dbPTM

OCAD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	OCAD1_HUMAN
UniProt AC	Q9NX40
Protein Name	OCIA domain-containing protein 1
Gene Name	OCIAD1 {ECO:0000312\|HGNC:HGNC:16074}
Organism	Homo sapiens (Human).
Sequence Length	245
Subcellular Localization	Endosome .
Protein Description	Maintains stem cell potency (By similarity). Increases STAT3 phosphorylation and controls ERK phosphorylation (By similarity). May act as a scaffold, increasing STAT3 recruitment onto endosomes (By similarity). Involved in integrin-mediated cancer cell adhesion and colony formation in ovarian cancer. [PubMed: 20515946]
Protein Sequence	MNGRADFREPNAEVPRPIPHIGPDYIPTEEERRVFAECNDESFWFRSVPLAATSMLITQGLISKGILSSHPKYGSIPKLILACIMGYFAGKLSYVKTCQEKFKKLENSPLGEALRSGQARRSSPPGHYYQKSKYDSSVSGQSSFVTSPAADNIEMLPHYEPIPFSSSMNESAPTGITDHIVQGPDPNLEESPKRKNITYEELRNKNRESYEVSLTQKTDPSVRPMHERVPKKEVKVNKYGDTWDE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Phosphorylation	IPHIGPDYIPTEEER CCCCCCCCCCCHHHH	16.37	24248375
28	Phosphorylation	IGPDYIPTEEERRVF CCCCCCCCHHHHHHH	46.61	24248375
47	Phosphorylation	DESFWFRSVPLAATS CCCCHHHCCHHHHHH	20.72	20068231
47 (in isoform 2)	Phosphorylation	-	20.72	-
53	Phosphorylation	RSVPLAATSMLITQG HCCHHHHHHHHHHHH	14.73	24043423
54	Phosphorylation	SVPLAATSMLITQGL CCHHHHHHHHHHHHH	13.58	20068231
58	Phosphorylation	AATSMLITQGLISKG HHHHHHHHHHHHHCH	16.78	20068231
63	Phosphorylation	LITQGLISKGILSSH HHHHHHHHCHHHHCC	29.85	20068231
63 (in isoform 2)	Phosphorylation	-	29.85	-
69	Phosphorylation	ISKGILSSHPKYGSI HHCHHHHCCCCCCCH	40.12	23911959
72 (in isoform 2)	Ubiquitination	-	57.74	21890473
72 (in isoform 1)	Ubiquitination	-	57.74	21890473
72	Ubiquitination	GILSSHPKYGSIPKL HHHHCCCCCCCHHHH	57.74	21890473
72	Acetylation	GILSSHPKYGSIPKL HHHHCCCCCCCHHHH	57.74	25825284
72	Ubiquitination	GILSSHPKYGSIPKL HHHHCCCCCCCHHHH	57.74	21890473
75	Phosphorylation	SSHPKYGSIPKLILA HCCCCCCCHHHHHHH	32.40	24719451
96	Ubiquitination	AGKLSYVKTCQEKFK HHHHHHHHHHHHHHH	35.04	19608861
96	Acetylation	AGKLSYVKTCQEKFK HHHHHHHHHHHHHHH	35.04	25953088
96	Sumoylation	AGKLSYVKTCQEKFK HHHHHHHHHHHHHHH	35.04	-
96	Sumoylation	AGKLSYVKTCQEKFK HHHHHHHHHHHHHHH	35.04	19608861
96 (in isoform 2)	Acetylation	-	35.04	-
101	Acetylation	YVKTCQEKFKKLENS HHHHHHHHHHHHCCC	36.28	25953088
104	Ubiquitination	TCQEKFKKLENSPLG HHHHHHHHHCCCHHH	65.25	-
108	Phosphorylation	KFKKLENSPLGEALR HHHHHCCCHHHHHHH	16.48	19664994
108 (in isoform 2)	Phosphorylation	-	16.48	-
116	Phosphorylation	PLGEALRSGQARRSS HHHHHHHHCCCCCCC	35.79	25159151
116 (in isoform 2)	Phosphorylation	-	35.79	-
122	Phosphorylation	RSGQARRSSPPGHYY HHCCCCCCCCCCCCC	41.46	22167270
122 (in isoform 2)	Phosphorylation	-	41.46	-
123	Phosphorylation	SGQARRSSPPGHYYQ HCCCCCCCCCCCCCC	33.05	22167270
123 (in isoform 2)	Phosphorylation	-	33.05	-
128	Phosphorylation	RSSPPGHYYQKSKYD CCCCCCCCCCCCCCC	17.32	23927012
129	Phosphorylation	SSPPGHYYQKSKYDS CCCCCCCCCCCCCCC	12.09	23927012
131	Ubiquitination	PPGHYYQKSKYDSSV CCCCCCCCCCCCCCC	32.56	-
131	Acetylation	PPGHYYQKSKYDSSV CCCCCCCCCCCCCCC	32.56	92373
132	Phosphorylation	PGHYYQKSKYDSSVS CCCCCCCCCCCCCCC	22.41	26074081
134	Phosphorylation	HYYQKSKYDSSVSGQ CCCCCCCCCCCCCCC	28.31	26074081
136	Phosphorylation	YQKSKYDSSVSGQSS CCCCCCCCCCCCCCC	29.56	26074081
137	Phosphorylation	QKSKYDSSVSGQSSF CCCCCCCCCCCCCCC	19.87	26074081
139	Phosphorylation	SKYDSSVSGQSSFVT CCCCCCCCCCCCCEE	32.82	26074081
142	Phosphorylation	DSSVSGQSSFVTSPA CCCCCCCCCCEECCC	29.30	26074081
143	Phosphorylation	SSVSGQSSFVTSPAA CCCCCCCCCEECCCC	18.82	26074081
146	Phosphorylation	SGQSSFVTSPAADNI CCCCCCEECCCCCCC	27.29	26074081
147	Phosphorylation	GQSSFVTSPAADNIE CCCCCEECCCCCCCE	13.77	26074081
159	Phosphorylation	NIEMLPHYEPIPFSS CCEECCCCCCCCCCC	22.81	22817900
165	Phosphorylation	HYEPIPFSSSMNESA CCCCCCCCCCCCCCC	19.02	26074081
166	Phosphorylation	YEPIPFSSSMNESAP CCCCCCCCCCCCCCC	33.70	26074081
167	Phosphorylation	EPIPFSSSMNESAPT CCCCCCCCCCCCCCC	25.16	26074081
171	Phosphorylation	FSSSMNESAPTGITD CCCCCCCCCCCCCCC	34.25	26074081
174	Phosphorylation	SMNESAPTGITDHIV CCCCCCCCCCCCHHH	40.72	26074081
177	Phosphorylation	ESAPTGITDHIVQGP CCCCCCCCCHHHCCC	23.91	26074081
191	Phosphorylation	PDPNLEESPKRKNIT CCCCCCCCCCCCCCC	26.75	21082442
195	Ubiquitination	LEESPKRKNITYEEL CCCCCCCCCCCHHHH	59.85	-
198	Phosphorylation	SPKRKNITYEELRNK CCCCCCCCHHHHHHC	33.98	28796482
199	Phosphorylation	PKRKNITYEELRNKN CCCCCCCHHHHHHCC	12.01	25159151
209	Phosphorylation	LRNKNRESYEVSLTQ HHHCCCCCEEEECCC	24.29	30266825
210	Phosphorylation	RNKNRESYEVSLTQK HHCCCCCEEEECCCC	18.65	30266825
213	Phosphorylation	NRESYEVSLTQKTDP CCCCEEEECCCCCCC	17.48	21815630
238	Ubiquitination	KKEVKVNKYGDTWDE CHHEECCCCCCCCCC	54.31	2190698
238	Acetylation	KKEVKVNKYGDTWDE CHHEECCCCCCCCCC	54.31	26051181
238 (in isoform 1)	Ubiquitination	-	54.31	21890473
239	Phosphorylation	KEVKVNKYGDTWDE- HHEECCCCCCCCCC-	18.28	27642862

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 OCAD1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of OCAD1_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 OCAD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCBP1_HUMAN	PCBP1	physical	26344197
OCAD1_HUMAN	OCIAD1	physical	27499296
MIC19_HUMAN	CHCHD3	physical	27499296
FUND2_HUMAN	FUNDC2	physical	27499296
AFG32_HUMAN	AFG3L2	physical	27499296
STML2_HUMAN	STOML2	physical	27499296
CISD1_HUMAN	CISD1	physical	27499296
MPPB_HUMAN	PMPCB	physical	27499296
CLPB_HUMAN	CLPB	physical	27499296
NB5R3_HUMAN	CYB5R3	physical	27499296
CX6A1_HUMAN	COX6A1	physical	27499296
TOM5_HUMAN	TOMM5	physical	27499296
ABCD3_HUMAN	ABCD3	physical	27499296
UQCC2_HUMAN	UQCC2	physical	27499296
USMG5_HUMAN	USMG5	physical	27499296
ATP5E_HUMAN	ATP5E	physical	27499296
COX6C_HUMAN	COX6C	physical	27499296
MIC60_HUMAN	IMMT	physical	27499296
NRDC_HUMAN	NRD1	physical	27499296
TIM44_HUMAN	TIMM44	physical	27499296
NDUV1_HUMAN	NDUFV1	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296
ATP5H_HUMAN	ATP5H	physical	27499296
ATD3A_HUMAN	ATAD3A	physical	27499296
TXTP_HUMAN	SLC25A1	physical	27499296
NDUS8_HUMAN	NDUFS8	physical	27499296
NDUS2_HUMAN	NDUFS2	physical	27499296
MTX1_HUMAN	MTX1	physical	27499296
ATAD1_HUMAN	ATAD1	physical	27499296
MTCH2_HUMAN	MTCH2	physical	27499296
ATPG_HUMAN	ATP5C1	physical	27499296
CX7A2_HUMAN	COX7A2	physical	27499296
ATPO_HUMAN	ATP5O	physical	27499296
TOM20_HUMAN	TOMM20	physical	27499296
TOM40_HUMAN	TOMM40	physical	27499296
YMEL1_HUMAN	YME1L1	physical	27499296
C1QBP_HUMAN	C1QBP	physical	27499296
BAX_HUMAN	BAX	physical	27499296
NDUS3_HUMAN	NDUFS3	physical	27499296
ATP5J_HUMAN	ATP5J	physical	27499296
TIM50_HUMAN	TIMM50	physical	27499296
SCO1_HUMAN	SCO1	physical	27499296
PDIP2_HUMAN	POLDIP2	physical	27499296
NDUA9_HUMAN	NDUFA9	physical	27499296
NDUB1_HUMAN	NDUFB1	physical	27499296

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 OCAD1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-108, AND MASSSPECTROMETRY.	18669648 [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 SER-108, AND MASSSPECTROMETRY.	18691976 [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-108, AND MASSSPECTROMETRY.	17924679 [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-108; SER-123 ANDSER-191, AND MASS SPECTROMETRY.	17081983 [Abstract]