dbPTM

ELOB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ELOB_HUMAN
UniProt AC	Q15370
Protein Name	Elongin-B
Gene Name	ELOB {ECO:0000312\|HGNC:HGNC:11619}
Organism	Homo sapiens (Human).
Sequence Length	118
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: 7638163 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	MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDVFLMIR -------CCEEEEEE	10.01	22814378
11	Acetylation	FLMIRRHKTTIFTDA EEEEECCCEEEECCC	45.62	11571253
13	Phosphorylation	MIRRHKTTIFTDAKE EEECCCEEEECCCCC	20.92	-
16	Phosphorylation	RHKTTIFTDAKESST CCCEEEECCCCCCCC	31.06	-
19	Ubiquitination	TTIFTDAKESSTVFE EEEECCCCCCCCHHH	62.02	-
28	Succinylation	SSTVFELKRIVEGIL CCCHHHHHHHHHHHH	32.64	23954790
28	Acetylation	SSTVFELKRIVEGIL CCCHHHHHHHHHHHH	32.64	27452117
28	Ubiquitination	SSTVFELKRIVEGIL CCCHHHHHHHHHHHH	32.64	-
36	Ubiquitination	RIVEGILKRPPDEQR HHHHHHHCCCCCHHH	62.02	21890473
36	Acetylation	RIVEGILKRPPDEQR HHHHHHHCCCCCHHH	62.02	25953088
36	Ubiquitination	RIVEGILKRPPDEQR HHHHHHHCCCCCHHH	62.02	21890473
43	Methylation	KRPPDEQRLYKDDQL CCCCCHHHCCCCCCC	37.63	115918313
45	Nitration	PPDEQRLYKDDQLLD CCCHHHCCCCCCCCC	17.98	-
46	Sumoylation	PDEQRLYKDDQLLDD CCHHHCCCCCCCCCC	60.46	-
46	Acetylation	PDEQRLYKDDQLLDD CCHHHCCCCCCCCCC	60.46	25953088
46	Ubiquitination	PDEQRLYKDDQLLDD CCHHHCCCCCCCCCC	60.46	21890473
46	Ubiquitination	PDEQRLYKDDQLLDD CCHHHCCCCCCCCCC	60.46	2189047
55	Ubiquitination	DQLLDDGKTLGECGF CCCCCCCCCCCCCCC	47.79	-
55	Acetylation	DQLLDDGKTLGECGF CCCCCCCCCCCCCCC	47.79	26051181
74	Phosphorylation	ARPQAPATVGLAFRA CCCCCCCEEEEEEEC	17.66	-
74	O-linked_Glycosylation	ARPQAPATVGLAFRA CCCCCCCEEEEEEEC	17.66	OGP
84	Phosphorylation	LAFRADDTFEALCIE EEEECCCCEEEEEEC	24.75	29507054
89	Glutathionylation	DDTFEALCIEPFSSP CCCEEEEEECCCCCC	4.22	22555962
94	Phosphorylation	ALCIEPFSSPPELPD EEEECCCCCCCCCCC	53.29	26074081
95	Phosphorylation	LCIEPFSSPPELPDV EEECCCCCCCCCCCC	44.87	26074081
103	Sulfoxidation	PPELPDVMKPQDSGS CCCCCCCCCCCCCCC	7.36	30846556
104	Ubiquitination	PELPDVMKPQDSGSS CCCCCCCCCCCCCCC	39.10	-
108	Phosphorylation	DVMKPQDSGSSANEQ CCCCCCCCCCCHHHH	35.01	26074081
110	Phosphorylation	MKPQDSGSSANEQAV CCCCCCCCCHHHHHC	30.17	26074081
111	Phosphorylation	KPQDSGSSANEQAVQ CCCCCCCCHHHHHCC	38.34	26074081
133 (in isoform 2)	Phosphorylation	-		25106551

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 ELOB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELOA1_HUMAN	TCEB3	physical	7660129
CUL2_HUMAN	CUL2	physical	12048197
RBX1_HUMAN	RBX1	physical	12048197
ELOA1_HUMAN	TCEB3	physical	12048197
VHL_HUMAN	VHL	physical	12048197
GAG_HV1H2	gag	physical	19327355
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
CUL5_HUMAN	CUL5	physical	21119685
MED8_HUMAN	MED8	physical	12149480
VIF_HV1B1	vif	physical	20463065
VIF_HV1BR	vif	physical	20463065
VIF_HV1H2	vif	physical	20463065
CUL5_HUMAN	CUL5	physical	20463065
PFD5_HUMAN	PFDN5	physical	17786314
ELOC_HUMAN	TCEB1	physical	17922844
VHL_HUMAN	VHL	physical	17922844
ZY11B_HUMAN	ZYG11B	physical	17304241
ZER1_HUMAN	ZER1	physical	17304241
ELOC_HUMAN	TCEB1	physical	10224134
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
VHL_HUMAN	VHL	physical	15935760
ELOC_HUMAN	TCEB1	physical	10449727
VHL_HUMAN	VHL	physical	10449727
ELOC_HUMAN	TCEB1	physical	22939629
UBP33_HUMAN	USP33	physical	19706539
VIF_HV1B1	vif	physical	23988114
VIF_HV1BR	vif	physical	23988114
VIF_HV1H2	vif	physical	23988114
SYEP_HUMAN	EPRS	physical	22863883
SYLC_HUMAN	LARS	physical	22863883
LRC47_HUMAN	LRRC47	physical	22863883
ELOC_HUMAN	TCEB1	physical	22863883
PRAME_HUMAN	PRAME	physical	21822215
CUL5_HUMAN	CUL5	physical	24402281
VIF_HV1B1	vif	physical	23333304
VIF_HV1BR	vif	physical	23333304
VIF_HV1H2	vif	physical	23333304
AP1S1_HUMAN	AP1S1	physical	26344197
FA50A_HUMAN	FAM50A	physical	26344197
ELOC_HUMAN	TCEB1	physical	26344197
GHR_HUMAN	GHR	physical	25505247
SQSTM_HUMAN	SQSTM1	physical	26743088
INTU_HUMAN	INTU	physical	27173435

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 ELOB_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]