CD22_HUMAN - dbPTM
CD22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CD22_HUMAN
UniProt AC P20273
Protein Name B-cell receptor CD22
Gene Name CD22
Organism Homo sapiens (Human).
Sequence Length 847
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules..
Protein Sequence MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLRMESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNTTIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQGLQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAESSEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH
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
67N-linked_GlycosylationHNPEYNKNTSKFDGT
CCCCCCCCCCCCCCC		46.04UniProtKB CARBOHYD
101N-linked_GlycosylationFLGDKNKNCTLSIHP
ECCCCCCCEEEEEEE		33.148702538
101N-linked_GlycosylationFLGDKNKNCTLSIHP
ECCCCCCCEEEEEEE		33.14UniProtKB CARBOHYD
112N-linked_GlycosylationSIHPVHLNDSGQLGL
EEEEEECCCCCCEEE		26.90UniProtKB CARBOHYD
135N-linked_GlycosylationWMERIHLNVSERPFP
HHHHHCCCCCCCCCC		22.55UniProtKB CARBOHYD
164N-linked_GlycosylationVTLTCLLNFSCYGYP
EEEEEEEECEECCCC		17.52UniProtKB CARBOHYD
192PhosphorylationQAAVTSTSLTIKSVF
CCCCEECCEEEEECE		24.2324719451
231N-linked_GlycosylationADGKFLSNDTVQLNV
CCCCCCCCCEEEEEC		51.63UniProtKB CARBOHYD
288SumoylationKDGTSLKKQNTFTLN
CCCCCCCCCCEEEEE		54.82-
288SumoylationKDGTSLKKQNTFTLN
CCCCCCCCCCEEEEE		54.8225218447
291PhosphorylationTSLKKQNTFTLNLRE
CCCCCCCEEEEECEE		18.5929759185
293PhosphorylationLKKQNTFTLNLREVT
CCCCCEEEEECEEEC		16.8229759185
300PhosphorylationTLNLREVTKDQSGKY
EEECEEECCCCCCCE		24.9329759185
363N-linked_GlycosylationLANPLPTNYTWYHNG
CCCCCCCCCEEEECC		30.23UniProtKB CARBOHYD
445N-linked_GlycosylationVTLSCNYNSSNPSVT
EEEEEECCCCCCCCE		25.60UniProtKB CARBOHYD
448N-linked_GlycosylationSCNYNSSNPSVTRYE
EEECCCCCCCCEEEE		32.46UniProtKB CARBOHYD
479N-linked_GlycosylationIQNVGWDNTTIACAA
EEECCCCCCEEEHHH		32.39UniProtKB CARBOHYD
574N-linked_GlycosylationGSYSCWVNNSIGQTA
CCCEEEECCCCCCCC		16.42UniProtKB CARBOHYD
591PhosphorylationAWTLEVLYAPRRLRV
CEEEEEEECCCEEEE		21.53-
634N-linked_GlycosylationYTWFDWNNQSLPYHS
EEEECCCCCCCCCCC		28.67UniProtKB CARBOHYD
715PhosphorylationLQRRWKRTQSQQGLQ
HHHHHHHHHHHHHCC		28.9230108239
717PhosphorylationRRWKRTQSQQGLQEN
HHHHHHHHHHHCCCC		24.6929507054
725PhosphorylationQQGLQENSSGQSFFV
HHHCCCCCCCCCEEE		34.7830108239
726PhosphorylationQGLQENSSGQSFFVR
HHCCCCCCCCCEEEC		53.0529507054
729PhosphorylationQENSSGQSFFVRNKK
CCCCCCCCEEECCCC		24.9530108239
752PhosphorylationGPHSLGCYNPMMEDG
CCCCCCCCCCCCCCC		22.0927642862
762PhosphorylationMMEDGISYTTLRFPE
CCCCCCCEEECCCCC		11.2119919568
762DephosphorylationMMEDGISYTTLRFPE
CCCCCCCEEECCCCC		11.219890995
795PhosphorylationPDCDDTVTYSALHKR
CCCCCCCCHHHHHHC		17.5321552520
796PhosphorylationDCDDTVTYSALHKRQ
CCCCCCCHHHHHHCC		6.3927155012
801UbiquitinationVTYSALHKRQVGDYE
CCHHHHHHCCCCCCC		45.43-
807PhosphorylationHKRQVGDYENVIPDF
HHCCCCCCCCCCCCC		11.9519919568
822PhosphorylationPEDEGIHYSELIQFG
CCCCCCCHHHHHHCC		11.2619919568
822DephosphorylationPEDEGIHYSELIQFG
CCCCCCCHHHHHHCC		11.269890995
842PhosphorylationQAQENVDYVILKH--
CCCCCCCEEEECC--		5.7719919568
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 CD22_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD22_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 CD22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2A1_HUMANAP2A1physical
12646615
PTN6_HUMANPTPN6physical
9890995
SHIP1_HUMANINPP5Dphysical
10748054
GRB2_HUMANGRB2physical
10748054
SHC1_HUMANSHC1physical
10748054
PTN6_HUMANPTPN6physical
11551923
GRB2_HUMANGRB2physical
11551923
PTPRC_HUMANPTPRCphysical
10228003
PTN6_HUMANPTPN6physical
10228003
LYN_HUMANLYNphysical
10228003
PTN6_HUMANPTPN6physical
8627166
KSYK_HUMANSYKphysical
8627166
PLCG1_HUMANPLCG1physical
8627166
CBPA4_HUMANCPA4physical
28514442
S10A7_HUMANS100A7physical
28514442
Drug and Disease Associations
Kegg Disease
H00001 Acute lymphoblastic leukemia (ALL) (precursor B lymphoblastic leukemia)
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D03066 Bectumomab (USAN/INN)
D04036 Epratuzumab (USAN/INN); Lymphocide (TN)
D06348 Yttrium Y 90 epratuzumab (USAN); LymphoCide (TN)
D06349 Yttrium Y 90 epratuzumab tetraxetan (USAN)
D08933 Inotuzumab ozogamicin (USAN/INN)
D09932 Moxetumomab pasudotox (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CD22_HUMAN

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Related Literatures of Post-Translational Modification

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