dbPTM

SENP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SENP6_HUMAN
UniProt AC	Q9GZR1
Protein Name	Sentrin-specific protease 6
Gene Name	SENP6
Organism	Homo sapiens (Human).
Sequence Length	1112
Subcellular Localization	Nucleus .
Protein Description	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..
Protein Sequence	MAAGKSGGSAGEITFLEALARSESKRDGGFKNNWSFDHEEESEGDTDKDGTNLLSVDEDEDSETSKGKKLNRRSEIVANSSGEFILKTYVRRNKSESFKTLKGNPIGLNMLSNNKKLSENTQNTSLCSGTVVHGRRFHHAHAQIPVVKTAAQSSLDRKERKEYPPHVQKVEINPVRLSRLQGVERIMKKTEESESQVEPEIKRKVQQKRHCSTYQPTPPLSPASKKCLTHLEDLQRNCRQAITLNESTGPLLRTSIHQNSGGQKSQNTGLTTKKFYGNNVEKVPIDIIVNCDDSKHTYLQTNGKVILPGAKIPKITNLKERKTSLSDLNDPIILSSDDDDDNDRTNRRESISPQPADSACSSPAPSTGKVEAALNENTCRAERELRSIPEDSELNTVTLPRKARMKDQFGNSIINTPLKRRKVFSQEPPDALALSCQSSFDSVILNCRSIRVGTLFRLLIEPVIFCLDFIKIQLDEPDHDPVEIILNTSDLTKCEWCNVRKLPVVFLQAIPAVYQKLSIQLQMNKEDKVWNDCKGVNKLTNLEEQYIILIFQNGLDPPANMVFESIINEIGIKNNISNFFAKIPFEEANGRLVACTRTYEESIKGSCGQKENKIKTVSFESKIQLRSKQEFQFFDEEEETGENHTIFIGPVEKLIVYPPPPAKGGISVTNEDLHCLNEGEFLNDVIIDFYLKYLVLEKLKKEDADRIHIFSSFFYKRLNQRERRNHETTNLSIQQKRHGRVKTWTRHVDIFEKDFIFVPLNEAAHWFLAVVCFPGLEKPKYEPNPHYHENAVIQKCSTVEDSCISSSASEMESCSQNSSAKPVIKKMLNKKHCIAVIDSNPGQEESDPRYKRNICSVKYSVKKINHTASENEEFNKGESTSQKVADRTKSENGLQNESLSSTHHTDGLSKIRLNYSDESPEAGKMLEDELVDFSEDQDNQDDSSDDGFLADDNCSSEIGQWHLKPTICKQPCILLMDSLRGPSRSNVVKILREYLEVEWEVKKGSKRSFSKDVMKGSNPKVPQQNNFSDCGVYVLQYVESFFENPILSFELPMNLANWFPPPRMRTKREEIRNIILKLQEDQSKEKRKHKDTYSTEAPLGEGTEQYVNSISD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAAGKSGGSAGEI --CCCCCCCCCHHHH	47.68	19060867
9	Phosphorylation	AAGKSGGSAGEITFL CCCCCCCCHHHHHHH	36.30	19060867
22	Phosphorylation	FLEALARSESKRDGG HHHHHHCCCCCCCCC	40.38	28555341
35	Phosphorylation	GGFKNNWSFDHEEES CCCCCCCCCCCCCCC	23.95	30576142
42	Phosphorylation	SFDHEEESEGDTDKD CCCCCCCCCCCCCCC	50.59	25159151
46	Phosphorylation	EEESEGDTDKDGTNL CCCCCCCCCCCCCCC	56.67	30576142
51	Phosphorylation	GDTDKDGTNLLSVDE CCCCCCCCCCCCCCC	32.59	28985074
55	Phosphorylation	KDGTNLLSVDEDEDS CCCCCCCCCCCCCCC	30.59	22199227
62	Phosphorylation	SVDEDEDSETSKGKK CCCCCCCCCCHHCCC	40.50	26852163
64	Phosphorylation	DEDEDSETSKGKKLN CCCCCCCCHHCCCCC	39.42	26852163
74	Phosphorylation	GKKLNRRSEIVANSS CCCCCCHHEEEECCC	28.56	28555341
80	Phosphorylation	RSEIVANSSGEFILK HHEEEECCCCHHHHH	29.95	28509920
81	Phosphorylation	SEIVANSSGEFILKT HEEEECCCCHHHHHH	41.99	29083192
88	Phosphorylation	SGEFILKTYVRRNKS CCHHHHHHHHHCCCC	24.65	28509920
89	Phosphorylation	GEFILKTYVRRNKSE CHHHHHHHHHCCCCC	7.14	29083192
97	Phosphorylation	VRRNKSESFKTLKGN HHCCCCCCCCCCCCC	38.85	29396449
99	Methylation	RNKSESFKTLKGNPI CCCCCCCCCCCCCCC	63.33	115981551
100	Phosphorylation	NKSESFKTLKGNPIG CCCCCCCCCCCCCCC	31.52	-
102	Methylation	SESFKTLKGNPIGLN CCCCCCCCCCCCCHH	62.97	115981543
124	Phosphorylation	LSENTQNTSLCSGTV CCCCCCCCCCCCCEE	17.17	28555341
125	Phosphorylation	SENTQNTSLCSGTVV CCCCCCCCCCCCEEE	34.62	28555341
189	Sumoylation	GVERIMKKTEESESQ HHHHHHHHHCCCHHH	43.73	-
189	Sumoylation	GVERIMKKTEESESQ HHHHHHHHHCCCHHH	43.73	-
212	Phosphorylation	VQQKRHCSTYQPTPP HHHHCCCCCCCCCCC	24.83	23312004
213	Phosphorylation	QQKRHCSTYQPTPPL HHHCCCCCCCCCCCC	31.41	27794612
214	Phosphorylation	QKRHCSTYQPTPPLS HHCCCCCCCCCCCCC	9.01	28152594
217	Phosphorylation	HCSTYQPTPPLSPAS CCCCCCCCCCCCHHH	23.24	28152594
221	Phosphorylation	YQPTPPLSPASKKCL CCCCCCCCHHHHHHH	24.97	25159151
224	Phosphorylation	TPPLSPASKKCLTHL CCCCCHHHHHHHHHH	35.71	28152594
226	Ubiquitination	PLSPASKKCLTHLED CCCHHHHHHHHHHHH	31.79	-
247	Phosphorylation	QAITLNESTGPLLRT HCHHCCCCCCCCEEC	37.28	28555341
248	Phosphorylation	AITLNESTGPLLRTS CHHCCCCCCCCEECE	36.32	28555341
264	Ubiquitination	HQNSGGQKSQNTGLT ECCCCCCCCCCCCCC	58.23	-
274	Sumoylation	NTGLTTKKFYGNNVE CCCCCCCEECCCCCC	41.55	-
274	Sumoylation	NTGLTTKKFYGNNVE CCCCCCCEECCCCCC	41.55	-
311	Acetylation	KVILPGAKIPKITNL EEEECCCCCCCCCCH	66.51	25953088
319	Ubiquitination	IPKITNLKERKTSLS CCCCCCHHHCCCCHH	58.50	-
323	Phosphorylation	TNLKERKTSLSDLND CCHHHCCCCHHHCCC	40.91	25690035
324	Phosphorylation	NLKERKTSLSDLNDP CHHHCCCCHHHCCCC	28.98	22115753
326	Phosphorylation	KERKTSLSDLNDPII HHCCCCHHHCCCCEE	39.56	22115753
335	Phosphorylation	LNDPIILSSDDDDDN CCCCEECCCCCCCCC	22.70	22617229
336	Phosphorylation	NDPIILSSDDDDDND CCCEECCCCCCCCCC	41.43	27362937
345	Phosphorylation	DDDDNDRTNRRESIS CCCCCCCCCCCCCCC	35.62	23909892
350	Phosphorylation	DRTNRRESISPQPAD CCCCCCCCCCCCCCC	26.93	23401153
352	Phosphorylation	TNRRESISPQPADSA CCCCCCCCCCCCCCC	27.11	19664994
358	Phosphorylation	ISPQPADSACSSPAP CCCCCCCCCCCCCCC	33.03	29255136
361	Phosphorylation	QPADSACSSPAPSTG CCCCCCCCCCCCCCC	38.79	29255136
362	Phosphorylation	PADSACSSPAPSTGK CCCCCCCCCCCCCCC	25.60	29255136
366	Phosphorylation	ACSSPAPSTGKVEAA CCCCCCCCCCCHHHH	52.47	29255136
367	Phosphorylation	CSSPAPSTGKVEAAL CCCCCCCCCCHHHHH	39.71	29255136
378	Phosphorylation	EAALNENTCRAEREL HHHHCCCCHHHHHHH	9.37	23312004
387	Phosphorylation	RAERELRSIPEDSEL HHHHHHHCCCCCCCC	55.94	27135362
396	Phosphorylation	PEDSELNTVTLPRKA CCCCCCCCCCCCCHH	27.73	28555341
398	Phosphorylation	DSELNTVTLPRKARM CCCCCCCCCCCHHHC	29.07	-
406	Sumoylation	LPRKARMKDQFGNSI CCCHHHCHHHCCCCC	42.71	-
406	Sumoylation	LPRKARMKDQFGNSI CCCHHHCHHHCCCCC	42.71	-
412	Phosphorylation	MKDQFGNSIINTPLK CHHHCCCCCCCCCCC	25.81	28450419
416	Phosphorylation	FGNSIINTPLKRRKV CCCCCCCCCCCCCCC	21.42	29255136
419	Sumoylation	SIINTPLKRRKVFSQ CCCCCCCCCCCCCCC	51.89	-
419	Sumoylation	SIINTPLKRRKVFSQ CCCCCCCCCCCCCCC	51.89	-
488	Phosphorylation	PVEIILNTSDLTKCE CEEEEEECCCCCCCC	21.85	21406692
489	Phosphorylation	VEIILNTSDLTKCEW EEEEEECCCCCCCCC	29.56	21406692
492	Phosphorylation	ILNTSDLTKCEWCNV EEECCCCCCCCCCCC	38.34	21406692
534	Ubiquitination	DKVWNDCKGVNKLTN CCHHHCCCCHHHCCC	69.61	-
577	Phosphorylation	IGIKNNISNFFAKIP HCCCCCHHHHHCCCC	29.70	-
582	Acetylation	NISNFFAKIPFEEAN CHHHHHCCCCHHHHC	45.84	26051181
599	Phosphorylation	LVACTRTYEESIKGS EEEEECCHHHHHCCC	17.89	21712546
606	Phosphorylation	YEESIKGSCGQKENK HHHHHCCCCCCCCCC	15.29	25159151
628	Sumoylation	SKIQLRSKQEFQFFD HCCCCCCCCEEECCC	47.62	28112733
711	Phosphorylation	ADRIHIFSSFFYKRL CCCEEEEHHHHHHHH	26.15	28348404
712	Phosphorylation	DRIHIFSSFFYKRLN CCEEEEHHHHHHHHH	14.50	28348404
728	O-linked_Glycosylation	RERRNHETTNLSIQQ HHHHCCCCCCCCHHH	17.27	23301498
736	Ubiquitination	TNLSIQQKRHGRVKT CCCCHHHHHHCCCCE	29.95	-
819	Phosphorylation	ESCSQNSSAKPVIKK HHHCCCCCCHHHHHH	48.11	-
860	Phosphorylation	NICSVKYSVKKINHT CCEEEEEEEECCCCC	23.03	28555341
867	Phosphorylation	SVKKINHTASENEEF EEECCCCCCCCCCCC	27.65	29083192
869	Phosphorylation	KKINHTASENEEFNK ECCCCCCCCCCCCCC	41.95	25159151
876	Acetylation	SENEEFNKGESTSQK CCCCCCCCCCCCHHH	70.18	26051181
879	Phosphorylation	EEFNKGESTSQKVAD CCCCCCCCCHHHHHH	41.86	29083192
880	Phosphorylation	EFNKGESTSQKVADR CCCCCCCCHHHHHHH	30.76	29083192
881	Phosphorylation	FNKGESTSQKVADRT CCCCCCCHHHHHHHH	36.96	29083192
888	Phosphorylation	SQKVADRTKSENGLQ HHHHHHHHHCCCCCC	39.20	29978859
890	Phosphorylation	KVADRTKSENGLQNE HHHHHHHCCCCCCCC	35.36	28555341
898	Phosphorylation	ENGLQNESLSSTHHT CCCCCCCCCCCCCCC	40.89	28555341
900	Phosphorylation	GLQNESLSSTHHTDG CCCCCCCCCCCCCCC	42.33	29449344
910	Acetylation	HHTDGLSKIRLNYSD CCCCCCCEEECCCCC	36.57	23236377
910	Ubiquitination	HHTDGLSKIRLNYSD CCCCCCCEEECCCCC	36.57	-
915	Phosphorylation	LSKIRLNYSDESPEA CCEEECCCCCCCCHH	23.30	23403867
916	Phosphorylation	SKIRLNYSDESPEAG CEEECCCCCCCCHHH	33.55	23927012
919	Phosphorylation	RLNYSDESPEAGKML ECCCCCCCCHHHHCH	32.79	23927012
983	Phosphorylation	MDSLRGPSRSNVVKI EECCCCCCHHHHHHH	51.68	26270265
985	Phosphorylation	SLRGPSRSNVVKILR CCCCCCHHHHHHHHH	38.01	22496350
1008	Phosphorylation	VKKGSKRSFSKDVMK ECCCCCCCCCHHHHC	37.29	24719451
1086	Ubiquitination	QEDQSKEKRKHKDTY HHHHHHHHHCCCCCC	71.17	-
1092	Phosphorylation	EKRKHKDTYSTEAPL HHHCCCCCCCCCCCC	24.95	21406692
1093	Phosphorylation	KRKHKDTYSTEAPLG HHCCCCCCCCCCCCC	24.59	21406692
1094	Phosphorylation	RKHKDTYSTEAPLGE HCCCCCCCCCCCCCC	23.12	21406692
1095	Phosphorylation	KHKDTYSTEAPLGEG CCCCCCCCCCCCCCC	26.25	21406692
1103	Phosphorylation	EAPLGEGTEQYVNSI CCCCCCCHHHHHHHC	18.66	27251275
1106	Phosphorylation	LGEGTEQYVNSISD- CCCCHHHHHHHCCC-	8.72	30576142
1109	Phosphorylation	GTEQYVNSISD---- CHHHHHHHCCC----	17.27	23663014
1111	Phosphorylation	EQYVNSISD------ HHHHHHCCC------	36.77	25159151

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of SENP6_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SENP6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of SENP6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT5_HUMAN	KAT5	physical	17704809
SUMO1_HUMAN	SUMO1	physical	21148299
SUMO2_HUMAN	SUMO2	physical	21148299
PA2GA_HUMAN	PLA2G2A	physical	22118674
ZDBF2_HUMAN	ZDBF2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SENP6_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND MASSSPECTROMETRY.	19413330 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-336; SER-350;SER-352 AND SER-361, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-336, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-919, AND MASSSPECTROMETRY.	15302935 [Abstract]