dbPTM

KHDR3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KHDR3_HUMAN
UniProt AC	O75525
Protein Name	KH domain-containing, RNA-binding, signal transduction-associated protein 3
Gene Name	KHDRBS3
Organism	Homo sapiens (Human).
Sequence Length	346
Subcellular Localization	Nucleus . Localized in a compartment adjacent to the nucleolus, but distinct from the peri-nucleolar one.
Protein Description	RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds preferentially to the 5'-[AU]UAAA-3' motif in vitro. Binds optimally to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). RNA-binding abilities are down-regulated by tyrosine kinase PTK6. [PubMed: 10564820]
Protein Sequence	MEEKYLPELMAEKDSLDPSFTHALRLVNQEIEKFQKGEGKDEEKYIDVVINKNMKLGQKVLIPVKQFPKFNFVGKLLGPRGNSLKRLQEETLTKMSILGKGSMRDKAKEEELRKSGEAKYFHLNDDLHVLIEVFAPPAEAYARMGHALEEIKKFLIPDYNDEIRQAQLQELTYLNGGSENADVPVVRGKPTLRTRGVPAPAITRGRGGVTARPVGVVVPRGTPTPRGVLSTRGPVSRGRGLLTPRARGVPPTGYRPPPPPPTQETYGEYDYDDGYGTAYDEQSYDSYDNSYSTPAQSGADYYDYGHGLSEETYDSYGQEEWTNSRHKAPSARTAKGVYRDQPYGRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Sumoylation	----MEEKYLPELMA ----CCCCCHHHHHH	38.49	28112733
5	Phosphorylation	---MEEKYLPELMAE ---CCCCCHHHHHHC	30.67	20068231
13	Acetylation	LPELMAEKDSLDPSF HHHHHHCCCCCCHHH	42.98	26051181
15	Phosphorylation	ELMAEKDSLDPSFTH HHHHCCCCCCHHHHH	45.82	-
19	Phosphorylation	EKDSLDPSFTHALRL CCCCCCHHHHHHHHH	42.30	17322306
36	Acetylation	QEIEKFQKGEGKDEE HHHHHHHCCCCCCHH	63.16	18530263
40	Acetylation	KFQKGEGKDEEKYID HHHCCCCCCHHHHHE	58.63	18530271
65	Acetylation	QKVLIPVKQFPKFNF CEEEEEHHHCCCCCC	40.65	25953088
75	Methylation	PKFNFVGKLLGPRGN CCCCCCHHHHCCCCH	34.93	72622545
75	Acetylation	PKFNFVGKLLGPRGN CCCCCCHHHHCCCCH	34.93	25953088
78	Ubiquitination	NFVGKLLGPRGNSLK CCCHHHHCCCCHHHH	21.94	24816145
79	Ubiquitination	FVGKLLGPRGNSLKR CCHHHHCCCCHHHHH	40.76	24816145
91	Phosphorylation	LKRLQEETLTKMSIL HHHHHHHHHHHHHHH	38.69	27174698
93	Phosphorylation	RLQEETLTKMSILGK HHHHHHHHHHHHHCC	31.92	27174698
96	Phosphorylation	EETLTKMSILGKGSM HHHHHHHHHHCCCHH	19.06	27174698
102	Phosphorylation	MSILGKGSMRDKAKE HHHHCCCHHHHHHHH	17.71	20068231
106	Ubiquitination	GKGSMRDKAKEEELR CCCHHHHHHHHHHHH	51.50	24816145
108	Acetylation	GSMRDKAKEEELRKS CHHHHHHHHHHHHHH	71.98	19817887
113	Methylation	KAKEEELRKSGEAKY HHHHHHHHHHCCCEE	34.08	-
152	Acetylation	GHALEEIKKFLIPDY HHHHHHHHHHHCCCC	40.53	23749302
178	Phosphorylation	LTYLNGGSENADVPV HHCCCCCCCCCCCCE	29.13	27251275
187	Methylation	NADVPVVRGKPTLRT CCCCCEECCCCCCCC	47.88	16186699
189	Methylation	DVPVVRGKPTLRTRG CCCEECCCCCCCCCC	25.02	115480927
193	Methylation	VRGKPTLRTRGVPAP ECCCCCCCCCCCCCC	25.51	82797567
195	Dimethylation	GKPTLRTRGVPAPAI CCCCCCCCCCCCCCC	37.36	-
195	Methylation	GKPTLRTRGVPAPAI CCCCCCCCCCCCCCC	37.36	83108403
204	Dimethylation	VPAPAITRGRGGVTA CCCCCCCCCCCCCCE	27.05	-
204	Methylation	VPAPAITRGRGGVTA CCCCCCCCCCCCCCE	27.05	83108411
206	Methylation	APAITRGRGGVTARP CCCCCCCCCCCCEEC	35.09	115383761
206	Dimethylation	APAITRGRGGVTARP CCCCCCCCCCCCEEC	35.09	-
220	Methylation	PVGVVVPRGTPTPRG CEEEEECCCCCCCCC	50.43	26494689
220	Dimethylation	PVGVVVPRGTPTPRG CEEEEECCCCCCCCC	50.43	-
226	Methylation	PRGTPTPRGVLSTRG CCCCCCCCCCEECCC	50.78	97778575
226	Dimethylation	PRGTPTPRGVLSTRG CCCCCCCCCCEECCC	50.78	-
230	Phosphorylation	PTPRGVLSTRGPVSR CCCCCCEECCCCCCC	17.41	20068231
231	Phosphorylation	TPRGVLSTRGPVSRG CCCCCEECCCCCCCC	35.17	21406692
232	Methylation	PRGVLSTRGPVSRGR CCCCEECCCCCCCCC	44.00	54561449
236	Phosphorylation	LSTRGPVSRGRGLLT EECCCCCCCCCCCCC	31.95	20068231
237	Methylation	STRGPVSRGRGLLTP ECCCCCCCCCCCCCC	38.78	54548351
237	Dimethylation	STRGPVSRGRGLLTP ECCCCCCCCCCCCCC	38.78	-
239	Dimethylation	RGPVSRGRGLLTPRA CCCCCCCCCCCCCCC	31.32	-
239	Methylation	RGPVSRGRGLLTPRA CCCCCCCCCCCCCCC	31.32	54548355
245	Methylation	GRGLLTPRARGVPPT CCCCCCCCCCCCCCC	31.51	54561457
245	Dimethylation	GRGLLTPRARGVPPT CCCCCCCCCCCCCCC	31.51	-
345	Methylation	YRDQPYGRY------ CCCCCCCCC------	28.30	115480919

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
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:15163637

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KHDR3_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 KHDR3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZN408_HUMAN	ZNF408	physical	16189514
BAHD1_HUMAN	BAHD1	physical	16189514
RBMX_HUMAN	RBMX	physical	16189514
CCD33_HUMAN	CCDC33	physical	16189514
LNX1_HUMAN	LNX1	physical	16189514
NUD18_HUMAN	NUDT18	physical	16189514
KHDR2_HUMAN	KHDRBS2	physical	16189514
SIAH1_HUMAN	SIAH1	physical	15163637
ANM1_HUMAN	PRMT1	physical	12529443
SPB5_HUMAN	SERPINB5	physical	21725612
FBX32_HUMAN	FBXO32	physical	21725612
RU1C_HUMAN	SNRPC	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
PTBP2_HUMAN	PTBP2	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	25416956
BAHD1_HUMAN	BAHD1	physical	25416956
PRP31_HUMAN	PRPF31	physical	25416956
NCOA5_HUMAN	NCOA5	physical	25416956
MARK4_HUMAN	MARK4	physical	25416956
DMRT3_HUMAN	DMRT3	physical	25416956
YTDC1_HUMAN	YTHDC1	physical	25416956
ATX2_HUMAN	ATXN2	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
ASPP1_HUMAN	PPP1R13B	physical	16474851

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 KHDR3_HUMAN

Related Literatures of Post-Translational Modification

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-5, AND MASSSPECTROMETRY.	17081983 [Abstract]