dbPTM

UBP42_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP42_HUMAN
UniProt AC	Q9H9J4
Protein Name	Ubiquitin carboxyl-terminal hydrolase 42
Gene Name	USP42
Organism	Homo sapiens (Human).
Sequence Length	1324
Subcellular Localization
Protein Description	Deubiquitinating enzyme which may play an important role during spermatogenesis..
Protein Sequence	MTIVDKASESSDPSAYQNQPGSSEAVSPGDMDAGSASWGAVSSLNDVSNHTLSLGPVPGAVVYSSSSVPDKSKPSPQKDQALGDGIAPPQKVLFPSEKICLKWQQTHRVGAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSHDVKNGGELTHPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNPPHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNASASVQNWSVNRSSVIPEHPKKQKITISIHNKLPVRQCQSQPNLHSNSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKVTKPIPRSESCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKENGIGTIVSSHSPGQDAEDEEATPHELQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKLMPAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSHHHSRHRSGVELDWVRHHYTEGERGWGREKFYPDRPRWDRCRYYHDRYALYAARDWKPFHGGREHERAGLHERPHKDHNRGRRGCEPARERERHRPSSPRAGAPHALAPHPDRFSHDRTALVAGDNCNLSDRFHEHENGKSRKRRHDSVENSDSHVEKKARRSEQKDPLEEPKAKKHKKSKKKKKSKDKHRDRDSRHQQDSDLSAACSDADLHRHKKKKKKKKRHSRKSEDFVKDSELHLPRVTSLETVAQFRRAQGGFPLSGGPPLEGVGPFREKTKHLRMESRDDRCRLFEYGQGKRRYLELGR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	Phosphorylation	PVPGAVVYSSSSVPD CCCCEEEEECCCCCC	9.02	-
72	Phosphorylation	SSSVPDKSKPSPQKD CCCCCCCCCCCCHHH	58.12	23927012
75	Phosphorylation	VPDKSKPSPQKDQAL CCCCCCCCCHHHCCC	43.64	23401153
91	Ubiquitination	DGIAPPQKVLFPSEK CCCCCCCEEEECCHH	46.83	29967540
158	Phosphorylation	EGFCMMCTMQAHITQ CCCHHHHHHHHHHHH	8.40	26552605
164	Phosphorylation	CTMQAHITQALSNPG HHHHHHHHHHHHCCC	9.64	26552605
168	Phosphorylation	AHITQALSNPGDVIK HHHHHHHHCCCCCCH	43.95	26552605
173	Ubiquitination	ALSNPGDVIKPMFVI HHHCCCCCCHHHHHH	8.21	21890473
181	Ubiquitination	IKPMFVINEMRRIAR CHHHHHHHHHHHHHH	31.54	21890473
216	Ubiquitination	MQKACLNGSNKLDRH HHHHHHCCCCCCCHH	21.46	21890473
237	Phosphorylation	VCQIFGGYLRSRVKC HHHHHHHHHHHCEEE	10.18	-
279	Ubiquitination	KALEQFVKPEQLDGE HHHHHHCCHHHCCCC	44.09	29967540
288	Phosphorylation	EQLDGENSYKCSKCK HHCCCCCCEECCCCC	22.97	-
289	Phosphorylation	QLDGENSYKCSKCKK HCCCCCCEECCCCCC	27.82	-
327	Ubiquitination	FANFTGGKIAKDVKY HHHCCCCCCCCCCCC	40.61	21890473
327	Ubiquitination	FANFTGGKIAKDVKY HHHCCCCCCCCCCCC	40.61	21890473
327	Acetylation	FANFTGGKIAKDVKY HHHCCCCCCCCCCCC	40.61	25953088
327	Ubiquitination	FANFTGGKIAKDVKY HHHCCCCCCCCCCCC	40.61	27667366
330	Ubiquitination	FTGGKIAKDVKYPEY CCCCCCCCCCCCCHH	67.53	-
422	Phosphorylation	VKNGGELTHPTHSPG CCCCCCCCCCCCCCC	22.85	20873877
425	Phosphorylation	GGELTHPTHSPGQSS CCCCCCCCCCCCCCC	27.64	30266825
427	Phosphorylation	ELTHPTHSPGQSSPR CCCCCCCCCCCCCCC	32.95	30266825
431	Phosphorylation	PTHSPGQSSPRPVIS CCCCCCCCCCCCEEE	48.50	30266825
432	Phosphorylation	THSPGQSSPRPVISQ CCCCCCCCCCCEEEE	19.62	30266825
438	Phosphorylation	SSPRPVISQRVVTNK CCCCCEEEEEEEECC	16.50	30266825
470	Phosphorylation	NPPHLNGTGPLKDTP CCCCCCCCCCCCCCC	34.26	26437602
479	Phosphorylation	PLKDTPSSSMSSPNG CCCCCCCCCCCCCCC	31.12	21815630
480	Phosphorylation	LKDTPSSSMSSPNGN CCCCCCCCCCCCCCC	27.33	21815630
482	Phosphorylation	DTPSSSMSSPNGNSS CCCCCCCCCCCCCCC	44.59	23186163
483	Phosphorylation	TPSSSMSSPNGNSSV CCCCCCCCCCCCCCC	17.47	21815630
494	Phosphorylation	NSSVNRASPVNASAS CCCCCCCCCCCCCCE	26.58	21815630
499	Phosphorylation	RASPVNASASVQNWS CCCCCCCCCEEECCC	18.84	21815630
501	Phosphorylation	SPVNASASVQNWSVN CCCCCCCEEECCCCC	23.03	27732954
585	Phosphorylation	VTKPIPRSESCSQPV CCCCCCCCCCCCCCC	28.62	27251275
587	Phosphorylation	KPIPRSESCSQPVMN CCCCCCCCCCCCCCC	21.95	27251275
589	Phosphorylation	IPRSESCSQPVMNGK CCCCCCCCCCCCCCC	46.96	27251275
601	Phosphorylation	NGKSKLNSSVLVPYG CCCCCCCCCEEEECC	32.06	20873877
602	Phosphorylation	GKSKLNSSVLVPYGA CCCCCCCCEEEECCC	20.56	20873877
607	Phosphorylation	NSSVLVPYGAESSED CCCEEEECCCCCCCC	22.84	22115753
611	Phosphorylation	LVPYGAESSEDSDEE EEECCCCCCCCCHHH	38.19	26503892
612	Phosphorylation	VPYGAESSEDSDEES EECCCCCCCCCHHHH	36.61	26503892
615	Phosphorylation	GAESSEDSDEESKGL CCCCCCCCHHHHCCC	42.76	26503892
619	Phosphorylation	SEDSDEESKGLGKEN CCCCHHHHCCCCCCC	29.94	25159151
630	Phosphorylation	GKENGIGTIVSSHSP CCCCCCCEEEECCCC	19.11	23898821
633	Phosphorylation	NGIGTIVSSHSPGQD CCCCEEEECCCCCCC	20.62	28348404
634	Phosphorylation	GIGTIVSSHSPGQDA CCCEEEECCCCCCCC	19.65	28348404
636	Phosphorylation	GTIVSSHSPGQDAED CEEEECCCCCCCCCC	32.45	22210691
656	Phosphorylation	HELQEPMTLNGANSA HHCCCCCCCCCCCCC	27.99	22210691
665	Phosphorylation	NGANSADSDSDPKEN CCCCCCCCCCCCCCC	38.44	22210691
702	Acetylation	KANGLPGKLMPAPLL HHCCCCCCCCCCCCC	39.41	25953088
729	Phosphorylation	LSNKLKGSTDEMSAP HHHCCCCCCCCCCCC	30.97	30377224
730	Phosphorylation	SNKLKGSTDEMSAPG HHCCCCCCCCCCCCC	44.65	30377224
734	Phosphorylation	KGSTDEMSAPGAERG CCCCCCCCCCCHHCC	29.30	30576142
754	Phosphorylation	DAEPQPGSPAAESLE CCCCCCCCCHHHHCC	20.32	29255136
759	Phosphorylation	PGSPAAESLEEPDAA CCCCHHHHCCCCCHH	36.03	23401153
770	Phosphorylation	PDAAAGLSSTKKAPP CCHHCCCCCCCCCCC	34.74	25850435
771	Phosphorylation	DAAAGLSSTKKAPPP CHHCCCCCCCCCCCC	49.65	25850435
772	Phosphorylation	AAAGLSSTKKAPPPR HHCCCCCCCCCCCCC	32.94	25850435
783	Phosphorylation	PPPRDPGTPATKEGA CCCCCCCCCCCCCCC	18.35	30266825
786	Phosphorylation	RDPGTPATKEGAWEA CCCCCCCCCCCCCEE	30.72	30266825
823	Phosphorylation	PDLCDPGSLTGDASP CCCCCCCCCCCCCCC	28.31	21406692
825	Phosphorylation	LCDPGSLTGDASPLS CCCCCCCCCCCCCCC	34.41	21406692
829	Phosphorylation	GSLTGDASPLSQDAK CCCCCCCCCCCCCCC	30.98	20068231
832	Phosphorylation	TGDASPLSQDAKGMI CCCCCCCCCCCCCHH	29.42	20068231
846	Phosphorylation	IAEGPRDSALAEAPE HCCCCCCHHHHHCCC	26.85	26552605
856	Phosphorylation	AEAPEGLSPAPPARS HHCCCCCCCCCCCCC	29.85	29255136
863	Phosphorylation	SPAPPARSEEPCEQP CCCCCCCCCCCCCCC	48.71	26074081
876	Phosphorylation	QPLLVHPSGDHARDA CCEEECCCCCCCCCC	41.81	26074081
919	Phosphorylation	PEGDAEPSPGERVED CCCCCCCCCCCCHHH	36.72	30266825
936	Phosphorylation	APKAPGPSPAKEKIG CCCCCCCCCHHHHHH	43.32	30266825
944	Phosphorylation	PAKEKIGSLRKVDRG CHHHHHHCCEECCCC	28.59	24719451
953	Phosphorylation	RKVDRGHYRSRRERS EECCCCCCCCHHHCC	17.07	17192257
960	Phosphorylation	YRSRRERSSSGEPAR CCCHHHCCCCCCCCC	24.89	30177828
961	Phosphorylation	RSRRERSSSGEPARE CCHHHCCCCCCCCCH	48.89	30177828
962	Phosphorylation	SRRERSSSGEPARES CHHHCCCCCCCCCHH	48.71	30177828
983	Phosphorylation	HRHRRRRTCPRERDR HHHHHHCCCCCHHHC	25.67	23532336
1007	Phosphorylation	PGHGDRLSPGERRSL CCCCCCCCHHCCCCC	31.58	26503892
1026	Phosphorylation	HHHSRHRSGVELDWV CCCHHCCCCCCEEEH	40.85	24247654
1066	Phosphorylation	CRYYHDRYALYAARD HHHHHHHHHHHHCCC	13.66	21712546
1069	Phosphorylation	YHDRYALYAARDWKP HHHHHHHHHCCCCCC	7.05	21447384
1115	Phosphorylation	ERERHRPSSPRAGAP HHHHCCCCCCCCCCC	53.59	20068231
1116	Phosphorylation	RERHRPSSPRAGAPH HHHCCCCCCCCCCCC	22.53	20068231
1133	Phosphorylation	APHPDRFSHDRTALV CCCCCCCCCCCEEEE	25.93	30266825
1148	Phosphorylation	AGDNCNLSDRFHEHE ECCCCCCHHHHHCCC	16.85	21815630
1166	Phosphorylation	SRKRRHDSVENSDSH CCCCCHHCCCCCHHH	25.79	30266825
1170	Phosphorylation	RHDSVENSDSHVEKK CHHCCCCCHHHHHHH	27.30	30266825
1172	Phosphorylation	DSVENSDSHVEKKAR HCCCCCHHHHHHHHH	29.29	30266825
1181	Phosphorylation	VEKKARRSEQKDPLE HHHHHHHHHCCCCCC	38.53	23401153
1184	Acetylation	KARRSEQKDPLEEPK HHHHHHCCCCCCCHH	58.21	7296969
1191	Acetylation	KDPLEEPKAKKHKKS CCCCCCHHHHHHHHH	75.91	7296979
1191	Ubiquitination	KDPLEEPKAKKHKKS CCCCCCHHHHHHHHH	75.91	-
1193	Ubiquitination	PLEEPKAKKHKKSKK CCCCHHHHHHHHHHH	62.63	-
1194	Ubiquitination	LEEPKAKKHKKSKKK CCCHHHHHHHHHHHH	66.57	-
1198	Phosphorylation	KAKKHKKSKKKKKSK HHHHHHHHHHHHHHH	55.28	26657352
1204	Phosphorylation	KSKKKKKSKDKHRDR HHHHHHHHHHHHCCH	55.77	26657352
1213	Phosphorylation	DKHRDRDSRHQQDSD HHHCCHHHHHHHHHH	32.34	-
1219	Phosphorylation	DSRHQQDSDLSAACS HHHHHHHHHHHHHCC	35.79	29255136
1220	Phosphorylation	SRHQQDSDLSAACSD HHHHHHHHHHHHCCH	53.59	18669648
1222	Phosphorylation	HQQDSDLSAACSDAD HHHHHHHHHHCCHHH	20.86	29255136
1223	Phosphorylation	QQDSDLSAACSDADL HHHHHHHHHCCHHHH	21.56	18669648
1226	Phosphorylation	SDLSAACSDADLHRH HHHHHHCCHHHHHHH	30.98	29255136
1227	Phosphorylation	DLSAACSDADLHRHK HHHHHCCHHHHHHHH	43.94	18669648
1244	Phosphorylation	KKKKKRHSRKSEDFV HHHHHHHCCCHHHHH	45.49	30108239
1247	Phosphorylation	KKRHSRKSEDFVKDS HHHHCCCHHHHHHHH	41.09	30266825
1254	Phosphorylation	SEDFVKDSELHLPRV HHHHHHHHCCCCCCC	36.02	23312004
1262	Phosphorylation	ELHLPRVTSLETVAQ CCCCCCCCCHHHHHH	28.95	30108239
1263	Phosphorylation	LHLPRVTSLETVAQF CCCCCCCCHHHHHHH	22.73	27499020
1266	Phosphorylation	PRVTSLETVAQFRRA CCCCCHHHHHHHHHH	26.83	30108239
1280	Phosphorylation	AQGGFPLSGGPPLEG HCCCCCCCCCCCCCC	41.77	20068231

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 UBP42_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBP42_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 UBP42_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAH2_HUMAN	CA2	physical	19615732
HEMH_HUMAN	FECH	physical	19615732
IMA4_HUMAN	KPNA3	physical	19615732
PLRG1_HUMAN	PLRG1	physical	19615732
CPNE3_HUMAN	CPNE3	physical	19615732
HERC2_HUMAN	HERC2	physical	19615732
BMS1_HUMAN	BMS1	physical	19615732
RANB9_HUMAN	RANBP9	physical	19615732
RAD50_HUMAN	RAD50	physical	19615732
RT31_HUMAN	MRPS31	physical	19615732
SAHH2_HUMAN	AHCYL1	physical	19615732
SRRM2_HUMAN	SRRM2	physical	19615732
DIM1_HUMAN	DIMT1	physical	19615732
RT21_HUMAN	MRPS21	physical	19615732
TEX10_HUMAN	TEX10	physical	19615732
WDR18_HUMAN	WDR18	physical	19615732
LRC47_HUMAN	LRRC47	physical	19615732
RT35_HUMAN	MRPS35	physical	19615732
RT14_HUMAN	MRPS14	physical	19615732
YTDC2_HUMAN	YTHDC2	physical	19615732
RT26_HUMAN	MRPS26	physical	19615732
RT34_HUMAN	MRPS34	physical	19615732
RIOX1_HUMAN	C14orf169	physical	19615732
AMOT_HUMAN	AMOT	physical	19615732
P53_HUMAN	TP53	physical	22085928
MDM2_HUMAN	MDM2	physical	22085928
H2B2E_HUMAN	HIST2H2BE	physical	25336640
ZEB1_HUMAN	ZEB1	physical	29119051

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 UBP42_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-856, 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-856, 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-856; SER-1219; SER-1222AND SER-1226, 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-856 AND SER-1226, 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-754 AND SER-856, ANDMASS SPECTROMETRY.	15302935 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-953, AND MASSSPECTROMETRY.	18691976 [Abstract]