dbPTM

KCMF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCMF1_HUMAN
UniProt AC	Q9P0J7
Protein Name	E3 ubiquitin-protein ligase KCMF1
Gene Name	KCMF1
Organism	Homo sapiens (Human).
Sequence Length	381
Subcellular Localization
Protein Description	Has intrinsic E3 ubiquitin ligase activity and promotes ubiquitination..
Protein Sequence	MSRHEGVSCDACLKGNFRGRRYKCLICYDYDLCASCYESGATTTRHTTDHPMQCILTRVDFDLYYGGEAFSVEQPQSFTCPYCGKMGYTETSLQEHVTSEHAETSTEVICPICAALPGGDPNHVTDDFAAHLTLEHRAPRDLDESSGVRHVRRMFHPGRGLGGPRARRSNMHFTSSSTGGLSSSQSSYSPSNREAMDPIAELLSQLSGVRRSAGGQLNSSGPSASQLQQLQMQLQLERQHAQAARQQLETARNATRRTNTSSVTTTITQSTATTNIANTESSQQTLQNSQFLLTRLNDPKMSETERQSMESERADRSLFVQELLLSTLVREESSSSDEDDRGEMADFGAMGCVDIMPLDVALENLNLKESNKGNEPPPPPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRHEGVSC ------CCCCCCCCC	42.20	23401153
2	Acetylation	------MSRHEGVSC ------CCCCCCCCC	42.20	20068231
3	Methylation	-----MSRHEGVSCD -----CCCCCCCCCH	30.49	115389043
8	Phosphorylation	MSRHEGVSCDACLKG CCCCCCCCCHHHHCC	19.69	25850435
14	Ubiquitination	VSCDACLKGNFRGRR CCCHHHHCCCCCCCC	52.25	21963094
14	Acetylation	VSCDACLKGNFRGRR CCCHHHHCCCCCCCC	52.25	25953088
44	Phosphorylation	YESGATTTRHTTDHP HHCCCCCCCCCCCCC	18.99	-
145	Phosphorylation	APRDLDESSGVRHVR CCCCCCCCCCCCHHH	31.87	28857561
146	Phosphorylation	PRDLDESSGVRHVRR CCCCCCCCCCCHHHH	38.98	28857561
147	Ubiquitination	RDLDESSGVRHVRRM CCCCCCCCCCHHHHH	29.74	24816145
149	Methylation	LDESSGVRHVRRMFH CCCCCCCCHHHHHCC	26.55	80701643
159	Dimethylation	RRMFHPGRGLGGPRA HHHCCCCCCCCCCCC	41.43	-
159	Methylation	RRMFHPGRGLGGPRA HHHCCCCCCCCCCCC	41.43	24394915
165	Dimethylation	GRGLGGPRARRSNMH CCCCCCCCCCCCCCE	43.96	-
165	Methylation	GRGLGGPRARRSNMH CCCCCCCCCCCCCCE	43.96	30762465
167	Methylation	GLGGPRARRSNMHFT CCCCCCCCCCCCEEE	43.79	54556979
168	Methylation	LGGPRARRSNMHFTS CCCCCCCCCCCEEEC	31.25	115480851
169	Phosphorylation	GGPRARRSNMHFTSS CCCCCCCCCCEEECC	32.71	21945579
174	Phosphorylation	RRSNMHFTSSSTGGL CCCCCEEECCCCCCC	17.02	21945579
175	O-linked_Glycosylation	RSNMHFTSSSTGGLS CCCCEEECCCCCCCC	22.73	28510447
175	Phosphorylation	RSNMHFTSSSTGGLS CCCCEEECCCCCCCC	22.73	21945579
176	Phosphorylation	SNMHFTSSSTGGLSS CCCEEECCCCCCCCC	28.94	21945579
177	Phosphorylation	NMHFTSSSTGGLSSS CCEEECCCCCCCCCC	30.73	21945579
178	Phosphorylation	MHFTSSSTGGLSSSQ CEEECCCCCCCCCCC	36.90	21945579
182	Phosphorylation	SSSTGGLSSSQSSYS CCCCCCCCCCCCCCC	31.08	21945579
183	Phosphorylation	SSTGGLSSSQSSYSP CCCCCCCCCCCCCCC	37.12	21945579
184	Phosphorylation	STGGLSSSQSSYSPS CCCCCCCCCCCCCCC	30.61	21945579
186	Phosphorylation	GGLSSSQSSYSPSNR CCCCCCCCCCCCCCH	32.94	21945579
187	Phosphorylation	GLSSSQSSYSPSNRE CCCCCCCCCCCCCHH	23.22	21945579
188	Phosphorylation	LSSSQSSYSPSNREA CCCCCCCCCCCCHHH	29.82	21945579
189	Phosphorylation	SSSQSSYSPSNREAM CCCCCCCCCCCHHHH	24.65	21945579
191	Phosphorylation	SQSSYSPSNREAMDP CCCCCCCCCHHHHHH	42.45	21945579
196	Sulfoxidation	SPSNREAMDPIAELL CCCCHHHHHHHHHHH	5.58	30846556
204	Phosphorylation	DPIAELLSQLSGVRR HHHHHHHHHHHCCCC	41.52	30576142
207	Phosphorylation	AELLSQLSGVRRSAG HHHHHHHHCCCCCCC	27.83	20068231
212	Phosphorylation	QLSGVRRSAGGQLNS HHHCCCCCCCCCCCC	22.24	30175587
219	Phosphorylation	SAGGQLNSSGPSASQ CCCCCCCCCCCCHHH	45.31	29978859
220	Phosphorylation	AGGQLNSSGPSASQL CCCCCCCCCCCHHHH	54.36	29978859
223	Phosphorylation	QLNSSGPSASQLQQL CCCCCCCCHHHHHHH	44.04	26657352
225	Phosphorylation	NSSGPSASQLQQLQM CCCCCCHHHHHHHHH	35.44	29978859
249	Ubiquitination	QAARQQLETARNATR HHHHHHHHHHHHHCH	35.76	24816145
300	Malonylation	LTRLNDPKMSETERQ HHHHCCCCCCHHHHH	58.90	26320211
300	Ubiquitination	LTRLNDPKMSETERQ HHHHCCCCCCHHHHH	58.90	24816145
300	Acetylation	LTRLNDPKMSETERQ HHHHCCCCCCHHHHH	58.90	25953088
308	Ubiquitination	MSETERQSMESERAD CCHHHHHHHHHHHHH	30.64	24816145
333	Phosphorylation	STLVREESSSSDEDD HHHHHCCCCCCCCCC	30.66	24275569
334	Phosphorylation	TLVREESSSSDEDDR HHHHCCCCCCCCCCH	36.82	24275569
335	Phosphorylation	LVREESSSSDEDDRG HHHCCCCCCCCCCHH	51.60	24275569
336	Phosphorylation	VREESSSSDEDDRGE HHCCCCCCCCCCHHH	47.14	24275569
372	Ubiquitination	LNLKESNKGNEPPPP CCCCCCCCCCCCCCC	72.84	-

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 KCMF1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCMF1_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 KCMF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BYST_HUMAN	BYSL	physical	22863883
EIF3L_HUMAN	EIF3L	physical	22863883
FLNC_HUMAN	FLNC	physical	22863883
VIGLN_HUMAN	HDLBP	physical	22863883
HERC1_HUMAN	HERC1	physical	22863883
NEMO_HUMAN	IKBKG	physical	22863883
PNO1_HUMAN	PNO1	physical	22863883
PRS4_HUMAN	PSMC1	physical	22863883
PRS8_HUMAN	PSMC5	physical	22863883
PSD11_HUMAN	PSMD11	physical	22863883
PSD12_HUMAN	PSMD12	physical	22863883
PSD13_HUMAN	PSMD13	physical	22863883
PSMD3_HUMAN	PSMD3	physical	22863883
PSMD7_HUMAN	PSMD7	physical	22863883
PSMD8_HUMAN	PSMD8	physical	22863883
RS13_HUMAN	RPS13	physical	22863883
ZO2_HUMAN	TJP2	physical	22863883
TXNL1_HUMAN	TXNL1	physical	22863883
UBR4_HUMAN	UBR4	physical	22863883
UCHL5_HUMAN	UCHL5	physical	22863883
WDR26_HUMAN	WDR26	physical	22863883
PYM1_HUMAN	WIBG	physical	22863883
KCMF1_HUMAN	KCMF1	physical	15581609
UB2D2_HUMAN	UBE2D2	physical	15581609
UBR4_HUMAN	UBR4	physical	26186194
ABHDA_HUMAN	ABHD10	physical	26186194
SYSM_HUMAN	SARS2	physical	26186194
IDHP_HUMAN	IDH2	physical	26186194
CEP85_HUMAN	CEP85	physical	26186194
NPS3A_HUMAN	NIPSNAP3A	physical	26186194
MRS2_HUMAN	MRS2	physical	26186194
UBR4_HUMAN	UBR4	physical	25582440
NIPS1_HUMAN	NIPSNAP1	physical	25582440
NPS3A_HUMAN	NIPSNAP3A	physical	25582440
ABHDA_HUMAN	ABHD10	physical	25582440
SSBP_HUMAN	SSBP1	physical	25582440
SYSM_HUMAN	SARS2	physical	25582440
ACOT9_HUMAN	ACOT9	physical	25582440
NU188_HUMAN	NUP188	physical	25582440
OGT1_HUMAN	OGT	physical	25582440
NUP93_HUMAN	NUP93	physical	25582440
NU214_HUMAN	NUP214	physical	25582440
PCP_HUMAN	PRCP	physical	25582440
SYQ_HUMAN	QARS	physical	25582440
UBE2A_HUMAN	UBE2A	physical	25582440
UBE2B_HUMAN	UBE2B	physical	25582440
NPS3A_HUMAN	NIPSNAP3A	physical	28514442
UBR4_HUMAN	UBR4	physical	28514442
ABHDA_HUMAN	ABHD10	physical	28514442
IDHP_HUMAN	IDH2	physical	28514442
SYSM_HUMAN	SARS2	physical	28514442
CEP85_HUMAN	CEP85	physical	28514442
MRS2_HUMAN	MRS2	physical	28514442

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 KCMF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-2, AND MASSSPECTROMETRY.	18691976 [Abstract]