dbPTM

DIAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DIAP1_HUMAN
UniProt AC	O60610
Protein Name	Protein diaphanous homolog 1
Gene Name	DIAPH1
Organism	Homo sapiens (Human).
Sequence Length	1272
Subcellular Localization	Cell membrane . Cell projection, ruffle membrane . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Membrane ruffles, especially at the tip of ruffles, of motile cells.
Protein Description	Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape. [PubMed: 20937854]
Protein Sequence	MEPPGGSLGPGRGTRDKKKGRSPDELPSAGGDGGKSKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYTSKAGMSQKESSKSAMMYIQELRSGLRDMPLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETAGSYDSRNKHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTTIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDLREIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECISQIVLHKNGADPDFKCRHLQIEIEGLIDQMIDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPPPPLPGEAGMPPPPPPLPGGPGIPPPPPFPGGPGIPPPPPGMGMPPPPPFGFGVPAAPVLPFGLTPKKLYKPEVQLRRPNWSKLVAEDLSQDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQANRKAGCAVTSLLASELTKDDAMAAVPAKVSKNSETFPTILEEAKELVGRAS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEPPGGSL -------CCCCCCCC	60.54	22223895
1	Sulfoxidation	-------MEPPGGSL -------CCCCCCCC	60.54	28183972
7	Phosphorylation	-MEPPGGSLGPGRGT -CCCCCCCCCCCCCC	35.75	28857561
12	Methylation	GGSLGPGRGTRDKKK CCCCCCCCCCCCCCC	46.58	-
14	Phosphorylation	SLGPGRGTRDKKKGR CCCCCCCCCCCCCCC	34.04	25106551
22	Phosphorylation	RDKKKGRSPDELPSA CCCCCCCCHHHCCCC	45.42	29255136
28	Phosphorylation	RSPDELPSAGGDGGK CCHHHCCCCCCCCCC	52.77	23401153
35	Acetylation	SAGGDGGKSKKFTLK CCCCCCCCCCCHHHH	65.71	25953088
35	Methylation	SAGGDGGKSKKFTLK CCCCCCCCCCCHHHH	65.71	-
35	Ubiquitination	SAGGDGGKSKKFTLK CCCCCCCCCCCHHHH	65.71	21906983
35 (in isoform 1)	Ubiquitination	-	65.71	21890473
35 (in isoform 2)	Ubiquitination	-	65.71	21890473
36	Phosphorylation	AGGDGGKSKKFTLKR CCCCCCCCCCHHHHH	44.33	26074081
37	Acetylation	GGDGGKSKKFTLKRL CCCCCCCCCHHHHHH	56.23	25953088
38	Acetylation	GDGGKSKKFTLKRLM CCCCCCCCHHHHHHH	51.15	30588159
40	Phosphorylation	GGKSKKFTLKRLMAD CCCCCCHHHHHHHHH	40.00	28258704
42	Methylation	KSKKFTLKRLMADEL CCCCHHHHHHHHHHH	40.19	-
45	Sulfoxidation	KFTLKRLMADELERF CHHHHHHHHHHHHHH	5.26	21406390
53	Phosphorylation	ADELERFTSMRIKKE HHHHHHHHHHCCCCC	28.03	26074081
54	Phosphorylation	DELERFTSMRIKKEK HHHHHHHHHCCCCCC	11.89	26074081
66	Phosphorylation	KEKEKPNSAHRNSSA CCCCCCCCCCCCCCC	33.70	26074081
71	Phosphorylation	PNSAHRNSSASYGDD CCCCCCCCCCCCCCC	27.51	26074081
72	Phosphorylation	NSAHRNSSASYGDDP CCCCCCCCCCCCCCC	25.45	26074081
74	Phosphorylation	AHRNSSASYGDDPTA CCCCCCCCCCCCCCC	31.43	26074081
75	Phosphorylation	HRNSSASYGDDPTAQ CCCCCCCCCCCCCCH	25.04	26074081
80	Phosphorylation	ASYGDDPTAQSLQDV CCCCCCCCCHHHCCC	44.30	26074081
83	Phosphorylation	GDDPTAQSLQDVSDE CCCCCCHHHCCCCHH	26.07	26074081
88	Phosphorylation	AQSLQDVSDEQVLVL CHHHCCCCHHHHHHH	43.66	26074081
124	Sulfoxidation	DIIIKREMVSQYLYT CEEEEHHHHHHHHHH	4.00	28183972
126	Phosphorylation	IIKREMVSQYLYTSK EEEHHHHHHHHHHCC	16.28	21945579
128	Phosphorylation	KREMVSQYLYTSKAG EHHHHHHHHHHCCCC	8.31	21945579
130	Phosphorylation	EMVSQYLYTSKAGMS HHHHHHHHHCCCCCC	12.20	21945579
131	Phosphorylation	MVSQYLYTSKAGMSQ HHHHHHHHCCCCCCH	22.58	21945579
132	Phosphorylation	VSQYLYTSKAGMSQK HHHHHHHCCCCCCHH	13.62	21945579
133	Ubiquitination	SQYLYTSKAGMSQKE HHHHHHCCCCCCHHH	40.95	-
137	Phosphorylation	YTSKAGMSQKESSKS HHCCCCCCHHHCHHH	36.86	23532336
141	Phosphorylation	AGMSQKESSKSAMMY CCCCHHHCHHHHHHH	50.53	30576142
148	Phosphorylation	SSKSAMMYIQELRSG CHHHHHHHHHHHHHC	6.08	30576142
154	Phosphorylation	MYIQELRSGLRDMPL HHHHHHHHCCCCCHH	55.60	-
159	Sulfoxidation	LRSGLRDMPLLSCLE HHHCCCCCHHHHHHH	1.72	21406390
193 (in isoform 2)	Ubiquitination	-	49.85	-
196	Ubiquitination	ASLLDILKRLHDEKE HHHHHHHHHHHHHCC	53.93	-
202	Acetylation	LKRLHDEKEETAGSY HHHHHHHCCCCCCCC	67.89	26822725
202	Ubiquitination	LKRLHDEKEETAGSY HHHHHHHCCCCCCCC	67.89	-
205	Phosphorylation	LHDEKEETAGSYDSR HHHHCCCCCCCCCCC	37.09	28509920
208	Phosphorylation	EKEETAGSYDSRNKH HCCCCCCCCCCCCHH	24.25	28509920
209	Phosphorylation	KEETAGSYDSRNKHE CCCCCCCCCCCCHHH	19.61	25839225
211	Phosphorylation	ETAGSYDSRNKHEII CCCCCCCCCCHHHHH	29.53	28102081
214	Ubiquitination	GSYDSRNKHEIIRCL CCCCCCCHHHHHHHH	41.31	-
222	Ubiquitination	HEIIRCLKAFMNNKF HHHHHHHHHHHCCCC	43.11	-
233	Phosphorylation	NNKFGIKTMLETEEG CCCCCCCCEEECCCC	25.68	28258704
237	Phosphorylation	GIKTMLETEEGILLL CCCCEEECCCCEEHH	35.06	28258704
303	Ubiquitination	QPLLDGLKSGTTIAL HHHHHHHCCCCEEHH	52.98	-
311	Ubiquitination	SGTTIALKVGCLQLI CCCEEHHHHHHHHHH	27.79	-
368 (in isoform 2)	Ubiquitination	-	67.45	21890473
373	Phosphorylation	DEQGEEDSYDLKGRL CCCCCCCCCCCCCCH	24.67	26074081
374	Phosphorylation	EQGEEDSYDLKGRLD CCCCCCCCCCCCCHH	37.30	27259358
377	Ubiquitination	EEDSYDLKGRLDDIR CCCCCCCCCCHHHHH	38.80	21906983
377 (in isoform 1)	Ubiquitination	-	38.80	21890473
415	Phosphorylation	PHFLSILQHLLLVRN HHHHHHHHHHHHHCC	24.42	19605366
424	Phosphorylation	LLLVRNDYEARPQYY HHHHCCCCCCCHHHH	18.29	28152594
430	Phosphorylation	DYEARPQYYKLIEEC CCCCCHHHHHHHHHH	12.78	28152594
437	Glutathionylation	YYKLIEECISQIVLH HHHHHHHHHHHHHHH	2.05	22555962
439	O-linked_Glycosylation	KLIEECISQIVLHKN HHHHHHHHHHHHHCC	26.05	23301498
453	Ubiquitination	NGADPDFKCRHLQIE CCCCCCCCCCHHHHH	37.43	-
473	Acetylation	DQMIDKTKVEKSEAK HHHHHHHHHCHHHHH	54.88	19811419
476	Acetylation	IDKTKVEKSEAKAAE HHHHHHCHHHHHHHH	57.49	19811425
476	Ubiquitination	IDKTKVEKSEAKAAE HHHHHHCHHHHHHHH	57.49	-
480	Acetylation	KVEKSEAKAAELEKK HHCHHHHHHHHHHHH	44.04	19811431
486	2-Hydroxyisobutyrylation	AKAAELEKKLDSELT HHHHHHHHHHCHHHH	71.86	-
486	Ubiquitination	AKAAELEKKLDSELT HHHHHHHHHHCHHHH	71.86	17370265
487	Ubiquitination	KAAELEKKLDSELTA HHHHHHHHHCHHHHH	48.42	-
490	O-linked_Glycosylation	ELEKKLDSELTARHE HHHHHHCHHHHHHHH	44.96	23301498
490	Phosphorylation	ELEKKLDSELTARHE HHHHHHCHHHHHHHH	44.96	21406692
493	Phosphorylation	KKLDSELTARHELQV HHHCHHHHHHHHHHH	20.00	21406692
494 (in isoform 2)	Ubiquitination	-	24.37	21890473
503	Acetylation	HELQVEMKKMESDFE HHHHHHHHHCHHHHH	35.15	25953088
503	Ubiquitination	HELQVEMKKMESDFE HHHHHHHHHCHHHHH	35.15	21906983
503 (in isoform 1)	Ubiquitination	-	35.15	21890473
505	Sulfoxidation	LQVEMKKMESDFEQK HHHHHHHCHHHHHHH	5.07	30846556
507	Phosphorylation	VEMKKMESDFEQKLQ HHHHHCHHHHHHHHH	44.06	-
518 (in isoform 2)	Ubiquitination	-	51.74	21890473
520	2-Hydroxyisobutyrylation	LQDLQGEKDALHSEK HHHHHCCHHHHHHHH	55.94	-
520	Acetylation	LQDLQGEKDALHSEK HHHHHCCHHHHHHHH	55.94	23749302
520	Ubiquitination	LQDLQGEKDALHSEK HHHHHCCHHHHHHHH	55.94	-
527	2-Hydroxyisobutyrylation	KDALHSEKQQIATEK HHHHHHHHHHHHHHH	50.98	-
527	Acetylation	KDALHSEKQQIATEK HHHHHHHHHHHHHHH	50.98	25953088
527	Ubiquitination	KDALHSEKQQIATEK HHHHHHHHHHHHHHH	50.98	21906983
527 (in isoform 1)	Ubiquitination	-	50.98	21890473
542	Phosphorylation	QDLEAEVSQLTGEVA HHHHHHHHHHHHHHH	15.81	-
550	Ubiquitination	QLTGEVAKLTKELED HHHHHHHHHHHHHHH	62.96	-
564	Phosphorylation	DAKKEMASLSAAAIT HHHHHHHHCHHHEEE	22.88	23532336
566	Phosphorylation	KKEMASLSAAAITVP HHHHHHCHHHEEECC	17.23	26503514
571	Phosphorylation	SLSAAAITVPPSVPS HCHHHEEECCCCCCC	23.41	26503514
665	Phosphorylation	PEGVGIPSPSSLPGG CCCCCCCCCCCCCCC	35.18	24275569
753 (in isoform 2)	Ubiquitination	-	18.26	21890473
765	Ubiquitination	PAAPVLPFGLTPKKL CCCCCCCCCCCHHHC	12.53	21890473
768	Phosphorylation	PVLPFGLTPKKLYKP CCCCCCCCHHHCCCC	33.18	23325789
771	Acetylation	PFGLTPKKLYKPEVQ CCCCCHHHCCCCCCC	59.25	25953088
771	Ubiquitination	PFGLTPKKLYKPEVQ CCCCCHHHCCCCCCC	59.25	-
773	Phosphorylation	GLTPKKLYKPEVQLR CCCHHHCCCCCCCCC	33.12	-
774	Ubiquitination	LTPKKLYKPEVQLRR CCHHHCCCCCCCCCC	45.17	21890473
774 (in isoform 1)	Ubiquitination	-	45.17	21890473
786	Ubiquitination	LRRPNWSKLVAEDLS CCCCCHHHHHHHHHC	38.30	-
793	Phosphorylation	KLVAEDLSQDCFWTK HHHHHHHCCCCCCHH	35.97	28857561
796	Glutathionylation	AEDLSQDCFWTKVKE HHHHCCCCCCHHCCC	2.08	22555962
800	Acetylation	SQDCFWTKVKEDRFE CCCCCCHHCCCCCCC	41.74	27452117
800	Ubiquitination	SQDCFWTKVKEDRFE CCCCCCHHCCCCCCC	41.74	-
802	Ubiquitination	DCFWTKVKEDRFENN CCCCHHCCCCCCCCC	56.29	-
814	Acetylation	ENNELFAKLTLTFSA CCCCEEHHHEEEEEC	34.37	30588165
823	Phosphorylation	TLTFSAQTKTSKAKK EEEEECCCCCCCCCC	35.69	28555341
824	Acetylation	LTFSAQTKTSKAKKD EEEECCCCCCCCCCC	38.43	20682765
824	Ubiquitination	LTFSAQTKTSKAKKD EEEECCCCCCCCCCC	38.43	-
830	Acetylation	TKTSKAKKDQEGGEE CCCCCCCCCCCCCCH	70.29	20682769
855	Ubiquitination	ELKVLDSKTAQNLSI EEEECCCHHCCCHHH	47.77	-
856	Phosphorylation	LKVLDSKTAQNLSIF EEECCCHHCCCHHHH	37.11	20068231
861	Phosphorylation	SKTAQNLSIFLGSFR CHHCCCHHHHHHHCC	20.88	20068231
866	Phosphorylation	NLSIFLGSFRMPYQE CHHHHHHHCCCCHHH	16.30	20068231
871	Phosphorylation	LGSFRMPYQEIKNVI HHHCCCCHHHHHHHH	14.94	30257219
947	Phosphorylation	ILFKLQFSEQVENIK HHHHHHCHHHHHCCC	17.73	20068231
959	Phosphorylation	NIKPEIVSVTAACEE CCCHHHHHHHHHHHH	21.29	20068231
961	Phosphorylation	KPEIVSVTAACEELR CHHHHHHHHHHHHHH	10.88	20068231
1031	Phosphorylation	AELCENDYPDVLKFP HHHHHCCCCCHHHCC	16.95	29083192
1033 (in isoform 2)	Ubiquitination	-	52.75	21890473
1046	Ubiquitination	DELAHVEKASRVSAE HHHHHHHHHHHCCHH	51.04	-
1048	Acetylation	LAHVEKASRVSAENL HHHHHHHHHCCHHHH	44.26	19608861
1048	Ubiquitination	LAHVEKASRVSAENL HHHHHHHHHCCHHHH	44.26	19608861
1048	Ubiquitination	LAHVEKASRVSAENL HHHHHHHHHCCHHHH	44.26	21890473
1051	Phosphorylation	VEKASRVSAENLQKN HHHHHHCCHHHHHHH	28.84	21406692
1057	Acetylation	VSAENLQKNLDQMKK CCHHHHHHHHHHHHH	63.74	19608861
1057	Ubiquitination	VSAENLQKNLDQMKK CCHHHHHHHHHHHHH	63.74	19608861
1057 (in isoform 1)	Ubiquitination	-	63.74	21890473
1063	Acetylation	QKNLDQMKKQISDVE HHHHHHHHHHHHHHH	35.57	25953088
1083	Acetylation	FPAATDEKDKFVEKM CCCCCCHHHHHHHHH	69.86	25953088
1091	Phosphorylation	DKFVEKMTSFVKDAQ HHHHHHHHHHHHHHH	30.04	23663014
1092	Phosphorylation	KFVEKMTSFVKDAQE HHHHHHHHHHHHHHH	25.25	23663014
1094	Acetylation	VEKMTSFVKDAQEQY HHHHHHHHHHHHHHH	5.70	19608861
1101	Phosphorylation	VKDAQEQYNKLRMMH HHHHHHHHHHHHHHH	17.32	23663014
1103	2-Hydroxyisobutyrylation	DAQEQYNKLRMMHSN HHHHHHHHHHHHHHC	32.32	-
1103	Acetylation	DAQEQYNKLRMMHSN HHHHHHHHHHHHHHC	32.32	19608861
1103	Ubiquitination	DAQEQYNKLRMMHSN HHHHHHHHHHHHHHC	32.32	19608861
1109	Phosphorylation	NKLRMMHSNMETLYK HHHHHHHHCHHHHHH	21.70	28851738
1115	Phosphorylation	HSNMETLYKELGEYF HHCHHHHHHHHHHHH	15.16	28851738
1121	Phosphorylation	LYKELGEYFLFDPKK HHHHHHHHHCCCHHH	12.09	23917254
1127	2-Hydroxyisobutyrylation	EYFLFDPKKLSVEEF HHHCCCHHHCCHHHH	69.09	-
1136	Sulfoxidation	LSVEEFFMDLHNFRN CCHHHHHHHHHHHHH	6.95	30846556
1150	Acetylation	NMFLQAVKENQKRRE HHHHHHHHHHHHHHH	54.70	25953088
1196	Phosphorylation	MNAEGDETGVMDSLL CCCCCCCCCHHHHHH	39.55	18452278
1201	Phosphorylation	DETGVMDSLLEALQS CCCCHHHHHHHHHHH	19.43	18452278
1224	Ubiquitination	GPRQANRKAGCAVTS CCCHHHHHHHHHHHH	49.27	-
1227	S-nitrosocysteine	QANRKAGCAVTSLLA HHHHHHHHHHHHHHH	3.08	-
1227	Glutathionylation	QANRKAGCAVTSLLA HHHHHHHHHHHHHHH	3.08	22555962
1227	S-nitrosylation	QANRKAGCAVTSLLA HHHHHHHHHHHHHHH	3.08	22178444
1230	Phosphorylation	RKAGCAVTSLLASEL HHHHHHHHHHHHHCC	8.64	27050516
1231	Phosphorylation	KAGCAVTSLLASELT HHHHHHHHHHHHCCC	18.13	28555341
1235	Phosphorylation	AVTSLLASELTKDDA HHHHHHHHCCCCCCH	32.86	27251275
1238	Phosphorylation	SLLASELTKDDAMAA HHHHHCCCCCCHHHH	28.51	21406692
1239	Ubiquitination	LLASELTKDDAMAAV HHHHCCCCCCHHHHC	67.26	-
1243	Sulfoxidation	ELTKDDAMAAVPAKV CCCCCCHHHHCCCCC	2.94	21406390
1249	Acetylation	AMAAVPAKVSKNSET HHHHCCCCCCCCCCC	40.76	25953088
1249	Ubiquitination	AMAAVPAKVSKNSET HHHHCCCCCCCCCCC	40.76	-
1251	Phosphorylation	AAVPAKVSKNSETFP HHCCCCCCCCCCCHH	25.97	28450419
1252	Ubiquitination	AVPAKVSKNSETFPT HCCCCCCCCCCCHHH	68.43	-
1254	Phosphorylation	PAKVSKNSETFPTIL CCCCCCCCCCHHHHH	41.57	29255136
1256	Phosphorylation	KVSKNSETFPTILEE CCCCCCCCHHHHHHH	34.43	29255136
1259	Phosphorylation	KNSETFPTILEEAKE CCCCCHHHHHHHHHH	33.72	26074081
1265	Ubiquitination	PTILEEAKELVGRAS HHHHHHHHHHHCCCC	55.66	-
1272	Phosphorylation	KELVGRAS------- HHHHCCCC-------	39.12	30576142

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
768	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
768	T	Phosphorylation		23325789
Phosphorylation at Thr-768 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement.

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 DIAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MYO1E_HUMAN	MYO1E	physical	22939629
HS74L_HUMAN	HSPA4L	physical	22939629
CENPA_HUMAN	CENPA	physical	15085137
COPD_HUMAN	ARCN1	physical	22863883
COPB_HUMAN	COPB1	physical	22863883
KINH_HUMAN	KIF5B	physical	22863883
KLC1_HUMAN	KLC1	physical	22863883
KLC4_HUMAN	KLC4	physical	22863883
PTN23_HUMAN	PTPN23	physical	22863883
P4R3B_HUMAN	SMEK2	physical	22863883
MTOR_HUMAN	MTOR	physical	26344197
TLN2_HUMAN	TLN2	physical	26344197
TTC4_HUMAN	TTC4	physical	26344197
UBL7_HUMAN	UBL7	physical	26344197
LRP1_HUMAN	LRP1	physical	26496610
PLXB1_HUMAN	PLXNB1	physical	26496610
PABP2_HUMAN	PABPN1	physical	26496610
MOT4_HUMAN	SLC16A3	physical	26496610
SWAHC_HUMAN	SOWAHC	physical	26496610
TUT7_HUMAN	ZCCHC6	physical	26496610
RAB34_HUMAN	RAB34	physical	26496610

Drug and Disease Associations

Kegg Disease
H00604	Deafness, autosomal dominant
OMIM Disease
124900	Deafness, autosomal dominant, 1 (DFNA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DIAP1_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]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1057 AND LYS-1103, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-22, AND MASSSPECTROMETRY.	19690332 [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-22, AND MASSSPECTROMETRY.	18669648 [Abstract]
Ubiquitylation
Reference	PubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-486, AND MASSSPECTROMETRY.	17370265 [Abstract]

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