dbPTM

KHDR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KHDR1_HUMAN
UniProt AC	Q07666
Protein Name	KH domain-containing, RNA-binding, signal transduction-associated protein 1
Gene Name	KHDRBS1 {ECO:0000312\|HGNC:HGNC:18116}
Organism	Homo sapiens (Human).
Sequence Length	443
Subcellular Localization	Nucleus . Cytoplasm . Membrane . Predominantly located in the nucleus but also located partially in the cytoplasm.
Protein Description	Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to. [PubMed: 22253824 RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (By similarity In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1]
Protein Sequence	MQRRDDPAARMSRSSGRSGSMDPSGAHPSVRQTPSRQPPLPHRSRGGGGGSRGGARASPATQPPPLLPPSATGPDATVGGPAPTPLLPPSATASVKMEPENKYLPELMAEKDSLDPSFTHAMQLLTAEIEKIQKGDSKKDDEENYLDLFSHKNMKLKERVLIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKAKEEELRKGGDPKYAHLNMDLHVFIEVFGPPCEAYALMAHAMEEVKKFLVPDMMDDICQEQFLELSYLNGVPEPSRGRGVPVRGRGAAPPPPPVPRGRGVGPPRGALVRGTPVRGAITRGATVTRGVPPPPTVRGAPAPRARTAGIQRIPLPPPPAPETYEEYGYDDTYAEQSYEGYEGYYSQSQGDSEYYDYGHGEVQDSYEAYGQDDWNGTRPSLKAPPARPVKGAYREHPYGRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Methylation	RRDDPAARMSRSSGR CCCCHHHHHHHCCCC	26.22	80700745
12	Phosphorylation	DDPAARMSRSSGRSG CCHHHHHHHCCCCCC	24.37	26074081
14	Phosphorylation	PAARMSRSSGRSGSM HHHHHHHCCCCCCCC	29.82	23911959
15	Phosphorylation	AARMSRSSGRSGSMD HHHHHHCCCCCCCCC	36.80	20068230
17	Methylation	RMSRSSGRSGSMDPS HHHHCCCCCCCCCCC	39.53	115480887
18	Phosphorylation	MSRSSGRSGSMDPSG HHHCCCCCCCCCCCC	38.45	29255136
20	Phosphorylation	RSSGRSGSMDPSGAH HCCCCCCCCCCCCCC	22.66	29255136
21	Sulfoxidation	SSGRSGSMDPSGAHP CCCCCCCCCCCCCCC	11.37	21406390
24	Phosphorylation	RSGSMDPSGAHPSVR CCCCCCCCCCCCCCC	44.33	30266825
29	Phosphorylation	DPSGAHPSVRQTPSR CCCCCCCCCCCCCCC	21.77	23927012
33	Phosphorylation	AHPSVRQTPSRQPPL CCCCCCCCCCCCCCC	16.80	30266825
35	Phosphorylation	PSVRQTPSRQPPLPH CCCCCCCCCCCCCCC	47.11	30266825
36	Methylation	SVRQTPSRQPPLPHR CCCCCCCCCCCCCCC	54.98	16187437
43	Methylation	RQPPLPHRSRGGGGG CCCCCCCCCCCCCCC	26.55	18958405
44	Phosphorylation	QPPLPHRSRGGGGGS CCCCCCCCCCCCCCC	32.04	24719451
45	Asymmetric dimethylarginine	PPLPHRSRGGGGGSR CCCCCCCCCCCCCCC	47.97	-
45	Methylation	PPLPHRSRGGGGGSR CCCCCCCCCCCCCCC	47.97	12529443
52	Asymmetric dimethylarginine	RGGGGGSRGGARASP CCCCCCCCCCCCCCC	51.33	-
52	Methylation	RGGGGGSRGGARASP CCCCCCCCCCCCCCC	51.33	12529443
58	Phosphorylation	SRGGARASPATQPPP CCCCCCCCCCCCCCC	14.98	29255136
61	Phosphorylation	GARASPATQPPPLLP CCCCCCCCCCCCCCC	45.02	29255136
70	Phosphorylation	PPPLLPPSATGPDAT CCCCCCCCCCCCCCC	36.20	29255136
72	Phosphorylation	PLLPPSATGPDATVG CCCCCCCCCCCCCCC	54.29	29255136
77	Phosphorylation	SATGPDATVGGPAPT CCCCCCCCCCCCCCC	27.36	29255136
84	Phosphorylation	TVGGPAPTPLLPPSA CCCCCCCCCCCCCCC	28.77	29255136
90	Phosphorylation	PTPLLPPSATASVKM CCCCCCCCCCCCCCC	35.99	24732914
92	Phosphorylation	PLLPPSATASVKMEP CCCCCCCCCCCCCCC	24.65	30278072
94	Phosphorylation	LPPSATASVKMEPEN CCCCCCCCCCCCCCC	20.23	23927012
96	Sumoylation	PSATASVKMEPENKY CCCCCCCCCCCCCCC	34.74	-
96	Acetylation	PSATASVKMEPENKY CCCCCCCCCCCCCCC	34.74	23954790
96	Sumoylation	PSATASVKMEPENKY CCCCCCCCCCCCCCC	34.74	28112733
102	Sumoylation	VKMEPENKYLPELMA CCCCCCCCCHHHHHH	46.64	-
102	2-Hydroxyisobutyrylation	VKMEPENKYLPELMA CCCCCCCCCHHHHHH	46.64	-
102	Sumoylation	VKMEPENKYLPELMA CCCCCCCCCHHHHHH	46.64	28112733
102	Ubiquitination	VKMEPENKYLPELMA CCCCCCCCCHHHHHH	46.64	32015554
103	Phosphorylation	KMEPENKYLPELMAE CCCCCCCCHHHHHHC	38.79	20068231
111	Ubiquitination	LPELMAEKDSLDPSF HHHHHHCCCCCCHHH	42.98	29967540
113	Phosphorylation	ELMAEKDSLDPSFTH HHHHCCCCCCHHHHH	45.82	25159151
119	Phosphorylation	DSLDPSFTHAMQLLT CCCCHHHHHHHHHHH	17.05	-
127 (in isoform 2)	Ubiquitination	-	18.75	21890473
131	Ubiquitination	LLTAEIEKIQKGDSK HHHHHHHHHHCCCCC	56.98	29967540
137	Phosphorylation	EKIQKGDSKKDDEEN HHHHCCCCCCCCHHC	50.72	30576142
138	Ubiquitination	KIQKGDSKKDDEENY HHHCCCCCCCCHHCH	66.03	32015554
139	2-Hydroxyisobutyrylation	IQKGDSKKDDEENYL HHCCCCCCCCHHCHH	74.49	-
139	Acetylation	IQKGDSKKDDEENYL HHCCCCCCCCHHCHH	74.49	26051181
139	Sumoylation	IQKGDSKKDDEENYL HHCCCCCCCCHHCHH	74.49	28112733
139	Ubiquitination	IQKGDSKKDDEENYL HHCCCCCCCCHHCHH	74.49	29967540
140 (in isoform 2)	Ubiquitination	-	72.75	21890473
144 (in isoform 2)	Ubiquitination	-	40.39	21890473
145	Phosphorylation	KKDDEENYLDLFSHK CCCCHHCHHHHHHHC	12.60	28152594
150	Phosphorylation	ENYLDLFSHKNMKLK HCHHHHHHHCCCCCH	40.63	30266825
150 (in isoform 2)	Ubiquitination	-	40.63	21890473
152	2-Hydroxyisobutyrylation	YLDLFSHKNMKLKER HHHHHHHCCCCCHHE	58.50	-
152	Acetylation	YLDLFSHKNMKLKER HHHHHHHCCCCCHHE	58.50	26822725
152	Malonylation	YLDLFSHKNMKLKER HHHHHHHCCCCCHHE	58.50	30639696
152	Ubiquitination	YLDLFSHKNMKLKER HHHHHHHCCCCCHHE	58.50	21890473
152 (in isoform 1)	Ubiquitination	-	58.50	21890473
152 (in isoform 3)	Ubiquitination	-	58.50	21890473
155	Ubiquitination	LFSHKNMKLKERVLI HHHHCCCCCHHEEEE	66.84	-
160 (in isoform 2)	Ubiquitination	-	6.27	21890473
165	2-Hydroxyisobutyrylation	ERVLIPVKQYPKFNF HEEEEEHHHCCCCCE	38.47	-
165	Acetylation	ERVLIPVKQYPKFNF HEEEEEHHHCCCCCE	38.47	23236377
165	Succinylation	ERVLIPVKQYPKFNF HEEEEEHHHCCCCCE	38.47	23954790
165	Ubiquitination	ERVLIPVKQYPKFNF HEEEEEHHHCCCCCE	38.47	23000965
165 (in isoform 1)	Ubiquitination	-	38.47	21890473
165 (in isoform 3)	Ubiquitination	-	38.47	21890473
169	Acetylation	IPVKQYPKFNFVGKI EEHHHCCCCCEEHHH	48.26	23749302
169	Ubiquitination	IPVKQYPKFNFVGKI EEHHHCCCCCEEHHH	48.26	23000965
169 (in isoform 1)	Ubiquitination	-	48.26	21890473
175	Sumoylation	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	-
175	Acetylation	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	19608861
175	Methylation	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	22640355
175	Sumoylation	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	28112733
175	Ubiquitination	PKFNFVGKILGPQGN CCCCEEHHHHCCCCH	29.47	23000965
175 (in isoform 1)	Ubiquitination	-	29.47	21890473
183	Phosphorylation	ILGPQGNTIKRLQEE HHCCCCHHHHHHHHH	34.40	20068231
185	Sumoylation	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	-
185	2-Hydroxyisobutyrylation	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	-
185	Acetylation	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	25953088
185	Succinylation	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	23954790
185	Sumoylation	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	-
185	Ubiquitination	GPQGNTIKRLQEETG CCCCHHHHHHHHHHC	45.04	23000965
185 (in isoform 1)	Ubiquitination	-	45.04	21890473
194	2-Hydroxyisobutyrylation	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	-
194	Acetylation	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	25953088
194	Methylation	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	23644510
194	Sumoylation	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	-
194	Ubiquitination	LQEETGAKISVLGKG HHHHHCCCEEEECCC	36.54	33845483
196	Phosphorylation	EETGAKISVLGKGSM HHHCCCEEEECCCHH	15.58	21406692
200	2-Hydroxyisobutyrylation	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	-
200	Acetylation	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	26051181
200	Malonylation	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	26320211
200	Methylation	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	23644510
200	Ubiquitination	AKISVLGKGSMRDKA CCEEEECCCHHHHHH	43.59	29967540
202	Phosphorylation	ISVLGKGSMRDKAKE EEEECCCHHHHHHHH	17.71	26434776
206	Ubiquitination	GKGSMRDKAKEEELR CCCHHHHHHHHHHHH	51.50	24816145
208	Acetylation	GSMRDKAKEEELRKG CHHHHHHHHHHHHHC	71.98	19818013
213	Methylation	KAKEEELRKGGDPKY HHHHHHHHHCCCCCC	38.56	-
241	Phosphorylation	FGPPCEAYALMAHAM HCCHHHHHHHHHHHH	4.30	28985074
252	Acetylation	AHAMEEVKKFLVPDM HHHHHHHHHHHCCHH	40.88	3751047
252	Methylation	AHAMEEVKKFLVPDM HHHHHHHHHHHCCHH	40.88	15782174
253	Acetylation	HAMEEVKKFLVPDMM HHHHHHHHHHCCHHH	49.45	30585355
265	Methylation	DMMDDICQEQFLELS HHHHHHHHHHHHHHH	48.11	12529443
271	Methylation	CQEQFLELSYLNGVP HHHHHHHHHHHCCCC	4.42	12529443
276	Methylation	LELSYLNGVPEPSRG HHHHHHCCCCCCCCC	33.49	12529443
281	Methylation	LNGVPEPSRGRGVPV HCCCCCCCCCCCCCC	45.78	12529443
282	Dimethylation	NGVPEPSRGRGVPVR CCCCCCCCCCCCCCC	49.93	-
282	Methylation	NGVPEPSRGRGVPVR CCCCCCCCCCCCCCC	49.93	24129315
284	Dimethylation	VPEPSRGRGVPVRGR CCCCCCCCCCCCCCC	41.65	-
284	Methylation	VPEPSRGRGVPVRGR CCCCCCCCCCCCCCC	41.65	24129315
286	Methylation	EPSRGRGVPVRGRGA CCCCCCCCCCCCCCC	3.69	15782174
289	Dimethylation	RGRGVPVRGRGAAPP CCCCCCCCCCCCCCC	24.03	-
289	Methylation	RGRGVPVRGRGAAPP CCCCCCCCCCCCCCC	24.03	54559025
291	Dimethylation	RGVPVRGRGAAPPPP CCCCCCCCCCCCCCC	22.48	-
291	Methylation	RGVPVRGRGAAPPPP CCCCCCCCCCCCCCC	22.48	15782174
292	Methylation	GVPVRGRGAAPPPPP CCCCCCCCCCCCCCC	28.99	15782174
301	Methylation	APPPPPVPRGRGVGP CCCCCCCCCCCCCCC	38.49	15782174
302	Dimethylation	PPPPPVPRGRGVGPP CCCCCCCCCCCCCCC	47.91	-
302	Methylation	PPPPPVPRGRGVGPP CCCCCCCCCCCCCCC	47.91	54559009
304	Asymmetric dimethylarginine	PPPVPRGRGVGPPRG CCCCCCCCCCCCCCC	37.59	-
304	Methylation	PPPVPRGRGVGPPRG CCCCCCCCCCCCCCC	37.59	12529443
307	Methylation	VPRGRGVGPPRGALV CCCCCCCCCCCCCCC	29.35	15782174
310	Dimethylation	GRGVGPPRGALVRGT CCCCCCCCCCCCCCC	46.26	-
310	Methylation	GRGVGPPRGALVRGT CCCCCCCCCCCCCCC	46.26	12529443
315	Dimethylation	PPRGALVRGTPVRGA CCCCCCCCCCCCCCE	44.08	-
315	Methylation	PPRGALVRGTPVRGA CCCCCCCCCCCCCCE	44.08	12529443
317	Phosphorylation	RGALVRGTPVRGAIT CCCCCCCCCCCCEEC	14.19	23403867
320	Dimethylation	LVRGTPVRGAITRGA CCCCCCCCCEECCCC	29.99	-
320	Methylation	LVRGTPVRGAITRGA CCCCCCCCCEECCCC	29.99	138001
325	Dimethylation	PVRGAITRGATVTRG CCCCEECCCCEECCC	27.00	-
325	Methylation	PVRGAITRGATVTRG CCCCEECCCCEECCC	27.00	12529443
328	Phosphorylation	GAITRGATVTRGVPP CEECCCCEECCCCCC	25.82	22210691
331	Asymmetric dimethylarginine	TRGATVTRGVPPPPT CCCCEECCCCCCCCC	39.51	-
331	Methylation	TRGATVTRGVPPPPT CCCCEECCCCCCCCC	39.51	26494637
340	Dimethylation	VPPPPTVRGAPAPRA CCCCCCCCCCCCCCC	37.73	-
340	Methylation	VPPPPTVRGAPAPRA CCCCCCCCCCCCCCC	37.73	24129315
346	Dimethylation	VRGAPAPRARTAGIQ CCCCCCCCCCCCCCC	38.52	-
346	Methylation	VRGAPAPRARTAGIQ CCCCCCCCCCCCCCC	38.52	15782174
348	Dimethylation	GAPAPRARTAGIQRI CCCCCCCCCCCCCCC	26.79	-
348	Methylation	GAPAPRARTAGIQRI CCCCCCCCCCCCCCC	26.79	54559033
349	Phosphorylation	APAPRARTAGIQRIP CCCCCCCCCCCCCCC	28.40	20068231
365	Phosphorylation	PPPPAPETYEEYGYD CCCCCCCCHHHHCCC	34.86	-
366	Phosphorylation	PPPAPETYEEYGYDD CCCCCCCHHHHCCCC	12.71	-
369	Phosphorylation	APETYEEYGYDDTYA CCCCHHHHCCCCCCC	14.73	-
371	Phosphorylation	ETYEEYGYDDTYAEQ CCHHHHCCCCCCCCC	15.11	22817900
374	Phosphorylation	EEYGYDDTYAEQSYE HHHCCCCCCCCCCCC	23.02	-
375	Phosphorylation	EYGYDDTYAEQSYEG HHCCCCCCCCCCCCC	18.35	22817900
380	Phosphorylation	DTYAEQSYEGYEGYY CCCCCCCCCCCCCCC	17.05	22817900
385	Ubiquitination	QSYEGYEGYYSQSQG CCCCCCCCCCCCCCC	20.42	29967540
387	Phosphorylation	YEGYEGYYSQSQGDS CCCCCCCCCCCCCCC	15.87	22817900
388	Phosphorylation	EGYEGYYSQSQGDSE CCCCCCCCCCCCCCC	18.18	-
390	Phosphorylation	YEGYYSQSQGDSEYY CCCCCCCCCCCCCEE	30.14	24275569
393	Ubiquitination	YYSQSQGDSEYYDYG CCCCCCCCCCEECCC	30.56	23000965
393 (in isoform 3)	Ubiquitination	-	30.56	21890473
396	Phosphorylation	QSQGDSEYYDYGHGE CCCCCCCEECCCCCC	12.94	22817900
397	Phosphorylation	SQGDSEYYDYGHGEV CCCCCCEECCCCCCC	9.91	22817900
407 (in isoform 2)	Ubiquitination	-	14.05	21890473
408	Phosphorylation	HGEVQDSYEAYGQDD CCCCCCHHHHHCCCC	16.93	22817900
411	Phosphorylation	VQDSYEAYGQDDWNG CCCHHHHHCCCCCCC	11.90	-
424	Acetylation	NGTRPSLKAPPARPV CCCCCCCCCCCCCCC	64.28	27452117
424	Ubiquitination	NGTRPSLKAPPARPV CCCCCCCCCCCCCCC	64.28	29967540
432	2-Hydroxyisobutyrylation	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	-
432	Acetylation	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	25953088
432	Methylation	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	100284921
432	Sumoylation	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	28112733
432	Ubiquitination	APPARPVKGAYREHP CCCCCCCCCCCCCCC	40.27	23000965
432 (in isoform 1)	Ubiquitination	-	40.27	21890473
435	Phosphorylation	ARPVKGAYREHPYGR CCCCCCCCCCCCCCC	25.79	28796482
440	Phosphorylation	GAYREHPYGRY---- CCCCCCCCCCC----	19.01	28796482
442	Methylation	YREHPYGRY------ CCCCCCCCC------	28.30	54559001
443	Phosphorylation	REHPYGRY------- CCCCCCCC-------	20.67	25218447

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
58	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
84	T	Phosphorylation	Kinase	MAPK1	P28482	Uniprot
84	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
317	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
435	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
440	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
443	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KHDR1_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 KHDR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAPSN_HUMAN	RAPSN	physical	9804166
CBP_HUMAN	CREBBP	physical	12496368
ANM1_HUMAN	PRMT1	physical	12529443
RASA1_HUMAN	RASA1	physical	11604231
RASA1_HUMAN	RASA1	physical	9743338
SRC_HUMAN	SRC	physical	1545818
CRK_HUMAN	CRK	physical	1545818
RASA1_HUMAN	RASA1	physical	1545818
GRB2_HUMAN	GRB2	physical	10467411
SRC_HUMAN	SRC	physical	10467411
P85A_HUMAN	PIK3R1	physical	10467411
PLCG1_HUMAN	PLCG1	physical	10467411
STAT3_HUMAN	STAT3	physical	11585385
YTDC1_HUMAN	YTHDC1	physical	10564280
KHDR1_HUMAN	KHDRBS1	physical	9315629
HNRPK_HUMAN	HNRNPK	physical	12370808
HNRPK_HUMAN	HNRNPK	genetic	12370808
LCK_HUMAN	LCK	physical	9045636
FYN_HUMAN	FYN	physical	9045636
SMCA2_HUMAN	SMARCA2	physical	16341228
RIPK1_HUMAN	RIPK1	physical	21620750
CASP8_HUMAN	CASP8	physical	21620750
FADD_HUMAN	FADD	physical	21620750
LYN_HUMAN	LYN	physical	22745667
FYN_HUMAN	FYN	physical	22745667
YES_HUMAN	YES1	physical	22745667
P85A_HUMAN	PIK3R1	physical	22745667
ITSN2_HUMAN	ITSN2	physical	22745667
SRC_HUMAN	SRC	physical	22745667
HCK_HUMAN	HCK	physical	22745667
NPHP1_HUMAN	NPHP1	physical	22745667
SNX9_HUMAN	SNX9	physical	22745667
NCK1_HUMAN	NCK1	physical	22745667
OSTF1_HUMAN	OSTF1	physical	22745667
SH3K1_HUMAN	SH3KBP1	physical	22745667
ABI2_HUMAN	ABI2	physical	22745667
AHI1_HUMAN	AHI1	physical	22745667
AMPH_HUMAN	AMPH	physical	22745667
ARHG9_HUMAN	ARHGEF9	physical	22745667
ARHG4_HUMAN	ARHGEF4	physical	22745667
ASPP1_HUMAN	PPP1R13B	physical	22745667
BI2L1_HUMAN	BAIAP2L1	physical	22745667
BTK_HUMAN	BTK	physical	22745667
PPIP1_HUMAN	PSTPIP1	physical	22745667
CD2AP_HUMAN	CD2AP	physical	22745667
DLG1_HUMAN	DLG1	physical	22745667
DLG2_HUMAN	DLG2	physical	22745667
DLG3_HUMAN	DLG3	physical	22745667
DLG4_HUMAN	DLG4	physical	22745667
DOCK2_HUMAN	DOCK2	physical	22745667
DOCK3_HUMAN	DOCK3	physical	22745667
FGR_HUMAN	FGR	physical	22745667
SPD2A_HUMAN	SH3PXD2A	physical	22745667
FRK_HUMAN	FRK	physical	22745667
GRB2_HUMAN	GRB2	physical	22745667
RIMB1_HUMAN	BZRAP1	physical	22745667
ITSN1_HUMAN	ITSN1	physical	22745667
ITK_HUMAN	ITK	physical	22745667
MIA2_HUMAN	MIA2	physical	22745667
MPP6_HUMAN	MPP6	physical	22745667
MYO1C_HUMAN	MYO1C	physical	22745667
MYO7A_HUMAN	MYO7A	physical	22745667
NCK2_HUMAN	NCK2	physical	22745667
NCF1_HUMAN	NCF1	physical	22745667
PACN1_HUMAN	PACSIN1	physical	22745667
SRBS1_HUMAN	SORBS1	physical	22745667
RUSC2_HUMAN	RUSC2	physical	22745667
SASH1_HUMAN	SASH1	physical	22745667
SH3Y1_HUMAN	SH3YL1	physical	22745667
SKAP2_HUMAN	SKAP2	physical	22745667
SNX30_HUMAN	SNX30	physical	22745667
SPT13_HUMAN	SPATA13	physical	22745667
SPN90_HUMAN	NCKIPSD	physical	22745667
UBS3B_HUMAN	UBASH3B	physical	22745667
DNMBP_HUMAN	DNMBP	physical	22745667
VAV_HUMAN	VAV1	physical	22745667
ZDHC6_HUMAN	ZDHHC6	physical	22745667
ZO1_HUMAN	TJP1	physical	22745667
U2AF2_HUMAN	U2AF2	physical	22365833
RALY_HUMAN	RALY	physical	22365833
RBM7_HUMAN	RBM7	physical	22365833
DDX5_HUMAN	DDX5	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
DHX9_HUMAN	DHX9	physical	22365833
CIRBP_HUMAN	CIRBP	physical	22365833
PTBP2_HUMAN	PTBP2	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
PLCG1_HUMAN	PLCG1	physical	8977179
IRS1_HUMAN	IRS1	physical	8175658
P85A_HUMAN	PIK3R1	physical	8175658
P55G_HUMAN	PIK3R3	physical	21988832
RBMX_HUMAN	RBMX	physical	21988832
7B2_HUMAN	SCG5	physical	21988832
SSFA2_HUMAN	SSFA2	physical	21988832
TBL1X_HUMAN	TBL1X	physical	21988832
POTE1_HUMAN	POT1	physical	21988832
ZBT7A_HUMAN	ZBTB7A	physical	24514149
ATX2_HUMAN	ATXN2	physical	26344197
ATX2L_HUMAN	ATXN2L	physical	26344197
COPA_HUMAN	COPA	physical	26344197
DDX17_HUMAN	DDX17	physical	26344197
DHX15_HUMAN	DHX15	physical	26344197
GLRX3_HUMAN	GLRX3	physical	26344197
HNRPR_HUMAN	HNRNPR	physical	26344197
NICA_HUMAN	NCSTN	physical	26344197
PACN3_HUMAN	PACSIN3	physical	26344197
RBM15_HUMAN	RBM15	physical	26344197
HNRPQ_HUMAN	SYNCRIP	physical	26344197
USO1_HUMAN	USO1	physical	26344197
WBP11_HUMAN	WBP11	physical	26344197
BANP_HUMAN	BANP	physical	26080397
HDAC6_HUMAN	HDAC6	physical	26080397
KHDR1_HUMAN	KHDRBS1	physical	16474851
KHDR3_HUMAN	KHDRBS3	physical	16474851
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 KHDR1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-175, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Sam68 RNA binding protein is an in vivo substrate for proteinarginine N-methyltransferase 1."; Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.; Mol. Biol. Cell 14:274-287(2003). Cited for: METHYLATION AT ARG-45; ARG-52; ARG-304; ARG-310; ARG-315; ARG-320 ANDARG-325, AND SUBCELLULAR LOCATION.	12529443 [Abstract]
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-291; ARG-325; ARG-331;ARG-340 AND ARG-346, AND MASS SPECTROMETRY.	15782174 [Abstract]
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-15; SER-18; SER-20 ANDSER-29, AND MASS SPECTROMETRY.	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-58, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	17287340 [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-18 AND THR-33, 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-18 AND SER-20, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Tyrosine phosphorylation of sam68 by breast tumor kinase regulatesintranuclear localization and cell cycle progression."; Lukong K.E., Larocque D., Tyner A.L., Richard S.; J. Biol. Chem. 280:38639-38647(2005). Cited for: PHOSPHORYLATION AT TYR-435; TYR-440 AND TYR-443, SUBCELLULAR LOCATION,AND MUTAGENESIS OF TYR-435; TYR-440 AND TYR-443.	16179349 [Abstract]