dbPTM

UBP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBP1_HUMAN
UniProt AC	O94782
Protein Name	Ubiquitin carboxyl-terminal hydrolase 1
Gene Name	USP1
Organism	Homo sapiens (Human).
Sequence Length	785
Subcellular Localization	Nucleus .
Protein Description	Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2. [PubMed: 15694335 Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA]
Protein Sequence	MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQVVPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKKEALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPKEEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQTRSKRKATSDTLESPPKIIPKYISENESPRPSQKKSRVKINWLKSATKQPSILSKFCSLGKITTNQGVKGQSKENECDPEEDLGKCESDNTTNGCGLESPGNTVTPVNVNEVKPINKGEEQIGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKVTDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGVVENYNDEEVSIRVGGNTQPSKVLNKKNVEAIGLLGGQKSKADYELYNKASNPDKVASTAFAENRNSETSDTTGTHESDRNKESSDQTGINISGFENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLLFYKKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MPGVIPSESNGLSR -CCCCCCCCCCCCCC	42.40	23927012
9	Phosphorylation	PGVIPSESNGLSRGS CCCCCCCCCCCCCCC	40.30	23401153
13	Phosphorylation	PSESNGLSRGSPSKK CCCCCCCCCCCCCCC	35.67	23401153
16	Phosphorylation	SNGLSRGSPSKKNRL CCCCCCCCCCCCCCC	25.53	25159151
18	Phosphorylation	GLSRGSPSKKNRLSL CCCCCCCCCCCCCCH	58.94	30108239
33	Phosphorylation	KFFQKKETKRALDFT HHHCHHHHHHHCCCC	34.41	-
40	Phosphorylation	TKRALDFTDSQENEE HHHHCCCCCCHHHHH	34.11	27732954
42	Phosphorylation	RALDFTDSQENEEKA HHCCCCCCHHHHHHH	36.01	17525332
48	Ubiquitination	DSQENEEKASEYRAS CCHHHHHHHHHHHHH	51.54	24816145
50	Phosphorylation	QENEEKASEYRASEI HHHHHHHHHHHHHHH	46.35	23312004
52	Phosphorylation	NEEKASEYRASEIDQ HHHHHHHHHHHHHHH	14.69	23312004
55	Phosphorylation	KASEYRASEIDQVVP HHHHHHHHHHHHHCC	26.53	22167270
66	Phosphorylation	QVVPAAQSSPINCEK HHCCHHHCCCCCCCH	33.10	23401153
67	Phosphorylation	VVPAAQSSPINCEKR HCCHHHCCCCCCCHH	20.09	29255136
73	Ubiquitination	SSPINCEKRENLLPF CCCCCCCHHCCCCCC	68.18	21963094
110	Ubiquitination	PGFKSGVKHLFNIIS CCHHHHHHHHHHHHH	37.81	29967540
124	Sumoylation	SRKKEALKDEANQKD HHHHHHHHHHHHHHC	61.65	-
124	Sumoylation	SRKKEALKDEANQKD HHHHHHHHHHHHHHC	61.65	-
130	Acetylation	LKDEANQKDKGNCKE HHHHHHHHCCCCCCH	62.30	19828857
224	Ubiquitination	LLKKEEVKNVAELPT HHCHHHHCCHHHCCC	49.32	29967540
232	Sumoylation	NVAELPTKVEEIPHP CHHHCCCCHHHCCCC	45.79	-
232	Ubiquitination	NVAELPTKVEEIPHP CHHHCCCCHHHCCCC	45.79	29967540
232	Sumoylation	NVAELPTKVEEIPHP CHHHCCCCHHHCCCC	45.79	-
248	Phosphorylation	EEMNGINSIEMDSMR HHHCCCCCCCHHHHC	20.29	20068231
253	Phosphorylation	INSIEMDSMRHSEDF CCCCCHHHHCCCHHH	19.19	26074081
257	Phosphorylation	EMDSMRHSEDFKEKL CHHHHCCCHHHHHHC	28.61	26074081
273	Phosphorylation	KGNGKRKSDTEFGNM CCCCCCCCCCCCHHH	54.52	28985074
275	Phosphorylation	NGKRKSDTEFGNMKK CCCCCCCCCCHHHHH	40.06	29449344
283	Ubiquitination	EFGNMKKKVKLSKEH CCHHHHHHHHHCHHH	38.80	-
285	Ubiquitination	GNMKKKVKLSKEHQS HHHHHHHHHCHHHHH	56.79	-
292	Phosphorylation	KLSKEHQSLEENQRQ HHCHHHHHHHHHHHH	39.39	30576142
307	Phosphorylation	TRSKRKATSDTLESP HHHHHHHCCCCCCCC	30.12	23684312
308	Phosphorylation	RSKRKATSDTLESPP HHHHHHCCCCCCCCC	33.20	30576142
310	Phosphorylation	KRKATSDTLESPPKI HHHHCCCCCCCCCCC	31.99	27794612
313	Phosphorylation	ATSDTLESPPKIIPK HCCCCCCCCCCCCCH	50.00	29255136
321	Phosphorylation	PPKIIPKYISENESP CCCCCCHHCCCCCCC	12.34	29396449
323	Phosphorylation	KIIPKYISENESPRP CCCCHHCCCCCCCCC	31.14	25262027
327	Phosphorylation	KYISENESPRPSQKK HHCCCCCCCCCCCCC	37.48	22167270
331	Phosphorylation	ENESPRPSQKKSRVK CCCCCCCCCCCCHHH	56.78	22167270
343	Ubiquitination	RVKINWLKSATKQPS HHHHHHHHHHCCCCC	29.65	29967540
344	Phosphorylation	VKINWLKSATKQPSI HHHHHHHHHCCCCCH	38.71	26074081
346	Phosphorylation	INWLKSATKQPSILS HHHHHHHCCCCCHHH	36.98	26074081
347	Acetylation	NWLKSATKQPSILSK HHHHHHCCCCCHHHH	60.99	25953088
350	Phosphorylation	KSATKQPSILSKFCS HHHCCCCCHHHHHHH	33.40	29978859
353	Phosphorylation	TKQPSILSKFCSLGK CCCCCHHHHHHHCCC	23.24	26074081
360	Acetylation	SKFCSLGKITTNQGV HHHHHCCCCCCCCCC	42.02	25953088
360	Ubiquitination	SKFCSLGKITTNQGV HHHHHCCCCCCCCCC	42.02	-
368	Ubiquitination	ITTNQGVKGQSKENE CCCCCCCCCCCCCCC	59.04	29967540
387	Phosphorylation	EDLGKCESDNTTNGC HHHCCCCCCCCCCCC	45.70	26074081
390	Phosphorylation	GKCESDNTTNGCGLE CCCCCCCCCCCCCCC	26.99	23663014
391	Phosphorylation	KCESDNTTNGCGLES CCCCCCCCCCCCCCC	35.55	23663014
398	Phosphorylation	TNGCGLESPGNTVTP CCCCCCCCCCCEECC	43.05	23663014
402	Phosphorylation	GLESPGNTVTPVNVN CCCCCCCEECCCCHH	31.50	25850435
404	Phosphorylation	ESPGNTVTPVNVNEV CCCCCEECCCCHHHC	21.34	26074081
457	Phosphorylation	REDFQDISVPVQEDE HHHHCCCCCCCCHHH	28.76	29978859
466	Phosphorylation	PVQEDELSKVEESSE CCCHHHHHCHHCCCC	32.38	28464451
471	Phosphorylation	ELSKVEESSEISPEP HHHCHHCCCCCCCCC	21.55	30266825
472	Phosphorylation	LSKVEESSEISPEPK HHCHHCCCCCCCCCC	42.08	30266825
475	Phosphorylation	VEESSEISPEPKTEM HHCCCCCCCCCCHHH	21.11	29255136
483	Ubiquitination	PEPKTEMKTLRWAIS CCCCHHHHHHHHHHH	37.87	-
503	Ubiquitination	ERIVGEDKYFCENCH HHHHCCCCEECCCCC	35.60	-
523	Ubiquitination	ERSLLFDKMPEVITI HHHHHHCCCCCEEEE	49.36	-
529	Phosphorylation	DKMPEVITIHLKCFA CCCCCEEEEEEHHHH	13.91	20068231
551	Ubiquitination	CYGGGLSKINTPLLT EECCCHHCCCCCCCC	45.05	21963094
554	Phosphorylation	GGLSKINTPLLTPLK CCHHCCCCCCCCCCE	20.84	29978859
558	Phosphorylation	KINTPLLTPLKLSLE CCCCCCCCCCEECHH	33.97	29978859
610	Ubiquitination	LNSLELDKGNFVVDQ CCCCCCCCCCEEEEC	69.27	29967540
623	Ubiquitination	DQMCEIGKPEPLNEE ECCCCCCCCCCCCHH	52.44	29967540
656	Ubiquitination	GGNTQPSKVLNKKNV CCCCCCCCCCCCCCH	58.38	29967540
675	Ubiquitination	LLGGQKSKADYELYN ECCCCCCHHHHHHHH	52.92	29967540
678	Phosphorylation	GQKSKADYELYNKAS CCCCHHHHHHHHHCC	16.82	-
681	Phosphorylation	SKADYELYNKASNPD CHHHHHHHHHCCCHH	11.59	-
683	Ubiquitination	ADYELYNKASNPDKV HHHHHHHHCCCHHHH	39.37	29967540
689	Ubiquitination	NKASNPDKVASTAFA HHCCCHHHHHHHHHH	40.74	21963094
689	Acetylation	NKASNPDKVASTAFA HHCCCHHHHHHHHHH	40.74	26051181
716	Acetylation	THESDRNKESSDQTG CCHHHCCCCCCCCCC	60.92	19814743
716	Ubiquitination	THESDRNKESSDQTG CCHHHCCCCCCCCCC	60.92	29967540
722	Phosphorylation	NKESSDQTGINISGF CCCCCCCCCCCCHHH	45.05	29978859
727	Phosphorylation	DQTGINISGFENKIS CCCCCCCHHHHHHHH	32.70	25159151
732	Ubiquitination	NISGFENKISYVVQS CCHHHHHHHHHHHHH	26.32	32015554
741	Ubiquitination	SYVVQSLKEYEGKWL HHHHHHHHHHCCEEE	64.59	21906983
746	Ubiquitination	SLKEYEGKWLLFDDS HHHHHCCEEEEECCC	23.80	22817900
756	Ubiquitination	LFDDSEVKVTEEKDF EECCCCCEEEECHHH	39.11	22817900
761	Ubiquitination	EVKVTEEKDFLNSLS CCEEEECHHHHHHCC	47.77	21906983
766	Phosphorylation	EEKDFLNSLSPSTSP ECHHHHHHCCCCCCC	32.16	22199227
768	Phosphorylation	KDFLNSLSPSTSPTS HHHHHHCCCCCCCCC	19.34	22199227
770	Phosphorylation	FLNSLSPSTSPTSTP HHHHCCCCCCCCCCC	37.83	22199227
771	Phosphorylation	LNSLSPSTSPTSTPY HHHCCCCCCCCCCCE	41.95	22199227
772	Phosphorylation	NSLSPSTSPTSTPYL HHCCCCCCCCCCCEE	30.44	22199227
774	Phosphorylation	LSPSTSPTSTPYLLF CCCCCCCCCCCEEEE	45.03	22199227
775	Phosphorylation	SPSTSPTSTPYLLFY CCCCCCCCCCEEEEE	30.67	22199227
776	Phosphorylation	PSTSPTSTPYLLFYK CCCCCCCCCEEEEEE	20.59	23090842
778	Phosphorylation	TSPTSTPYLLFYKKL CCCCCCCEEEEEECC	19.00	23090842
782	Phosphorylation	STPYLLFYKKL---- CCCEEEEEECC----	13.74	23090842
783	Ubiquitination	TPYLLFYKKL----- CCEEEEEECC-----	40.02	21890473

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
313	S	Phosphorylation	Kinase	CDK1	P06493	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:21768287

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBP1_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 UBP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CALL3_HUMAN	CALML3	physical	19615732
DSC1_HUMAN	DSC1	physical	19615732
DSG1_HUMAN	DSG1	physical	19615732
FILA_HUMAN	FLG	physical	19615732
HSPB1_HUMAN	HSPB1	physical	19615732
PLAK_HUMAN	JUP	physical	19615732
IMA5_HUMAN	KPNA1	physical	19615732
K1C17_HUMAN	KRT17	physical	19615732
LEG7_HUMAN	LGALS7	physical	19615732
LYSC_HUMAN	LYZ	physical	19615732
MYH9_HUMAN	MYH9	physical	19615732
PKP1_HUMAN	PKP1	physical	19615732
UBP4_HUMAN	USP4	physical	19615732
TAGL2_HUMAN	TAGLN2	physical	19615732
PHLP1_HUMAN	PHLPP1	physical	19615732
CALL5_HUMAN	CALML5	physical	19615732
WDR48_HUMAN	WDR48	physical	19615732
A16A1_HUMAN	ALDH16A1	physical	19615732
FACD2_HUMAN	FANCD2	physical	15694335
UBP1_HUMAN	USP1	physical	20147293
ATAD5_HUMAN	ATAD5	physical	20147293
WDR48_HUMAN	WDR48	physical	20147293
WDR48_HUMAN	WDR48	physical	18082604
FACD2_HUMAN	FANCD2	physical	18082604
PCNA_HUMAN	PCNA	physical	16531995
ID2_HUMAN	ID2	physical	21925315
UBC_HUMAN	UBC	physical	22195557
PCNA_HUMAN	PCNA	physical	22989887
PCNA_HUMAN	PCNA	physical	22987070
PHLP1_HUMAN	PHLPP1	physical	22426999
VP26A_HUMAN	VPS26A	physical	22939629
WDR5_HUMAN	WDR5	physical	22939629
UN45A_HUMAN	UNC45A	physical	22939629
VPS36_HUMAN	VPS36	physical	22939629
XPO2_HUMAN	CSE1L	physical	22939629
WDR48_HUMAN	WDR48	physical	23116119
WDR48_HUMAN	WDR48	physical	22701671
TRAF6_HUMAN	TRAF6	physical	23105109
PHF7_HUMAN	PHF7	physical	23105109
TRI46_HUMAN	TRIM46	physical	23105109
DTX3_HUMAN	DTX3	physical	23105109
WDR48_HUMAN	WDR48	physical	19075014
FZR1_HUMAN	FZR1	physical	21768287
WDR48_HUMAN	WDR48	physical	25744535
WDR48_HUMAN	WDR48	physical	26388029
WDR48_HUMAN	WDR48	physical	27463890
PHLP1_HUMAN	PHLPP1	physical	27463890
PHLP2_HUMAN	PHLPP2	physical	27463890
R51A1_HUMAN	RAD51AP1	physical	27463890
STAT2_HUMAN	STAT2	physical	28514442
WDR48_HUMAN	WDR48	physical	28514442
PHLP1_HUMAN	PHLPP1	physical	28514442
LRC15_HUMAN	LRRC15	physical	28514442
UBE2K_HUMAN	UBE2K	physical	28270494

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 UBP1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-67; SER-313 AND SER-475,AND MASS SPECTROMETRY.	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-67, AND MASSSPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASSSPECTROMETRY.	17924679 [Abstract]