dbPTM

ELOC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELOC_HUMAN
UniProt AC	Q15369
Protein Name	Elongin-C
Gene Name	ELOC {ECO:0000312\|HGNC:HGNC:11617}
Organism	Homo sapiens (Human).
Sequence Length	112
Subcellular Localization	Nucleus .
Protein Description	SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). [PubMed: 7821821 In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity; The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.]
Protein Sequence	MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Ubiquitination	--MDGEEKTYGGCEG --CCCCCCCCCCCCC	42.62	-
7	Phosphorylation	-MDGEEKTYGGCEGP -CCCCCCCCCCCCCC	30.58	27642862
8	Phosphorylation	MDGEEKTYGGCEGPD CCCCCCCCCCCCCCC	23.69	29496907
11	S-nitrosocysteine	EEKTYGGCEGPDAMY CCCCCCCCCCCCEEE	4.79	-
11	S-nitrosylation	EEKTYGGCEGPDAMY CCCCCCCCCCCCEEE	4.79	19483679
11	Glutathionylation	EEKTYGGCEGPDAMY CCCCCCCCCCCCEEE	4.79	22555962
16	Ubiquitination	GGCEGPDAMYVKLIS CCCCCCCEEEEEEEC	8.37	19608861
16	Acetylation	GGCEGPDAMYVKLIS CCCCCCCEEEEEEEC	8.37	19608861
17	Sulfoxidation	GCEGPDAMYVKLISS CCCCCCEEEEEEECC	5.28	30846556
18	Phosphorylation	CEGPDAMYVKLISSD CCCCCEEEEEEECCC	8.99	22817900
20	Acetylation	GPDAMYVKLISSDGH CCCEEEEEEECCCCC	23.71	27452117
20	Ubiquitination	GPDAMYVKLISSDGH CCCEEEEEEECCCCC	23.71	-
24	Phosphorylation	MYVKLISSDGHEFIV EEEEEECCCCCEEEE	40.39	-
32	Sumoylation	DGHEFIVKREHALTS CCCEEEEECCEEECC	47.45	19608861
32	Ubiquitination	DGHEFIVKREHALTS CCCEEEEECCEEECC	47.45	21906983
32	Sumoylation	DGHEFIVKREHALTS CCCEEEEECCEEECC	47.45	-
32	Acetylation	DGHEFIVKREHALTS CCCEEEEECCEEECC	47.45	23749302
38	Phosphorylation	VKREHALTSGTIKAM EECCEEECCCCHHHH	26.37	23911959
39	Phosphorylation	KREHALTSGTIKAML ECCEEECCCCHHHHH	34.49	20860994
43	Ubiquitination	ALTSGTIKAMLSGPG EECCCCHHHHHCCCC	27.81	21890473
45	Sulfoxidation	TSGTIKAMLSGPGQF CCCCHHHHHCCCCCC	2.32	21406390
47	Phosphorylation	GTIKAMLSGPGQFAE CCHHHHHCCCCCCCC	29.83	-
67	Phosphorylation	VNFREIPSHVLSKVC CCHHHCCHHHHHHHH	31.71	20068231
71	Phosphorylation	EIPSHVLSKVCMYFT HCCHHHHHHHHHHEE	23.19	20068231
72	Acetylation	IPSHVLSKVCMYFTY CCHHHHHHHHHHEEE	34.98	30592871
72	Ubiquitination	IPSHVLSKVCMYFTY CCHHHHHHHHHHEEE	34.98	-
80	Acetylation	VCMYFTYKVRYTNSS HHHHEEEEEEECCCC	19.71	26051181

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 ELOC_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELOB_HUMAN	TCEB2	physical	16189514
ELOB_HUMAN	TCEB2	physical	10587522
ELOB_HUMAN	TCEB2	physical	7660129
ELOA1_HUMAN	TCEB3	physical	7660129
VHL_HUMAN	VHL	physical	11739384
UBP33_HUMAN	USP33	physical	11739384
ELOB_HUMAN	TCEB2	physical	11739384
SAT2_HUMAN	SAT2	physical	17558023
COMD1_HUMAN	COMMD1	physical	17183367
SRTD1_HUMAN	SERTAD1	physical	20211142
ASB9_HUMAN	ASB9	physical	20211142
MCM7_HUMAN	MCM7	physical	21658608
GAG_HV1H2	gag	physical	19327355
SPSB1_HUMAN	SPSB1	physical	21199876
SPSB2_HUMAN	SPSB2	physical	21199876
SPSB4_HUMAN	SPSB4	physical	21199876
NOS2_HUMAN	NOS2	physical	21199876
CUL5_HUMAN	CUL5	physical	21199876
SPSB3_HUMAN	SPSB3	physical	21199876
CORO7_HUMAN	CORO7	physical	21130766
VIF_HV1B1	vif	physical	20728451
VIF_HV1BR	vif	physical	20728451
VIF_HV1H2	vif	physical	20728451
ASB2_HUMAN	ASB2	physical	21119685
SOCS1_HUMAN	SOCS1	physical	21119685
VIF_HV1B1	vif	physical	20463065
VIF_HV1BR	vif	physical	20463065
VIF_HV1H2	vif	physical	20463065
CUL5_HUMAN	CUL5	physical	20463065
RACK1_HUMAN	GNB2L1	physical	17244529
VIF_HV1B1	vif	physical	15574592
VIF_HV1BR	vif	physical	15574592
VIF_HV1H2	vif	physical	15574592
VIF_HV1B1	vif	physical	19109396
VIF_HV1BR	vif	physical	19109396
VIF_HV1H2	vif	physical	19109396
VHL_HUMAN	VHL	physical	17922844
ELOB_HUMAN	TCEB2	physical	17922844
SOCS2_HUMAN	SOCS2	physical	19159283
RB40B_HUMAN	RAB40B	physical	19159283
SPSB2_HUMAN	SPSB2	physical	19159283
SPSB1_HUMAN	SPSB1	physical	19159283
SPSB4_HUMAN	SPSB4	physical	19159283
ASB9_HUMAN	ASB9	physical	19159283
ASB1_HUMAN	ASB1	physical	19159283
ASB6_HUMAN	ASB6	physical	19159283
ASB8_HUMAN	ASB8	physical	19159283
ASB2_HUMAN	ASB2	physical	19159283
ELOB_HUMAN	TCEB2	physical	19159283
WSB1_HUMAN	WSB1	physical	19159283
CUL2_HUMAN	CUL2	physical	9447969
ORF73_HHV8P	HHV8GK18_gp81	physical	17069461
ZY11B_HUMAN	ZYG11B	physical	17304241
ZER1_HUMAN	ZER1	physical	17304241
VHL_HUMAN	VHL	physical	18187417
PCMD2_HUMAN	PCMTD2	physical	18187417
FEM1B_HUMAN	FEM1B	physical	18187417
ZER1_HUMAN	ZER1	physical	18187417
APBP2_HUMAN	APPBP2	physical	18187417
NRBP_HUMAN	NRBP1	physical	18187417
VIF_HV1B1	vif	physical	18499212
VIF_HV1BR	vif	physical	18499212
VIF_HV1H2	vif	physical	18499212
VIF_HV1B1	vif	physical	15574593
VIF_HV1BR	vif	physical	15574593
VIF_HV1H2	vif	physical	15574593
VHL_HUMAN	VHL	physical	15935760
VIF_HV1B1	vif	physical	22379088
VIF_HV1BR	vif	physical	22379088
VIF_HV1H2	vif	physical	22379088
ELOB_HUMAN	TCEB2	physical	10205047
VHL_HUMAN	VHL	physical	10205047
SOCS3_HUMAN	SOCS3	physical	22084247
SOCS3_HUMAN	SOCS3	physical	12783885
ELOB_HUMAN	TCEB2	physical	10449727
ELOA1_HUMAN	TCEB3	physical	10449727
VHL_HUMAN	VHL	physical	10449727
UBP33_HUMAN	USP33	physical	19706539
WNT7B_HUMAN	WNT7B	physical	21988832
ELOB_HUMAN	TCEB2	physical	23988114
ELOB_HUMAN	TCEB2	physical	21822215
PRAME_HUMAN	PRAME	physical	21822215
CUL5_HUMAN	CUL5	physical	24402281
ELOB_HUMAN	TCEB2	physical	25416956
MT21C_HUMAN	METTL21C	physical	25416956
VIF_HV1B1	vif	physical	23333304
VIF_HV1BR	vif	physical	23333304
VIF_HV1H2	vif	physical	23333304
ELOB_HUMAN	TCEB2	physical	23333304
RHG01_HUMAN	ARHGAP1	physical	26344197
SPRE_HUMAN	SPR	physical	26344197
ELOB_HUMAN	TCEB2	physical	21516116
CUL2_HUMAN	CUL2	physical	26735018
ID2_HUMAN	ID2	physical	26735018
GHR_HUMAN	GHR	physical	25505247
SQSTM_HUMAN	SQSTM1	physical	26743088

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 ELOC_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-32, AND MASS SPECTROMETRY.	19608861 [Abstract]