dbPTM

DIAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DIAP2_HUMAN
UniProt AC	O60879
Protein Name	Protein diaphanous homolog 2
Gene Name	DIAPH2
Organism	Homo sapiens (Human).
Sequence Length	1101
Subcellular Localization	Isoform 3: Cytoplasm, cytosol. Early endosome. Isoform 3 is cytosolic but when coexpressed with RHOD, the 2 proteins colocalize to early endosomes.
Protein Description	Could be involved in oogenesis. Involved in the regulation of endosome dynamics. Implicated in a novel signal transduction pathway, in which isoform 3 and CSK are sequentially activated by RHOD to regulate the motility of early endosomes through interactions with the actin cytoskeleton..
Protein Sequence	MEQPGAAASGAGGGSEEPGGGRSNKRSAGNRAANEEETKNKPKLNIQIKTLADDVRDRITSFRKSTVKKEKPLIQHPIDSQVAMSEFPAAQPLYDERSLNLSEKEVLDLFEKMMEDMNLNEEKKAPLRNKDFTTKREMVVQYISATAKSGGLKNSKHECTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSNPVSWVNNFGHEGLGLLLDELEKLLDKKQQENIDKKNQYKLIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQPNMMTEIVKILSAICIVGEENILDKLLGAITTAAERNNRERFSPIVEGLENQEALQLQVACMQFINALVTSPYELDFRIHLRNEFLRSGLKTMLPDLKEKENDELDIQLKVFDENKEDDLTELSHRLNDIRAEMDDMNEVYHLLYNMLKDTAAENYFLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRLDIDLTHLIDSCVNKAKVEESEQKAAEFSKKFDEEFTARQEAQAELQKRDEKIKELEAEIQQLRTQAQVLSSSSGIPGPPAAPPLPGVGPPPPPPAPPLPGGAPLPPPPPPLPGMMGIPPPPPPPLLFGGPPPPPPLGGVPPPPGISLNLPYGMKQKKMYKPEVSMKRINWSKIEPTELSENCFWLRVKEDKFENPDLFAKLALNFATQIKVQKNAEALEEKKTGPTKKKVKELRILDPKTAQNLSIFLGSYRMPYEDIRNVILEVNEDMLSEALIQNLVKHLPEQKILNELAELKNEYDDLCEPEQFGVVMSSVKMLQPRLSSILFKLTFEEHINNIKPSIIAVTLACEELKKSESFNRLLELVLLVGNYMNSGSRNAQSLGFKINFLCKIRDTKSADQKTTLLHFIADICEEKYRDILKFPEELEHVESASKVSAQILKSNLASMEQQIVHLERDIKKFPQAENQHDKFVEKMTSFTKTAREQYEKLSTMHNNMMKLYENLGEYFIFDSKTVSIEEFFGDLNNFRTLFLEAVRENNKRREMEEKTRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRVPLERSRSRHNGAISSK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEQPGAAA -------CCCCCCCC	45.69	22814378
15	Phosphorylation	ASGAGGGSEEPGGGR CCCCCCCCCCCCCCC	41.90	28674151
23	Phosphorylation	EEPGGGRSNKRSAGN CCCCCCCCCCCCCCC	50.40	28674151
49	Ubiquitination	PKLNIQIKTLADDVR CCCCEEEEHHHHHHH	22.55	33845483
61	Phosphorylation	DVRDRITSFRKSTVK HHHHHHHHHHHHCCC	22.23	21712546
65	Phosphorylation	RITSFRKSTVKKEKP HHHHHHHHCCCCCCC	33.89	21712546
66	Phosphorylation	ITSFRKSTVKKEKPL HHHHHHHCCCCCCCC	39.10	-
85	Phosphorylation	IDSQVAMSEFPAAQP CCCHHHHCCCCCCCC	26.75	29978859
94	Phosphorylation	FPAAQPLYDERSLNL CCCCCCCCCCCCCCC	23.57	28796482
123	Acetylation	DMNLNEEKKAPLRNK HCCCCHHHCCCCCCC	48.32	20167786
124	Acetylation	MNLNEEKKAPLRNKD CCCCHHHCCCCCCCC	59.52	20167786
130	Acetylation	KKAPLRNKDFTTKRE HCCCCCCCCCCCCHH	48.03	20167786
131 (in isoform 3)	Phosphorylation	-	50.07	29083192
133 (in isoform 3)	Phosphorylation	-	41.35	29083192
135 (in isoform 3)	Phosphorylation	-	43.22	29083192
138 (in isoform 3)	Phosphorylation	-	4.09	29083192
142 (in isoform 3)	Phosphorylation	-	5.80	29083192
145 (in isoform 3)	Phosphorylation	-	11.30	29083192
189	Phosphorylation	CLESLRVSLTSNPVS HHHHHCCCCCCCCCH	21.35	-
232	Acetylation	IDKKNQYKLIQCLKA CCHHHHHHHHHHHHH	29.38	25953088
238	Ubiquitination	YKLIQCLKAFMNNKF HHHHHHHHHHHCCCC	47.40	-
366	Ubiquitination	KTMLPDLKEKENDEL HHHCCCHHHHCCCCC	74.29	32015554
439	Phosphorylation	FLLIRNDYYIRPQYY HHHHCCCCCCCHHHH	12.35	26074081
440	Phosphorylation	LLIRNDYYIRPQYYK HHHCCCCCCCHHHHH	8.04	26074081
445	Phosphorylation	DYYIRPQYYKIIEEC CCCCCHHHHHHHHHH	14.92	26074081
446	Phosphorylation	YYIRPQYYKIIEECV CCCCHHHHHHHHHHH	7.17	26074081
454	Phosphorylation	KIIEECVSQIVLHCS HHHHHHHHHHHHHHC	26.33	26074081
503	Acetylation	KAAEFSKKFDEEFTA HHHHHHHHHCHHHHH	57.77	25953088
509	Phosphorylation	KKFDEEFTARQEAQA HHHCHHHHHHHHHHH	24.98	-
520	Ubiquitination	EAQAELQKRDEKIKE HHHHHHHHHHHHHHH	74.56	24816145
526	Ubiquitination	QKRDEKIKELEAEIQ HHHHHHHHHHHHHHH	68.28	24816145
632	Phosphorylation	GMKQKKMYKPEVSMK CCCCCCCCCCCCCCC	32.07	17081983
637	Phosphorylation	KMYKPEVSMKRINWS CCCCCCCCCCCCCHH	19.54	28857561
639	Acetylation	YKPEVSMKRINWSKI CCCCCCCCCCCHHHC	42.49	25953088
661	Ubiquitination	NCFWLRVKEDKFENP CEEEEEECCCCCCCH	54.48	29967540
700	Acetylation	EKKTGPTKKKVKELR HHCCCCCHHHHEEEE	54.45	7695091
701	Acetylation	KKTGPTKKKVKELRI HCCCCCHHHHEEEEE	66.34	30588141
713	Phosphorylation	LRILDPKTAQNLSIF EEECCHHHCCCHHHH	38.57	27174698
718	Phosphorylation	PKTAQNLSIFLGSYR HHHCCCHHHHHHCCC	20.88	27174698
723	Phosphorylation	NLSIFLGSYRMPYED CHHHHHHCCCCCHHH	16.23	27174698
724	Phosphorylation	LSIFLGSYRMPYEDI HHHHHHCCCCCHHHH	14.77	27174698
728	Phosphorylation	LGSYRMPYEDIRNVI HHCCCCCHHHHHHHH	19.52	27174698
759	Ubiquitination	VKHLPEQKILNELAE HHHCCHHHHHHHHHH	47.72	32015554
813	Phosphorylation	HINNIKPSIIAVTLA HHHHCCHHHHHHHHH	22.94	-
875	Phosphorylation	KSADQKTTLLHFIAD CCCCCHHHHHHHHHH	34.07	-
949	Phosphorylation	KFVEKMTSFTKTARE HHHHHHHHHHHHHHH	27.67	24719451
970	Acetylation	TMHNNMMKLYENLGE HHHHHHHHHHHHHHC	36.83	126682799
1026	Ubiquitination	TRRAKLAKEKAEQEK HHHHHHHHHHHHHHH	70.90	24816145
1053	Phosphorylation	INKEGDETGVMDNLL CCCCCCCCCHHHHHH	39.55	24043423
1065	Phosphorylation	NLLEALQSGAAFRDR HHHHHHHHCCHHHHH	31.11	24043423

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 DIAP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DIAP2_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 DIAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
RHOD_HUMAN	RHOD	physical	12577064

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300511	Premature ovarian failure 2A (POF2A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DIAP2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"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 TYR-632, AND MASSSPECTROMETRY.	17081983 [Abstract]