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Q9GZR1

- SENP6_HUMAN

UniProt

Q9GZR1 - SENP6_HUMAN

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Protein

Sentrin-specific protease 6

Gene

SENP6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei765 – 7651By similarity
Active sitei917 – 9171By similarity
Active sitei1030 – 10301By similarity

GO - Molecular functioni

  1. SUMO-specific protease activity Source: UniProtKB

GO - Biological processi

  1. protein desumoylation Source: UniProtKB
  2. protein modification by small protein removal Source: UniProtKB
  3. protein sumoylation Source: UniProtKB-UniPathway
  4. regulation of kinetochore assembly Source: UniProtKB
  5. regulation of spindle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00886.

Protein family/group databases

MEROPSiC48.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Sentrin-specific protease 6 (EC:3.4.22.68)
Alternative name(s):
SUMO-1-specific protease 1
Sentrin/SUMO-specific protease SENP6
Gene namesi
Name:SENP6
Synonyms:KIAA0797, SSP1, SUSP1
ORF Names:FKSG6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20944. SENP6.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1030 – 10301C → S: Abolishes enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA134893291.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11121112Sentrin-specific protease 6PRO_0000101725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei335 – 3351Phosphoserine1 Publication
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei352 – 3521Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9GZR1.
PaxDbiQ9GZR1.
PRIDEiQ9GZR1.

PTM databases

PhosphoSiteiQ9GZR1.

Expressioni

Tissue specificityi

Highly expressed in reproductive organs, such as testis, ovary and prostate.

Gene expression databases

BgeeiQ9GZR1.
CleanExiHS_SENP6.
ExpressionAtlasiQ9GZR1. baseline and differential.
GenevestigatoriQ9GZR1.

Organism-specific databases

HPAiHPA024376.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi117517. 11 interactions.
IntActiQ9GZR1. 3 interactions.
STRINGi9606.ENSP00000402527.

Structurei

3D structure databases

ProteinModelPortaliQ9GZR1.
SMRiQ9GZR1. Positions 651-782, 967-1084.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni666 – 1112447ProteaseAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C48 family.Curated

Phylogenomic databases

eggNOGiCOG5160.
GeneTreeiENSGT00530000063531.
HOVERGENiHBG059746.
InParanoidiQ9GZR1.
KOiK08595.
OrthoDBiEOG780RMX.
PhylomeDBiQ9GZR1.
TreeFamiTF350136.

Family and domain databases

InterProiIPR003653. Peptidase_C48.
[Graphical view]
PfamiPF02902. Peptidase_C48. 2 hits.
[Graphical view]
PROSITEiPS50600. ULP_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9GZR1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAAGKSGGSA GEITFLEALA RSESKRDGGF KNNWSFDHEE ESEGDTDKDG
60 70 80 90 100
TNLLSVDEDE DSETSKGKKL NRRSEIVANS SGEFILKTYV RRNKSESFKT
110 120 130 140 150
LKGNPIGLNM LSNNKKLSEN TQNTSLCSGT VVHGRRFHHA HAQIPVVKTA
160 170 180 190 200
AQSSLDRKER KEYPPHVQKV EINPVRLSRL QGVERIMKKT EESESQVEPE
210 220 230 240 250
IKRKVQQKRH CSTYQPTPPL SPASKKCLTH LEDLQRNCRQ AITLNESTGP
260 270 280 290 300
LLRTSIHQNS GGQKSQNTGL TTKKFYGNNV EKVPIDIIVN CDDSKHTYLQ
310 320 330 340 350
TNGKVILPGA KIPKITNLKE RKTSLSDLND PIILSSDDDD DNDRTNRRES
360 370 380 390 400
ISPQPADSAC SSPAPSTGKV EAALNENTCR AERELRSIPE DSELNTVTLP
410 420 430 440 450
RKARMKDQFG NSIINTPLKR RKVFSQEPPD ALALSCQSSF DSVILNCRSI
460 470 480 490 500
RVGTLFRLLI EPVIFCLDFI KIQLDEPDHD PVEIILNTSD LTKCEWCNVR
510 520 530 540 550
KLPVVFLQAI PAVYQKLSIQ LQMNKEDKVW NDCKGVNKLT NLEEQYIILI
560 570 580 590 600
FQNGLDPPAN MVFESIINEI GIKNNISNFF AKIPFEEANG RLVACTRTYE
610 620 630 640 650
ESIKGSCGQK ENKIKTVSFE SKIQLRSKQE FQFFDEEEET GENHTIFIGP
660 670 680 690 700
VEKLIVYPPP PAKGGISVTN EDLHCLNEGE FLNDVIIDFY LKYLVLEKLK
710 720 730 740 750
KEDADRIHIF SSFFYKRLNQ RERRNHETTN LSIQQKRHGR VKTWTRHVDI
760 770 780 790 800
FEKDFIFVPL NEAAHWFLAV VCFPGLEKPK YEPNPHYHEN AVIQKCSTVE
810 820 830 840 850
DSCISSSASE MESCSQNSSA KPVIKKMLNK KHCIAVIDSN PGQEESDPRY
860 870 880 890 900
KRNICSVKYS VKKINHTASE NEEFNKGEST SQKVADRTKS ENGLQNESLS
910 920 930 940 950
STHHTDGLSK IRLNYSDESP EAGKMLEDEL VDFSEDQDNQ DDSSDDGFLA
960 970 980 990 1000
DDNCSSEIGQ WHLKPTICKQ PCILLMDSLR GPSRSNVVKI LREYLEVEWE
1010 1020 1030 1040 1050
VKKGSKRSFS KDVMKGSNPK VPQQNNFSDC GVYVLQYVES FFENPILSFE
1060 1070 1080 1090 1100
LPMNLANWFP PPRMRTKREE IRNIILKLQE DQSKEKRKHK DTYSTEAPLG
1110
EGTEQYVNSI SD
Length:1,112
Mass (Da):126,146
Last modified:December 12, 2006 - v2
Checksum:iA7B07C75C39EE786
GO
Isoform 2 (identifier: Q9GZR1-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,105
Mass (Da):125,330
Checksum:i7C0F2FF3E8BE3D46
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti293 – 2931D → V in BAC04794. (PubMed:14702039)Curated
Sequence conflicti1043 – 10431E → Q in AAG29831. (PubMed:10806345)Curated
Sequence conflicti1043 – 10431E → Q in AAG30253. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211T → M.2 Publications
Corresponds to variant rs17414086 [ dbSNP | Ensembl ].
VAR_029653
Natural varianti637 – 6371E → K.
Corresponds to variant rs1061347 [ dbSNP | Ensembl ].
VAR_029654
Natural varianti717 – 7171R → P.
Corresponds to variant rs12195603 [ dbSNP | Ensembl ].
VAR_029655
Natural varianti820 – 8201A → V.
Corresponds to variant rs34045941 [ dbSNP | Ensembl ].
VAR_051545
Natural varianti1106 – 11061Y → C.2 Publications
Corresponds to variant rs9250 [ dbSNP | Ensembl ].
VAR_016096

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 1597Missing in isoform 2. 2 PublicationsVSP_005274

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43483.1. [Q9GZR1-2]
CCDS47454.1. [Q9GZR1-1]
RefSeqiNP_001093879.1. NM_001100409.1. [Q9GZR1-2]
NP_056386.2. NM_015571.2. [Q9GZR1-1]
UniGeneiHs.485784.

Genome annotation databases

EnsembliENST00000370010; ENSP00000359027; ENSG00000112701. [Q9GZR1-2]
ENST00000447266; ENSP00000402527; ENSG00000112701. [Q9GZR1-1]
GeneIDi26054.
KEGGihsa:26054.
UCSCiuc003pid.4. human. [Q9GZR1-1]
uc003pie.4. human. [Q9GZR1-2]

Polymorphism databases

DMDMi119370526.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43483.1. [Q9GZR1-2 ]
CCDS47454.1. [Q9GZR1-1 ]
RefSeqi NP_001093879.1. NM_001100409.1. [Q9GZR1-2 ]
NP_056386.2. NM_015571.2. [Q9GZR1-1 ]
UniGenei Hs.485784.

3D structure databases

ProteinModelPortali Q9GZR1.
SMRi Q9GZR1. Positions 651-782, 967-1084.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117517. 11 interactions.
IntActi Q9GZR1. 3 interactions.
STRINGi 9606.ENSP00000402527.

Chemistry

ChEMBLi CHEMBL1741215.

Protein family/group databases

MEROPSi C48.004.

PTM databases

PhosphoSitei Q9GZR1.

Polymorphism databases

DMDMi 119370526.

Proteomic databases

MaxQBi Q9GZR1.
PaxDbi Q9GZR1.
PRIDEi Q9GZR1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370010 ; ENSP00000359027 ; ENSG00000112701 . [Q9GZR1-2 ]
ENST00000447266 ; ENSP00000402527 ; ENSG00000112701 . [Q9GZR1-1 ]
GeneIDi 26054.
KEGGi hsa:26054.
UCSCi uc003pid.4. human. [Q9GZR1-1 ]
uc003pie.4. human. [Q9GZR1-2 ]

Organism-specific databases

CTDi 26054.
GeneCardsi GC06P076311.
HGNCi HGNC:20944. SENP6.
HPAi HPA024376.
MIMi 605003. gene.
neXtProti NX_Q9GZR1.
PharmGKBi PA134893291.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5160.
GeneTreei ENSGT00530000063531.
HOVERGENi HBG059746.
InParanoidi Q9GZR1.
KOi K08595.
OrthoDBi EOG780RMX.
PhylomeDBi Q9GZR1.
TreeFami TF350136.

Enzyme and pathway databases

UniPathwayi UPA00886 .

Miscellaneous databases

ChiTaRSi SENP6. human.
GeneWikii SENP6.
GenomeRNAii 26054.
NextBioi 47924.
PROi Q9GZR1.
SOURCEi Search...

Gene expression databases

Bgeei Q9GZR1.
CleanExi HS_SENP6.
ExpressionAtlasi Q9GZR1. baseline and differential.
Genevestigatori Q9GZR1.

Family and domain databases

InterProi IPR003653. Peptidase_C48.
[Graphical view ]
Pfami PF02902. Peptidase_C48. 2 hits.
[Graphical view ]
PROSITEi PS50600. ULP_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.
    , 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. 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.
    , 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. 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. 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].

Entry informationi

Entry nameiSENP6_HUMAN
AccessioniPrimary (citable) accession number: Q9GZR1
Secondary accession number(s): A6NNY9
, O94891, Q5VUL3, Q5VUL4, Q8TBY4, Q9UJV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: December 12, 2006
Last modified: October 29, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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