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Q9GZR1 (SENP6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sentrin-specific protease 6

EC=3.4.22.68
Alternative name(s):
SUMO-1-specific protease 1
Sentrin/SUMO-specific protease SENP6
Gene names
Name:SENP6
Synonyms:KIAA0797, SSP1, SUSP1
ORF Names:FKSG6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1112 AA.
Sequence statusComplete.
Protein existenceEvidence 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 recombination. Ref.10 Ref.11 Ref.12 Ref.16 Ref.17 Ref.19

Catalytic activity

Hydrolysis of the alpha-linked peptide bond in the sequence Gly-Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.

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.10 Ref.17

Subcellular location

Nucleus Ref.10 Ref.11.

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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11121112Sentrin-specific protease 6
PRO_0000101725

Regions

Region666 – 1112447Protease

Sites

Active site7651 By similarity
Active site9171 By similarity
Active site10301 By similarity

Amino acid modifications

Modified residue421Phosphoserine Ref.20
Modified residue3351Phosphoserine Ref.14
Modified residue3361Phosphoserine Ref.14
Modified residue3501Phosphoserine Ref.14
Modified residue3521Phosphoserine Ref.14

Natural variations

Alternative sequence153 – 1597Missing in isoform 2.
VSP_005274
Natural variant1211T → M. Ref.2 Ref.4
Corresponds to variant rs17414086 [ dbSNP | Ensembl ].
VAR_029653
Natural variant6371E → K.
Corresponds to variant rs1061347 [ dbSNP | Ensembl ].
VAR_029654
Natural variant7171R → P.
Corresponds to variant rs12195603 [ dbSNP | Ensembl ].
VAR_029655
Natural variant8201A → V.
Corresponds to variant rs34045941 [ dbSNP | Ensembl ].
VAR_051545
Natural variant11061Y → C. Ref.2 Ref.4
Corresponds to variant rs9250 [ dbSNP | Ensembl ].
VAR_016096

Experimental info

Mutagenesis10301C → S: Abolishes enzymatic activity. Ref.10
Sequence conflict2931D → V in BAC04794. Ref.9
Sequence conflict10431E → Q in AAG29831. Ref.1
Sequence conflict10431E → Q in AAG30253. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 12, 2006. Version 2.
Checksum: A7B07C75C39EE786

FASTA1,112126,146
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7C0F2FF3E8BE3D46
Show »

FASTA1,105125,330

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-692 (ISOFORM 2).
Tissue: Tongue.
[10]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RXRA, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-1030.
[11]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[12]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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. expand/collapse author list , Hu R., Huang H., Jin C., Yao X.
Oncogene 27:931-941(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION OF KAT5-UBE2I-SENP6 COMPLEX.
[14]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-350 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"The SUMO protease SENP6 is essential for inner kinetochore assembly."
Mukhopadhyay D., Arnaoutov A., Dasso M.
J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RPA1.
[18]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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 expand/collapse EMBL AC list , AL109897, AL355797, AL356057 Genomic DNA. Translation: CAH72480.1. Sequence problems.
AL589656, AL355797, AL356057 Genomic DNA. Translation: CAH72481.1. Sequence problems.
AL356057 expand/collapse EMBL AC list , AL109897, AL355797, AL589656 Genomic DNA. Translation: CAH74168.1. Sequence problems.
AL356057, AL355797, AL589656 Genomic DNA. Translation: CAH74170.1. Sequence problems.
AL109897 expand/collapse EMBL AC list , AL355797, AL356057, AL589656 Genomic DNA. Translation: CAI19523.1. Sequence problems.
AL355797 expand/collapse EMBL AC list , 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.
RefSeqNP_001093879.1. NM_001100409.1.
NP_056386.2. NM_015571.2.
UniGeneHs.485784.

3D structure databases

ProteinModelPortalQ9GZR1.
SMRQ9GZR1. Positions 651-1084.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117517. 9 interactions.
IntActQ9GZR1. 3 interactions.
STRING9606.ENSP00000402527.

Chemistry

ChEMBLCHEMBL1741215.

Protein family/group databases

MEROPSC48.004.

PTM databases

PhosphoSiteQ9GZR1.

Polymorphism databases

DMDM119370526.

Proteomic databases

PaxDbQ9GZR1.
PRIDEQ9GZR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370010; ENSP00000359027; ENSG00000112701. [Q9GZR1-2]
ENST00000447266; ENSP00000402527; ENSG00000112701. [Q9GZR1-1]
GeneID26054.
KEGGhsa:26054.
UCSCuc003pid.4. human. [Q9GZR1-1]
uc003pie.4. human. [Q9GZR1-2]

Organism-specific databases

CTD26054.
GeneCardsGC06P076311.
HGNCHGNC:20944. SENP6.
HPAHPA024376.
MIM605003. gene.
neXtProtNX_Q9GZR1.
PharmGKBPA134893291.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5160.
HOVERGENHBG059746.
InParanoidQ9GZR1.
KOK08595.
OrthoDBEOG780RMX.
PhylomeDBQ9GZR1.
TreeFamTF350136.

Enzyme and pathway databases

UniPathwayUPA00886.

Gene expression databases

ArrayExpressQ9GZR1.
BgeeQ9GZR1.
CleanExHS_SENP6.
GenevestigatorQ9GZR1.

Family and domain databases

InterProIPR003653. Peptidase_C48.
[Graphical view]
PfamPF02902. Peptidase_C48. 2 hits.
[Graphical view]
PROSITEPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSENP6. human.
GeneWikiSENP6.
GenomeRNAi26054.
NextBio47924.
PROQ9GZR1.
SOURCESearch...

Entry information

Entry nameSENP6_HUMAN
AccessionPrimary (citable) accession number: Q9GZR1
Secondary accession number(s): A6NNY9 expand/collapse secondary AC list , O94891, Q5VUL3, Q5VUL4, Q8TBY4, Q9UJV5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM