P20273 (CD22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
B-cell receptor CD22

Alternative name(s):
B-lymphocyte cell adhesion molecule
Short name=BL-CAM
Sialic acid-binding Ig-like lectin 2
Short name=Siglec-2
T-cell surface antigen Leu-14
CD_antigen=CD22

Gene names

Name:	CD22
Synonyms:	SIGLEC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Predominantly monomer of isoform CD22-beta. Also found as heterodimer of isoform CD22-beta and a shorter isoform. Interacts with PTPN6/SHP-1, LYN, SYK, PIK3R1/PIK3R2 and PLCG1 upon phosphorylation. Interacts with GRB2, INPP5D and SHC1 upon phosphorylation By similarity. May form a complex with INPP5D/SHIP, GRB2 and SHC1. Ref.8 Ref.9 Ref.10
Subcellular location	Cell membrane; Single-pass type I membrane protein.
Tissue specificity	B-lymphocytes.
Domain	Contains 4 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.
Post-translational modification	Phosphorylation of Tyr-762, Tyr-807 and Tyr-822 are involved in binding to SYK, GRB2 and SYK, respectively. Phosphorylation of Tyr-842 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2. Phosphorylated on tyrosine residues by LYN By similarity.
Sequence similarities	Belongs to the immunoglobulin superfamily. SIGLEC (sialic acid binding Ig-like lectin) family. Contains 6 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 Ig-like V-type (immunoglobulin-like) domain.
Sequence caution	The sequence CAA36988.1 differs from that shown. Reason: Frameshift at position 806.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Lectin
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Non-traceable author statement PubMed 7925291. Source: ProtInc
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LYN	P07948	2	EBI-78277,EBI-79452
PLCG1	P19174	2	EBI-78277,EBI-79387
PTPN6	P29350	4	EBI-78277,EBI-78260
SYK	P43405	4	EBI-78277,EBI-78302

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform CD22-beta (identifier: P20273-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform CD22-alpha (identifier: P20273-2)

The sequence of this isoform differs from the canonical sequence as follows:
     241-417: Missing.

Isoform 3 (identifier: P20273-3)

The sequence of this isoform differs from the canonical sequence as follows:
     330-417: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 847	828	B-cell receptor CD22		PRO_0000014873
Regions
	Topological domain	20 – 687	668	Extracellular Potential
	Transmembrane	688 – 706	19	Helical; Potential
	Topological domain	707 – 847	141	Cytoplasmic Potential
	Domain	20 – 138	119	Ig-like V-type
	Domain	143 – 235	93	Ig-like C2-type 1
	Domain	242 – 326	85	Ig-like C2-type 2
	Domain	331 – 416	86	Ig-like C2-type 3
	Domain	419 – 500	82	Ig-like C2-type 4
	Domain	505 – 582	78	Ig-like C2-type 5
	Domain	593 – 676	84	Ig-like C2-type 6
	Motif	760 – 765	6	ITIM motif 1
	Motif	794 – 799	6	ITIM motif 2
	Motif	820 – 825	6	ITIM motif 3
	Motif	840 – 845	6	ITIM motif 4
Sites
	Binding site	120	1	Sialic acid By similarity
Amino acid modifications
	Glycosylation	67	1	N-linked (GlcNAc...) Potential
	Glycosylation	101	1	N-linked (GlcNAc...) Potential
	Glycosylation	112	1	N-linked (GlcNAc...) Potential
	Glycosylation	135	1	N-linked (GlcNAc...) Potential
	Glycosylation	164	1	N-linked (GlcNAc...) Potential
	Glycosylation	231	1	N-linked (GlcNAc...) Potential
	Glycosylation	363	1	N-linked (GlcNAc...) Potential
	Glycosylation	445	1	N-linked (GlcNAc...) Potential
	Glycosylation	448	1	N-linked (GlcNAc...) Potential
	Glycosylation	479	1	N-linked (GlcNAc...) Potential
	Glycosylation	574	1	N-linked (GlcNAc...) Potential
	Glycosylation	634	1	N-linked (GlcNAc...) Potential
	Disulfide bond	39 ↔ 167		By similarity
	Disulfide bond	44 ↔ 102		By similarity
	Disulfide bond	161 ↔ 219		By similarity
	Disulfide bond	265 ↔ 309		By similarity
	Disulfide bond	353 ↔ 396		By similarity
	Disulfide bond	442 ↔ 484		By similarity
	Disulfide bond	529 ↔ 571		By similarity
	Disulfide bond	616 ↔ 659		By similarity
Natural variations
	Alternative sequence	241 – 417	177	Missing in isoform CD22-alpha.		VSP_002531
	Alternative sequence	330 – 417	88	Missing in isoform 3.		VSP_045363
	Natural variant	34	1	A → T. Ref.6		VAR_014133
	Natural variant	152	1	Q → E Observed with a marginally higher frequency in patients with systemic lupus erythematosus. Ref.6		VAR_003913
	Natural variant	203	1	E → K. Ref.6		VAR_014134
	Natural variant	551	1	G → R. Corresponds to variant rs35715143 [ dbSNP | Ensembl ].		VAR_049903
	Natural variant	639	1	Y → H. Ref.2 Corresponds to variant rs1058407 [ dbSNP | Ensembl ].		VAR_014135
	Natural variant	664	1	S → G. Ref.6 Corresponds to variant rs17719289 [ dbSNP | Ensembl ].		VAR_003914
	Natural variant	669	1	R → C. Ref.6		VAR_003915
	Natural variant	745	1	G → D. Ref.6 Corresponds to variant rs10406069 [ dbSNP | Ensembl ].		VAR_003916
Experimental info
	Sequence conflict	486	1	A → R in CAA42006. Ref.1
	Sequence conflict	788 – 789	2	PD → RT in CAA42006. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform CD22-beta [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 38EB0BE4220ACA2D	FASTA	847	95,348
	10 20 30 40 50 60 MHLLGPWLLL LVLEYLAFSD SSKWVFEHPE TLYAWEGACV WIPCTYRALD GDLESFILFH 70 80 90 100 110 120 NPEYNKNTSK FDGTRLYEST KDGKVPSEQK RVQFLGDKNK NCTLSIHPVH LNDSGQLGLR 130 140 150 160 170 180 MESKTEKWME RIHLNVSERP FPPHIQLPPE IQESQEVTLT CLLNFSCYGY PIQLQWLLEG 190 200 210 220 230 240 VPMRQAAVTS TSLTIKSVFT RSELKFSPQW SHHGKIVTCQ LQDADGKFLS NDTVQLNVKH 250 260 270 280 290 300 TPKLEIKVTP SDAIVREGDS VTMTCEVSSS NPEYTTVSWL KDGTSLKKQN TFTLNLREVT 310 320 330 340 350 360 KDQSGKYCCQ VSNDVGPGRS EEVFLQVQYA PEPSTVQILH SPAVEGSQVE FLCMSLANPL 370 380 390 400 410 420 PTNYTWYHNG KEMQGRTEEK VHIPKILPWH AGTYSCVAEN ILGTGQRGPG AELDVQYPPK 430 440 450 460 470 480 KVTTVIQNPM PIREGDTVTL SCNYNSSNPS VTRYEWKPHG AWEEPSLGVL KIQNVGWDNT 490 500 510 520 530 540 TIACAACNSW CSWASPVALN VQYAPRDVRV RKIKPLSEIH SGNSVSLQCD FSSSHPKEVQ 550 560 570 580 590 600 FFWEKNGRLL GKESQLNFDS ISPEDAGSYS CWVNNSIGQT ASKAWTLEVL YAPRRLRVSM 610 620 630 640 650 660 SPGDQVMEGK SATLTCESDA NPPVSHYTWF DWNNQSLPYH SQKLRLEPVK VQHSGAYWCQ 670 680 690 700 710 720 GTNSVGKGRS PLSTLTVYYS PETIGRRVAV GLGSCLAILI LAICGLKLQR RWKRTQSQQG 730 740 750 760 770 780 LQENSSGQSF FVRNKKVRRA PLSEGPHSLG CYNPMMEDGI SYTTLRFPEM NIPRTGDAES 790 800 810 820 830 840 SEMQRPPPDC DDTVTYSALH KRQVGDYENV IPDFPEDEGI HYSELIQFGV GERPQAQENV DYVILKH
	Isoform CD22-alpha [UniParc]. Checksum: 04F241A74FF61471	FASTA	670	75,799
	10 20 30 40 50 60 MHLLGPWLLL LVLEYLAFSD SSKWVFEHPE TLYAWEGACV WIPCTYRALD GDLESFILFH 70 80 90 100 110 120 NPEYNKNTSK FDGTRLYEST KDGKVPSEQK RVQFLGDKNK NCTLSIHPVH LNDSGQLGLR 130 140 150 160 170 180 MESKTEKWME RIHLNVSERP FPPHIQLPPE IQESQEVTLT CLLNFSCYGY PIQLQWLLEG 190 200 210 220 230 240 VPMRQAAVTS TSLTIKSVFT RSELKFSPQW SHHGKIVTCQ LQDADGKFLS NDTVQLNVKH 250 260 270 280 290 300 PPKKVTTVIQ NPMPIREGDT VTLSCNYNSS NPSVTRYEWK PHGAWEEPSL GVLKIQNVGW 310 320 330 340 350 360 DNTTIACAAC NSWCSWASPV ALNVQYAPRD VRVRKIKPLS EIHSGNSVSL QCDFSSSHPK 370 380 390 400 410 420 EVQFFWEKNG RLLGKESQLN FDSISPEDAG SYSCWVNNSI GQTASKAWTL EVLYAPRRLR 430 440 450 460 470 480 VSMSPGDQVM EGKSATLTCE SDANPPVSHY TWFDWNNQSL PYHSQKLRLE PVKVQHSGAY 490 500 510 520 530 540 WCQGTNSVGK GRSPLSTLTV YYSPETIGRR VAVGLGSCLA ILILAICGLK LQRRWKRTQS 550 560 570 580 590 600 QQGLQENSSG QSFFVRNKKV RRAPLSEGPH SLGCYNPMME DGISYTTLRF PEMNIPRTGD 610 620 630 640 650 660 AESSEMQRPP PDCDDTVTYS ALHKRQVGDY ENVIPDFPED EGIHYSELIQ FGVGERPQAQ 670 ENVDYVILKH
	Isoform 3 [UniParc]. Checksum: 18C7BFA0D4C94AE5	FASTA	759	85,675
	10 20 30 40 50 60 MHLLGPWLLL LVLEYLAFSD SSKWVFEHPE TLYAWEGACV WIPCTYRALD GDLESFILFH 70 80 90 100 110 120 NPEYNKNTSK FDGTRLYEST KDGKVPSEQK RVQFLGDKNK NCTLSIHPVH LNDSGQLGLR 130 140 150 160 170 180 MESKTEKWME RIHLNVSERP FPPHIQLPPE IQESQEVTLT CLLNFSCYGY PIQLQWLLEG 190 200 210 220 230 240 VPMRQAAVTS TSLTIKSVFT RSELKFSPQW SHHGKIVTCQ LQDADGKFLS NDTVQLNVKH 250 260 270 280 290 300 TPKLEIKVTP SDAIVREGDS VTMTCEVSSS NPEYTTVSWL KDGTSLKKQN TFTLNLREVT 310 320 330 340 350 360 KDQSGKYCCQ VSNDVGPGRS EEVFLQVQYP PKKVTTVIQN PMPIREGDTV TLSCNYNSSN 370 380 390 400 410 420 PSVTRYEWKP HGAWEEPSLG VLKIQNVGWD NTTIACAACN SWCSWASPVA LNVQYAPRDV 430 440 450 460 470 480 RVRKIKPLSE IHSGNSVSLQ CDFSSSHPKE VQFFWEKNGR LLGKESQLNF DSISPEDAGS 490 500 510 520 530 540 YSCWVNNSIG QTASKAWTLE VLYAPRRLRV SMSPGDQVME GKSATLTCES DANPPVSHYT 550 560 570 580 590 600 WFDWNNQSLP YHSQKLRLEP VKVQHSGAYW CQGTNSVGKG RSPLSTLTVY YSPETIGRRV 610 620 630 640 650 660 AVGLGSCLAI LILAICGLKL QRRWKRTQSQ QGLQENSSGQ SFFVRNKKVR RAPLSEGPHS 670 680 690 700 710 720 LGCYNPMMED GISYTTLRFP EMNIPRTGDA ESSEMQRPPP DCDDTVTYSA LHKRQVGDYE 730 740 750 NVIPDFPEDE GIHYSELIQF GVGERPQAQE NVDYVILKH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion." Stamenkovic I., Seed B. Nature 345:74-77(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD22-BETA).
[2]	"cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions." Wilson G.L., Fox C.H., Fauci A.S., Kehrl J.H. J. Exp. Med. 173:137-146(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CD22-BETA), VARIANT HIS-639. Tissue: Tonsil.
[3]	"Genomic structure and chromosomal mapping of the human CD22 gene." Wilson G.L., Najfeld V., Kozlow E., Menniger J., Ward D., Kehrl J.H. J. Immunol. 150:5013-5024(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CD22-ALPHA AND CD22-BETA).
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Spleen.
[5]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Identification of the gene variations in human CD22." Hatta Y., Tsuchiya N., Matsushita M., Shiota M., Hagiwara K., Tokunaga K. Immunogenetics 49:280-286(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 13-137; 139-239; 241-328 AND 418-502, VARIANTS THR-34; GLU-152; LYS-203; GLY-664; CYS-669 AND ASP-745.
[7]	"Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition." Powell L.D., Sgroi D., Sjoberg E.R., Stamenkovic I., Varki A. J. Biol. Chem. 268:7019-7027(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SIALIC ACID-BINDING.
[8]	"A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP." Doody G.M., Justement L.B., Delibrias C.C., Matthews R.J., Lin J., Thomas M.L., Fearon D.T. Science 269:242-244(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN6.
[9]	"Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22." Tuscano J.M., Engel P., Tedder T.F., Agarwal A., Kehrl J.H. Eur. J. Immunol. 26:1246-1252(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LYN; SYK AND PIK3R1/PIK3R2.
[10]	"CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation." Law C.L., Sidorenko S.P., Chandran K.A., Zhao Z., Shen S.H., Fischer E.H., Clark E.A. J. Exp. Med. 183:547-560(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN6; SYK AND PLCG1.
[11]	"CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling." Tedder T.F., Tuscano J., Sato S., Kehrl J.H. Annu. Rev. Immunol. 15:481-504(1997) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Siglec-2 [3 Fc Domains]

Functional Glycomics Gateway - Glycan Binding

Siglec-2

Cross-references

Sequence databases
EMBL GenBank DDBJ	U62631 Genomic DNA. Translation: AAB06448.1. U62631 Genomic DNA. Translation: AAB06449.1. X59350 mRNA. Translation: CAA42006.1. X52785 mRNA. Translation: CAA36988.1. Frameshift. AK225625 mRNA. No translation available. AB012995 Genomic DNA. Translation: BAA36564.1. AB012996 Genomic DNA. Translation: BAA36565.1. AB012997 Genomic DNA. Translation: BAA36566.1. AB012998 Genomic DNA. Translation: BAA36567.1. AB012999 Genomic DNA. Translation: BAA36568.1. AB013000 Genomic DNA. Translation: BAA36569.1. AB013002 Genomic DNA. Translation: BAA36571.1. AB013003 Genomic DNA. Translation: BAA36572.1. AB013004 Genomic DNA. Translation: BAA36573.1. AB013006 Genomic DNA. Translation: BAA36575.1.
IPI	IPI00218390. IPI00295133. IPI00975891.
PIR	A35648.
RefSeq	NP_001172028.1. NM_001185099.1. NP_001172029.1. NM_001185100.1. NP_001172030.1. NM_001185101.1. NP_001762.2. NM_001771.3.
UniGene	Hs.579691.
3D structure databases
ProteinModelPortal	P20273.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20273. 6 interactions.
Protein family/group databases
MEROPS	I43.001.
PTM databases
PhosphoSite	P20273.
Polymorphism databases
DMDM	6166019.
Proteomic databases
PaxDb	P20273.
PRIDE	P20273.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000085219; ENSP00000085219; ENSG00000012124. ENST00000341773; ENSP00000339349; ENSG00000012124. ENST00000536635; ENSP00000442279; ENSG00000012124. ENST00000594250; ENSP00000469984; ENSG00000012124.
GeneID	933.
KEGG	hsa:933.
UCSC	uc002nzb.4. human. uc010edt.3. human.
Organism-specific databases
CTD	933.
GeneCards	GC19P035820.
HGNC	HGNC:1643. CD22.
HPA	CAB002418. HPA024353.
MIM	107266. gene.
neXtProt	NX_P20273.
PharmGKB	PA26201.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG287433.
HOVERGEN	HBG005272.
InParanoid	P20273.
KO	K06467.
OMA	SGAYWCQ.
OrthoDB	EOG4C87RQ.
Enzyme and pathway databases
Pathway_Interaction_DB	bcr_5pathway. BCR signaling pathway.
Gene expression databases
ArrayExpress	P20273.
Bgee	P20273.
Genevestigator	P20273.
GermOnline	ENSG00000012124. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.10. 7 hits.
InterPro	IPR013162. CD80_C2-set. IPR007110. Ig-like_dom. IPR013783. Ig-like_fold. IPR003599. Ig_sub. IPR003598. Ig_sub2. IPR013151. Immunoglobulin. [Graphical view]
Pfam	PF08205. C2-set_2. 1 hit. PF00047. ig. 2 hits. [Graphical view]
SMART	SM00409. IG. 2 hits. SM00408. IGc2. 4 hits. [Graphical view]
PROSITE	PS50835. IG_LIKE. 6 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P20273.
ChEMBL	CHEMBL3218.
DrugBank	DB00045. OspA lipoprotein.
GenomeRNAi	933.
NextBio	3874.
SOURCE	Search...

Entry information

Entry name

CD22_HUMAN

Accession

Primary (citable) accession number: P20273
Secondary accession number(s): F5H7U3 , O95699, O95701, O95702, O95703, Q01665, Q92872, Q92873, Q9UQA6, Q9UQA7, Q9UQA8, Q9UQA9, Q9UQB0, Q9Y2A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 15, 1999
Last modified:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.