFIGP VEKLIVYPPP 670 680 690 700 710 720 PAKGGISVTN EDLHCLNEGE FLNDVIIDFY LKYLVLEKLK KEDADRIHIF SSFFYKRLNQ 730 740 750 760 770 780 RERRNHETTN LSIQQKRHGR VKTWTRHVDI FEKDFIFVPL NEAAHWFLAV VCFPGLEKPK 790 800 810 820 830 840 YEPNPHYHEN AVIQKCSTVE DSCISSSASE MESCSQNSSA KPVIKKMLNK KHCIAVIDSN 850 860 870 880 890 900 PGQEESDPRY KRNICSVKYS VKKINHTASE NEEFNKGEST SQKVADRTKS ENGLQNESLS 910 920 930 940 950 960 STHHTDGLSK IRLNYSDESP EAGKMLEDEL VDFSEDQDNQ DDSSDDGFLA DDNCSSEIGQ 970 980 990 1000 1010 1020 WHLKPTICKQ PCILLMDSLR GPSRSNVVKI LREYLEVEWE VKKGSKRSFS KDVMKGSNPK 1030 1040 1050 1060 1070 1080 VPQQNNFSDC GVYVLQYVES FFENPILSFE LPMNLANWFP PPRMRTKREE IRNIILKLQE 1090 1100 1110 DQSKEKRKHK DTYSTEAPLG EGTEQYVNSI SD
	Isoform 2 [UniParc]. Checksum: 7C0F2FF3E8BE3D46	FASTA	1,105	125,330
	10 20 30 40 50 60 MAAGKSGGSA GEITFLEALA RSESKRDGGF KNNWSFDHEE ESEGDTDKDG TNLLSVDEDE 70 80 90 100 110 120 DSETSKGKKL NRRSEIVANS SGEFILKTYV RRNKSESFKT LKGNPIGLNM LSNNKKLSEN 130 140 150 160 170 180 TQNTSLCSGT VVHGRRFHHA HAQIPVVKTA AQRKEYPPHV QKVEINPVRL SRLQGVERIM 190 200 210 220 230 240 KKTEESESQV EPEIKRKVQQ KRHCSTYQPT PPLSPASKKC LTHLEDLQRN CRQAITLNES 250 260 270 280 290 300 TGPLLRTSIH QNSGGQKSQN TGLTTKKFYG NNVEKVPIDI IVNCDDSKHT YLQTNGKVIL 310 320 330 340 350 360 PGAKIPKITN LKERKTSLSD LNDPIILSSD DDDDNDRTNR RESISPQPAD SACSSPAPST 370 380 390 400 410 420 GKVEAALNEN TCRAERELRS IPEDSELNTV TLPRKARMKD QFGNSIINTP LKRRKVFSQE 430 440 450 460 470 480 PPDALALSCQ SSFDSVILNC RSIRVGTLFR LLIEPVIFCL DFIKIQLDEP DHDPVEIILN 490 500 510 520 530 540 TSDLTKCEWC NVRKLPVVFL QAIPAVYQKL SIQLQMNKED KVWNDCKGVN KLTNLEEQYI 550 560 570 580 590 600 ILIFQNGLDP PANMVFESII NEIGIKNNIS NFFAKIPFEE ANGRLVACTR TYEESIKGSC 610 620 630 640 650 660 GQKENKIKTV SFESKIQLRS KQEFQFFDEE EETGENHTIF IGPVEKLIVY PPPPAKGGIS 670 680 690 700 710 720 VTNEDLHCLN EGEFLNDVII DFYLKYLVLE KLKKEDADRI HIFSSFFYKR LNQRERRNHE 730 740 750 760 770 780 TTNLSIQQKR HGRVKTWTRH VDIFEKDFIF VPLNEAAHWF LAVVCFPGLE KPKYEPNPHY 790 800 810 820 830 840 HENAVIQKCS TVEDSCISSS ASEMESCSQN SSAKPVIKKM LNKKHCIAVI DSNPGQEESD 850 860 870 880 890 900 PRYKRNICSV KYSVKKINHT ASENEEFNKG ESTSQKVADR TKSENGLQNE SLSSTHHTDG 910 920 930 940 950 960 LSKIRLNYSD ESPEAGKMLE DELVDFSEDQ DNQDDSSDDG FLADDNCSSE IGQWHLKPTI 970 980 990 1000 1010 1020 CKQPCILLMD SLRGPSRSNV VKILREYLEV EWEVKKGSKR SFSKDVMKGS NPKVPQQNNF 1030 1040 1050 1060 1070 1080 SDCGVYVLQY VESFFENPIL SFELPMNLAN WFPPPRMRTK REEIRNIILK LQEDQSKEKR 1090 1100 KHKDTYSTEA PLGEGTEQYV NSISD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ubiquitin-like proteins: new wines in new bottles." Yeh E.T.H., Gong L., Kamitani T. Gene 248:1-14(2000) [PubMed: 10806345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs." Kim K.I., Baek S.H., Jeon Y.-J., Nishimori S., Suzuki T., Uchida S., Shimbara N., Saitoh H., Tanaka K., Chung C.H. J. Biol. Chem. 275:14102-14106(2000) [PubMed: 10799485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-121 AND CYS-1106, CHARACTERIZATION. Tissue: Brain.
[3]	"Identification of FKSG6, a novel protein with protease activity." Wang Y.-G. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"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." Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:277-286(1998) [PubMed: 9872452] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS MET-121 AND CYS-1106. Tissue: Brain.
[5]	Ohara O., Suyama M., Nagase T., Ishikawa K., Kikuno R. Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[6]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692 (ISOFORM 2). Tissue: Tongue.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-336, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1." 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. J. Biol. Chem. 281:30669-30677(2006) [PubMed: 16912044] [Abstract] Cited for: INTERACTION WITH RXRA, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-1030.
[13]	"SUSP1 antagonizes formation of highly SUMO2/3-conjugated species." Mukhopadhyay D., Ayaydin F., Kolli N., Tan S.-H., Anan T., Kametaka A., Azuma Y., Wilkinson K.D., Dasso M. J. Cell Biol. 174:939-949(2006) [PubMed: 17000875] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
[14]	"Structure of the human SENP7 catalytic domain and poly-SUMO deconjugation activities for SENP6 and SENP7." Lima C.D., Reverter D. J. Biol. Chem. 283:32045-32055(2008) [PubMed: 18799455] [Abstract] Cited for: FUNCTION.
[15]	"Functional characterization of TIP60 sumoylation in UV-irradiated DNA damage response." 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. Oncogene 27:931-941(2008) [PubMed: 17704809] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-350; SER-352 AND SER-361, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"The SUMO protease SENP6 is essential for inner kinetochore assembly." Mukhopadhyay D., Arnaoutov A., Dasso M. J. Cell Biol. 188:681-692(2010) [PubMed: 20212317] [Abstract] Cited for: FUNCTION.
[20]	"Regulation of DNA Repair through DeSUMOylation and SUMOylation of Replication Protein A Complex." Dou H., Huang C., Singh M., Carpenter P.B., Yeh E.T. Mol. Cell 39:333-345(2010) [PubMed: 20705237] [Abstract] Cited for: FUNCTION, INTERACTION WITH RPA1.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"The SUMO protease SENP6 is a direct regulator of PML nuclear bodies." Hattersley N., Shen L., Jaffray E.G., Hay R.T. Mol. Biol. Cell 22:78-90(2011) [PubMed: 21148299] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF196304 mRNA. Translation: AAF04852.1. AF307849 mRNA. Translation: AAG29831.1. AF306508 mRNA. Translation: AAG30253.1. AB018340 mRNA. Translation: BAA34517.2. Different initiation. AL589656 , AL109897, AL355797, AL356057 Genomic DNA. Translation: CAH72480.1. Sequence problems. AL589656, AL355797, AL356057 Genomic DNA. Translation: CAH72481.1. Sequence problems. AL356057 , AL109897, AL355797, AL589656 Genomic DNA. Translation: CAH74168.1. Sequence problems. AL356057, AL355797, AL589656 Genomic DNA. Translation: CAH74170.1. Sequence problems. AL109897 , AL355797, AL356057, AL589656 Genomic DNA. Translation: CAI19523.1. Sequence problems. AL355797 , AL109897, AL356057, AL589656 Genomic DNA. Translation: CAI23575.1. Sequence problems. AL355797, AL356057, AL589656 Genomic DNA. Translation: CAI23576.1. Sequence problems. CH471051 Genomic DNA. Translation: EAW48734.1. BC028583 mRNA. Translation: AAH28583.1. AK096455 mRNA. Translation: BAC04794.1.
IPI	IPI00023586. IPI00747900.
RefSeq	NP_001093879.1. NM_001100409.1. NP_056386.2. NM_015571.2.
UniGene	Hs.485784.
3D structure databases
ProteinModelPortal	Q9GZR1.
SMR	Q9GZR1. Positions 651-1084.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9GZR1. 3 interactions.
STRING	Q9GZR1.
Protein family/group databases
MEROPS	C48.004.
PTM databases
PhosphoSite	Q9GZR1.
Polymorphism databases
DMDM	119370526.
Proteomic databases
PRIDE	Q9GZR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000447266; ENSP00000402527; ENSG00000112701.
GeneID	26054.
KEGG	hsa:26054.
UCSC	uc003pid.2. human. uc003pie.2. human.
Organism-specific databases
CTD	26054.
GeneCards	GC06P076311.
HGNC	HGNC:20944. SENP6.
HPA	HPA024376.
MIM	605003. gene.
neXtProt	NX_Q9GZR1.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04721.
GeneTree	ENSGT00530000063531.
HOVERGEN	HBG059746.
InParanoid	Q9GZR1.
OMA	PVIKKML.
Gene expression databases
ArrayExpress	Q9GZR1.
Bgee	Q9GZR1.
CleanEx	HS_SENP6.
Genevestigator	Q9GZR1.
GermOnline	ENSG00000112701. Homo sapiens.
Family and domain databases
InterPro	IPR003653. Peptidase_C48. [Graphical view]
KO	K08595.
Pfam	PF02902. Peptidase_C48. 2 hits. [Graphical view]
PROSITE	PS50600. ULP_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	47924.
SOURCE	Search...

Entry information

Entry name

SENP6_HUMAN

Accession

Primary (citable) accession number: Q9GZR1
Secondary accession number(s): A6NNY9 , O94891, Q5VUL3, Q5VUL4, Q8TBY4, Q9UJV5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.