dbPTM

CD79B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CD79B_HUMAN
UniProt AC	P40259
Protein Name	B-cell antigen receptor complex-associated protein beta chain
Gene Name	CD79B
Organism	Homo sapiens (Human).
Sequence Length	229
Subcellular Localization	Cell membrane Single-pass type I membrane protein. Following antigen binding, the BCR has been shown to translocate from detergent-soluble regions of the cell membrane to lipid rafts although signal transduction through the complex can also occur ou
Protein Description	Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation..
Protein Sequence	MARLALSPVPSHWMVALLLLLSAEPVPAARSEDRYRNPKGSACSRIWQSPRFIARKRGFTVKMHCYMNSASGNVSWLWKQEMDENPQQLKLEKGRMEESQNESLATLTIQGIRFEDNGIYFCQQKCNNTSEVYQGCGTELRVMGFSTLAQLKQRNTLKDGIIMIQTLLIILFIIVPIFLLLDKDDSKAGMEEDHTYEGLDIDQTATYEDIVTLRTGEVKWSVGEHPGQE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MARLALSPVPSHWM -CCCCCCCCCCHHHH	20.46	-
22 (in isoform 3)	Phosphorylation	-	30.47	-
22	Phosphorylation	VALLLLLSAEPVPAA HHHHHHHHCCCCCCC	30.47	-
73	N-linked_Glycosylation	YMNSASGNVSWLWKQ EEECCCCCEEEEEEH	23.35	UniProtKB CARBOHYD
99	Phosphorylation	EKGRMEESQNESLAT HHCCCCHHHCCCCEE	25.62	-
101	N-linked_Glycosylation	GRMEESQNESLATLT CCCCHHHCCCCEEEE	50.53	UniProtKB CARBOHYD
115	Ubiquitination	TIQGIRFEDNGIYFC EEECEEECCCEEEEE	40.49	25015289
116	Ubiquitination	IQGIRFEDNGIYFCQ EECEEECCCEEEEEE	56.81	25015289
127	N-linked_Glycosylation	YFCQQKCNNTSEVYQ EEEEECCCCCCHHHC	62.95	UniProtKB CARBOHYD
128	N-linked_Glycosylation	FCQQKCNNTSEVYQG EEEECCCCCCHHHCC	55.22	UniProtKB CARBOHYD
146	Phosphorylation	ELRVMGFSTLAQLKQ EEHHCCHHHHHHHHH	19.44	-
152 (in isoform 1)	Ubiquitination	-	34.82	21906983
152	Ubiquitination	FSTLAQLKQRNTLKD HHHHHHHHHCCCHHH	34.82	21906983
195	Phosphorylation	AGMEEDHTYEGLDID CCCCCCCCCCCCCCC	35.27	27155012
196	Phosphorylation	GMEEDHTYEGLDIDQ CCCCCCCCCCCCCCC	12.46	27155012
207	Phosphorylation	DIDQTATYEDIVTLR CCCCCEECCCEEEEE	14.78	27155012
219	Ubiquitination	TLRTGEVKWSVGEHP EEECCCEEEECCCCC	29.46	25015289
220	Ubiquitination	LRTGEVKWSVGEHPG EECCCEEEECCCCCC	11.92	25015289
221	Phosphorylation	RTGEVKWSVGEHPGQ ECCCEEEECCCCCCC	17.96	30108239

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
196	Y	Phosphorylation	Kinase	FYN	P06241	PhosphoELM
196	Y	Phosphorylation	Kinase	LYN	P07948	PhosphoELM
196	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot
207	Y	Phosphorylation	Kinase	FYN	P06241	PhosphoELM
207	Y	Phosphorylation	Kinase	LYN	P07948	PhosphoELM
207	Y	Phosphorylation	Kinase	SRC-TYPE TYR-KINASES	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CD79B_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 CD79B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KSYK_HUMAN	SYK	physical	7500027
SGTA_HUMAN	SGTA	physical	25416956
TBRG4_HUMAN	TBRG4	physical	28514442
NF1_HUMAN	NF1	physical	28514442
S12A6_HUMAN	SLC12A6	physical	28514442
TRPM4_HUMAN	TRPM4	physical	28514442
TSC2_HUMAN	TSC2	physical	28514442
CQ062_HUMAN	C17orf62	physical	28514442
ENTP4_HUMAN	ENTPD4	physical	28514442
TMTC4_HUMAN	TMTC4	physical	28514442
MANEA_HUMAN	MANEA	physical	28514442
TMUB2_HUMAN	TMUB2	physical	28514442
TTMP_HUMAN	C3orf52	physical	28514442
ZRAB3_HUMAN	ZRANB3	physical	28514442
GOLI4_HUMAN	GOLIM4	physical	28514442
SCMC3_HUMAN	SLC25A23	physical	28514442
PLAP_HUMAN	PLAA	physical	28514442
EXTL3_HUMAN	EXTL3	physical	28514442
ZNT5_HUMAN	SLC30A5	physical	28514442
B3GN2_HUMAN	B3GNT2	physical	28514442
ERBB2_HUMAN	ERBB2	physical	28514442
RUFY1_HUMAN	RUFY1	physical	28514442
AVR2B_HUMAN	ACVR2B	physical	28514442
KMCP1_HUMAN	SLC25A30	physical	28514442
INT7_HUMAN	INTS7	physical	28514442
HUS1_HUMAN	HUS1	physical	28514442
D19L1_HUMAN	DPY19L1	physical	28514442
NLRX1_HUMAN	NLRX1	physical	28514442
FA69A_HUMAN	FAM69A	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
CXCR4_HUMAN	CXCR4	physical	28514442
WDFY3_HUMAN	WDFY3	physical	28514442
RBGP1_HUMAN	RABGAP1	physical	28514442
TBA1A_HUMAN	TUBA1A	physical	28514442
SGK3_HUMAN	SGK3	physical	28514442
DPOE2_HUMAN	POLE2	physical	28514442
PIGA_HUMAN	PIGA	physical	28514442
SCMC2_HUMAN	SLC25A25	physical	28514442
AT2B2_HUMAN	ATP2B2	physical	28514442
ALG2_HUMAN	ALG2	physical	28514442
VPS52_HUMAN	VPS52	physical	28514442
INT4_HUMAN	INTS4	physical	28514442
GDC_HUMAN	SLC25A16	physical	28514442
ADCY3_HUMAN	ADCY3	physical	28514442
COL12_HUMAN	COLEC12	physical	28514442
DUSTY_HUMAN	DSTYK	physical	28514442
D2HDH_HUMAN	D2HGDH	physical	28514442
ALG8_HUMAN	ALG8	physical	28514442
DSE_HUMAN	DSE	physical	28514442
AB17B_HUMAN	ABHD17B	physical	28514442
GOGA5_HUMAN	GOLGA5	physical	28514442
VPS51_HUMAN	VPS51	physical	28514442
RPTOR_HUMAN	RPTOR	physical	28514442
FA8A1_HUMAN	FAM8A1	physical	28514442
UCP5_HUMAN	SLC25A14	physical	28514442
GCP3_HUMAN	TUBGCP3	physical	28514442
LTN1_HUMAN	LTN1	physical	28514442
MFAP3_HUMAN	MFAP3	physical	28514442
AT8B2_HUMAN	ATP8B2	physical	28514442
XPR1_HUMAN	XPR1	physical	28514442
AT132_HUMAN	ATP13A2	physical	28514442
INT5_HUMAN	INTS5	physical	28514442
KDIS_HUMAN	KIDINS220	physical	28514442
BIG2_HUMAN	ARFGEF2	physical	28514442
ABCA3_HUMAN	ABCA3	physical	28514442
MELK_HUMAN	MELK	physical	28514442
HELLS_HUMAN	HELLS	physical	28514442
ADT3_HUMAN	SLC25A6	physical	28514442
GRM1A_HUMAN	GRAMD1A	physical	28514442
HEAT6_HUMAN	HEATR6	physical	28514442
CQ080_HUMAN	C17orf80	physical	28514442
XYLK_HUMAN	FAM20B	physical	28514442
SRBP2_HUMAN	SREBF2	physical	28514442
IPRI_HUMAN	ITPRIP	physical	28514442
KIRR1_HUMAN	KIRREL	physical	28514442
MYO19_HUMAN	MYO19	physical	28514442
PDE3B_HUMAN	PDE3B	physical	28514442
AP3M1_HUMAN	AP3M1	physical	28514442
MICU1_HUMAN	MICU1	physical	28514442
TIM29_HUMAN	C19orf52	physical	28514442
F189B_HUMAN	FAM189B	physical	28514442
TARB1_HUMAN	TARBP1	physical	28514442
SG196_HUMAN	POMK	physical	28514442
ATLA2_HUMAN	ATL2	physical	28514442
VANG2_HUMAN	VANGL2	physical	28514442
EXT1_HUMAN	EXT1	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
PLPL6_HUMAN	PNPLA6	physical	28514442
MA1B1_HUMAN	MAN1B1	physical	28514442
FGFR1_HUMAN	FGFR1	physical	28514442
LGR4_HUMAN	LGR4	physical	28514442
VPS50_HUMAN	CCDC132	physical	28514442

Drug and Disease Associations

Kegg Disease
H00085	Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
OMIM Disease
612692	Agammaglobulinemia 6, autosomal recessive (AGM6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CD79B_HUMAN

Related Literatures of Post-Translational Modification