CD79A_HUMAN - dbPTM
CD79A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD79A_HUMAN
UniProt AC P11912
Protein Name B-cell antigen receptor complex-associated protein alpha chain
Gene Name CD79A
Organism Homo sapiens (Human).
Sequence Length 226
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 CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells..
Protein Sequence MPGGPGVLQALPATIFLLFLLSAVYLGPGCQALWMHKVPASLMVSLGEDAHFQCPHNSSNNANVTWWRVLHGNYTWPPEFLGPGEDPNGTLIIQNVNKSHGGIYVCRVQEGNESYQQSCGTYLRVRQPPPRPFLDMGEGTKNRIITAEGIILLFCAVVPGTLLLFRKRWQNEKLGLDAGDEYEDENLYEGLNLDDCSMYEDISRGLQGTYQDVGSLNIGDVQLEKP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
57N-linked_GlycosylationAHFQCPHNSSNNANV
CCCCCCCCCCCCCCE
32.07UniProtKB CARBOHYD
63N-linked_GlycosylationHNSSNNANVTWWRVL
CCCCCCCCEEEEEEE
33.60UniProtKB CARBOHYD
73N-linked_GlycosylationWWRVLHGNYTWPPEF
EEEEEECCCCCCHHH
21.95UniProtKB CARBOHYD
88N-linked_GlycosylationLGPGEDPNGTLIIQN
CCCCCCCCCCEEEEE
69.29UniProtKB CARBOHYD
97N-linked_GlycosylationTLIIQNVNKSHGGIY
CEEEEECCCCCCCEE
47.89UniProtKB CARBOHYD
112N-linked_GlycosylationVCRVQEGNESYQQSC
EEEEEECCCEEHHHC
34.00UniProtKB CARBOHYD
140PhosphorylationFLDMGEGTKNRIITA
CCCCCCCCCCEEEEE
22.35-
141UbiquitinationLDMGEGTKNRIITAE
CCCCCCCCCEEEEEH
55.9025015289
161PhosphorylationFCAVVPGTLLLFRKR
HHHHCCCHHHHHHHH
14.259531288
173UbiquitinationRKRWQNEKLGLDAGD
HHHHHCCCCCCCCCC
56.24-
182PhosphorylationGLDAGDEYEDENLYE
CCCCCCCCCCCCCCC
33.1622817900
187UbiquitinationDEYEDENLYEGLNLD
CCCCCCCCCCCCCHH
3.7629967540
188PhosphorylationEYEDENLYEGLNLDD
CCCCCCCCCCCCHHH
21.3822817900
197PhosphorylationGLNLDDCSMYEDISR
CCCHHHCCHHHHHHH
31.2425954137
199PhosphorylationNLDDCSMYEDISRGL
CHHHCCHHHHHHHHC
8.3122817900
204Asymmetric dimethylarginineSMYEDISRGLQGTYQ
CHHHHHHHHCCCCCC
50.61-
204MethylationSMYEDISRGLQGTYQ
CHHHHHHHHCCCCCC
50.61-
209PhosphorylationISRGLQGTYQDVGSL
HHHHCCCCCCCCCCC
12.6828796482
210PhosphorylationSRGLQGTYQDVGSLN
HHHCCCCCCCCCCCE
15.0028796482
215PhosphorylationGTYQDVGSLNIGDVQ
CCCCCCCCCEECCEE
20.3526657352
225UbiquitinationIGDVQLEKP------
ECCEEECCC------
65.7029967540

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
188YPhosphorylationKinaseLYNP07948
PhosphoELM
188YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot
199YPhosphorylationKinaseFYNP06241
PhosphoELM
199YPhosphorylationKinaseSRC-TYPE TYR-KINASES-Uniprot
210YPhosphorylationKinaseTYR-KINASES-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD79A_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 CD79A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD79B_HUMANCD79Bphysical
12886015
KSYK_HUMANSYKphysical
7500027
AMBP_HUMANAMBPphysical
6196366
BLNK_HUMANBLNKphysical
11909947
CD79B_HUMANCD79Bphysical
9531288
FATE1_HUMANFATE1physical
25416956
ATP23_HUMANXRCC6BP1physical
28514442
NDKM_HUMANNME4physical
28514442
TTC28_HUMANTTC28physical
28514442
NTCP7_HUMANSLC10A7physical
28514442
MTG2_HUMANMTG2physical
28514442
CDYL_HUMANCDYLphysical
28514442
MET15_HUMANMETTL15physical
28514442
SYHM_HUMANHARS2physical
28514442
TYK2_HUMANTYK2physical
28514442
MICU1_HUMANMICU1physical
28514442
NSUN3_HUMANNSUN3physical
28514442
GTPB6_HUMANGTPBP6physical
28514442
PEX16_HUMANPEX16physical
28514442
PEX6_HUMANPEX6physical
28514442
KMCP1_HUMANSLC25A30physical
28514442
ABD18_HUMANC4orf29physical
28514442
UFSP2_HUMANUFSP2physical
28514442
NEK4_HUMANNEK4physical
28514442
GTR8_HUMANSLC2A8physical
28514442
TBB3_HUMANTUBB3physical
28514442
RL23_HUMANRPL23physical
28514442
DEGS1_HUMANDEGS1physical
28514442
S26A6_HUMANSLC26A6physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
TBB8_HUMANTUBB8physical
28514442
DD19B_HUMANDDX19Bphysical
28514442
NOCT_HUMANCCRN4Lphysical
28514442
PAPD1_HUMANMTPAPphysical
28514442
SPG7_HUMANSPG7physical
28514442
BCAM_HUMANBCAMphysical
28514442
PTPM1_HUMANPTPMT1physical
28514442
UBP30_HUMANUSP30physical
28514442
BDH_HUMANBDH1physical
28514442

Drug and Disease Associations
Kegg Disease
H00001 Acute lymphoblastic leukemia (ALL) (precursor B lymphoblastic leukemia)
H00085 Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
OMIM Disease
613501Agammaglobulinemia 3, autosomal recessive (AGM3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD79A_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP