CD19_HUMAN - dbPTM
CD19_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD19_HUMAN
UniProt AC P15391
Protein Name B-lymphocyte antigen CD19
Gene Name CD19
Organism Homo sapiens (Human).
Sequence Length 556
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Assembles with the antigen receptor of B-lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation..
Protein Sequence MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLRRKRKRMTDPTRRFFKVTPPPGSGPQNQYGNVLSLPTPTSGLGRAQRWAAGLGGTAPSYGNPSSDVQADGALGSRSPPGVGPEEEEGEGYEEPDSEEDSEFYENDSNLGQDQLSQDGSGYENPEDEPLGPEDEDSFSNAESYENEDEELTQPVARTMDFLSPHGSAWDPSREATSLGSQSYEDMRGILYAAPQLRSIRGQPGPNHEEDADSYENMDNPDGPDPAWGGGGRMGTWSTR
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
56PhosphorylationQLTWSRESPLKPFLK
EEEECCCCCCHHHHH		34.1324719451
86N-linked_GlycosylationAIWLFIFNVSQQMGG
HHHHHHCCHHHHCCC		27.9329490423
125N-linked_GlycosylationSGELFRWNVSDLGGL
CCEEEEEEHHHCCCC		21.1129490423
138N-linked_GlycosylationGLGCGLKNRSSEGPS
CCCCCCCCCCCCCCC		54.85UniProtKB CARBOHYD
181N-linked_GlycosylationLPPRDSLNQSLSQDL
CCCCCCCCHHHCCCC		33.09UniProtKB CARBOHYD
227PhosphorylationKGPKSLLSLELKDDR
CCCCCEEEEEECCCC		25.70-
265N-linked_GlycosylationKYYCHRGNLTMSFHL
CEEEECCCEEEEEEE		32.09UniProtKB CARBOHYD
337PhosphorylationTRRFFKVTPPPGSGP
CCCCEECCCCCCCCC		30.5730108239
342PhosphorylationKVTPPPGSGPQNQYG
ECCCCCCCCCCCCCC		53.7427155012
348PhosphorylationGSGPQNQYGNVLSLP
CCCCCCCCCCEECCC		20.4410706702
353PhosphorylationNQYGNVLSLPTPTSG
CCCCCEECCCCCCCC		28.2028348404
356PhosphorylationGNVLSLPTPTSGLGR
CCEECCCCCCCCCCH		44.48-
378PhosphorylationLGGTAPSYGNPSSDV
CCCCCCCCCCCCHHC		21.6210706702
409PhosphorylationEEEEGEGYEEPDSEE
HHCCCCCCCCCCCHH		16.9010706702
439PhosphorylationLSQDGSGYENPEDEP
CCCCCCCCCCCCCCC		17.7710706702
475PhosphorylationLTQPVARTMDFLSPH
HHHHHHHHHHHHCCC		16.0330108239
480PhosphorylationARTMDFLSPHGSAWD
HHHHHHHCCCCCCCC		18.1630108239
484PhosphorylationDFLSPHGSAWDPSRE
HHHCCCCCCCCCCCC		24.1330108239
489PhosphorylationHGSAWDPSREATSLG
CCCCCCCCCCCCCCC		40.0430108239
493PhosphorylationWDPSREATSLGSQSY
CCCCCCCCCCCCCCH		21.5230108239
493 (in isoform 2)Phosphorylation-21.5230108239
494PhosphorylationDPSREATSLGSQSYE
CCCCCCCCCCCCCHH		37.4730108239
494 (in isoform 2)Phosphorylation-37.4730108239
497PhosphorylationREATSLGSQSYEDMR
CCCCCCCCCCHHHHH		22.6517525332
498 (in isoform 2)Phosphorylation-48.5130108239
499PhosphorylationATSLGSQSYEDMRGI
CCCCCCCCHHHHHHH		31.9930108239
500 (in isoform 2)Phosphorylation-14.3330108239
500PhosphorylationTSLGSQSYEDMRGIL
CCCCCCCHHHHHHHH		14.3327155012
501 (in isoform 2)Phosphorylation-51.0530108239
508PhosphorylationEDMRGILYAAPQLRS
HHHHHHHHHHHHHHH		9.9729978859
509PhosphorylationDMRGILYAAPQLRSI
HHHHHHHHHHHHHHC		14.8227642862
515PhosphorylationYAAPQLRSIRGQPGP
HHHHHHHHCCCCCCC		25.8127251275
516PhosphorylationAAPQLRSIRGQPGPN
HHHHHHHCCCCCCCC		4.6627251275
530PhosphorylationNHEEDADSYENMDNP
CCHHCCHHHCCCCCC		35.7521552520
531PhosphorylationHEEDADSYENMDNPD
CHHCCHHHCCCCCCC		16.3329490423
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
500YPhosphorylationKinaseLYNP07948
PSP
508YPhosphorylationKinaseABL1P00519
GPS
531YPhosphorylationKinaseLYNP07948
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD19_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 CD19_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD81_HUMANCD81physical
1383329
IFM1_HUMANIFITM1physical
1383329
CR2_HUMANCR2physical
1383329
CD81_HUMANCD81physical
7636191
CD82_HUMANCD82physical
7636191
VAV_HUMANVAV1physical
7528218
CD22_HUMANCD22physical
9120258
KSYK_HUMANSYKphysical
9120258
CD79A_HUMANCD79Aphysical
9120258
CD79B_HUMANCD79Bphysical
9120258
CD9_HUMANCD9physical
9804823
CR2_HUMANCR2physical
9804823
CD81_HUMANCD81physical
9804823
CD82_HUMANCD82physical
9804823
VAV_HUMANVAV1physical
16289966
MYZAP_HUMANPOLR2Mphysical
26186194
GRL1A_HUMANPOLR2Mphysical
26186194
GL1AD_HUMANPOLR2Mphysical
26186194
MINY3_HUMANFAM188Aphysical
26186194
B3GN3_HUMANB3GNT3physical
26186194
CD82_HUMANCD82physical
25241761
MYZAP_HUMANPOLR2Mphysical
28514442
GRL1A_HUMANPOLR2Mphysical
28514442
GL1AD_HUMANPOLR2Mphysical
28514442
MINY3_HUMANFAM188Aphysical
28514442
B3GN3_HUMANB3GNT3physical
28514442
IGSF8_HUMANIGSF8physical
28514442
Drug and Disease Associations
Kegg Disease
H00001 Acute lymphoblastic leukemia (ALL) (precursor B lymphoblastic leukemia)
H00011 Lymphoplasmacytic lymphoma
H00088 Common variable immunodeficiency (CVID), including the following four diseases: Inducible T Cell cos
OMIM Disease
613493Immunodeficiency, common variable, 3 (CVID3)
Kegg Drug
D09325 Blinatumomab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD19_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASSSPECTROMETRY.
"Systematic analysis of the role of CD19 cytoplasmic tyrosines inenhancement of activation in Daudi human B cells: clustering ofphospholipase C and Vav and of Grb2 and Sos with different CD19tyrosines.";
Brooks S.R., Li X., Volanakis E.J., Carter R.H.;
J. Immunol. 164:3123-3131(2000).
Cited for: INTERACTION WITH GRB2; SOS; VAV AND PLCG2, AND PHOSPHORYLATION ATTYR-348; TYR-378; TYR-409 AND TYR-439.

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