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P35329

- CD22_MOUSE

UniProt

P35329 - CD22_MOUSE

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Protein

B-cell receptor CD22

Gene

Cd22

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Sialic acidBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. coreceptor activity Source: MGI

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell surface receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
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 namesi
Name:Cd22
Synonyms:Lyb-8, Siglec2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:88322. Cd22.

Subcellular locationi

GO - Cellular componenti

  1. external side of plasma membrane Source: MGI
  2. integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi822 – 8221Y → F: Abolishes binding to GRB2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 862841B-cell receptor CD22PRO_0000014874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 171PROSITE-ProRule annotation
Disulfide bondi46 ↔ 106PROSITE-ProRule annotation
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi165 ↔ 229PROSITE-ProRule annotation
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi272 ↔ 324PROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi368 ↔ 411PROSITE-ProRule annotation
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi457 ↔ 499PROSITE-ProRule annotation
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi544 ↔ 586PROSITE-ProRule annotation
Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi631 ↔ 674PROSITE-ProRule annotation
Modified residuei777 – 7771Phosphotyrosine1 Publication
Modified residuei822 – 8221Phosphotyrosine1 Publication
Modified residuei837 – 8371Phosphotyrosine1 Publication
Modified residuei857 – 8571Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues by LYN.Curated
Phosphorylation of Tyr-777 and Tyr-837 are involved in binding to SYK. Phosphorylation of Tyr-822 is involved in binding to GRB2. Phosphorylation of Tyr-857 is involved in binding to SYK, PLCG2 and PIK3R1/PIK3R2.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP35329.
PaxDbiP35329.
PRIDEiP35329.

PTM databases

PhosphoSiteiP35329.

Expressioni

Tissue specificityi

B-lymphocytes.

Gene expression databases

CleanExiMM_CD22.
GenevestigatoriP35329.

Interactioni

Subunit structurei

Interacts with LYN, SYK, PIK3R1/PIK3R2, PLCG1, SHC1, INPP5D and GRB2 upon phosphorylation. May form a complex with INPP5D/SHIP, GRB2 and SHC1. Interacts with PTPN6/SHP-1 upon phosphorylation (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Grb2Q606314EBI-300059,EBI-1688
Ptpn6P293515EBI-300059,EBI-2620699

Protein-protein interaction databases

IntActiP35329. 8 interactions.
MINTiMINT-1659949.

Structurei

3D structure databases

ProteinModelPortaliP35329.
SMRiP35329. Positions 38-692.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 702681ExtracellularSequence AnalysisAdd
BLAST
Topological domaini722 – 862141CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei703 – 72119HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 142121Ig-like V-typeAdd
BLAST
Domaini147 – 24498Ig-like C2-type 1Add
BLAST
Domaini251 – 34191Ig-like C2-type 2Add
BLAST
Domaini346 – 42984Ig-like C2-type 3Add
BLAST
Domaini434 – 51582Ig-like C2-type 4Add
BLAST
Domaini520 – 59778Ig-like C2-type 5Add
BLAST
Domaini608 – 69184Ig-like C2-type 6Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi775 – 7806ITIM motif 1
Motifi835 – 8406ITIM motif 2
Motifi855 – 8606ITIM motif 3

Domaini

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG287433.
HOVERGENiHBG005272.
InParanoidiP35329.
KOiK06467.
PhylomeDBiP35329.

Family and domain databases

Gene3Di2.60.40.10. 6 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamiPF08205. C2-set_2. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35329-1) [UniParc]FASTAAdd to Basket

Also known as: CD22-beta

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.

« Hide

        10         20         30         40         50
MRVHYLWLLL ILGHAASAQY SSANDWTVDH PQTLFAWEGA CIRIPCKYKT
60 70 80 90 100
PLPKARLDNI LLFQNYEFDK ATKKFKGTVL YNKAEPELYP PKQRRVTFLG
110 120 130 140 150
NSIDNCTLKI HPIRANDSGN LGLRMTAGTE RWMEPIHLNV SEKPFQPYIQ
160 170 180 190 200
MPSEIRESQS VTLTCGLNFS CFEYDILLQW FLEDSKITSV TPSVTSITSS
210 220 230 240 250
VTSSIKNVYT ESKLTFQPKW TDHGKSVKCQ VQHSSEVLSE RTVRLDVKYT
260 270 280 290 300
PKLEIKVNPT EVEKNNSVTM TCRVNSSNPK LRTVAVSWFK DGRPLEDQEL
310 320 330 340 350
EQEQQMSKLI LHSVTKDMRG KYRCQASNDI GPGESEEVEL TVHYAPEPSR
360 370 380 390 400
VHIYPSPAEE GQSVELICES LASPSATNYT WYHNRKPIPG DTQEKLRIPK
410 420 430 440 450
VSPWHAGNYS CLAENRLGHG KIDQEAKLDV HYAPKAVTTV IQSFTPILEG
460 470 480 490 500
DSVTLVCRYN SSNPDVTSYR WNPQGSGSVL KPGVLRIQKV TWDSMPVSCA
510 520 530 540 550
ACNHKCSWAL PVILNVHYAP RDVKVLKVSP ASEIRAGQRV LLQCDFAESN
560 570 580 590 600
PAEVRFFWKK NGSLVQEGRY LSFGSVSPED SGNYNCMVNN SIGETLSQAW
610 620 630 640 650
NLQVLYAPRR LRVSISPGDH VMEGKKATLS CESDANPPIS QYTWFDSSGQ
660 670 680 690 700
DLHSSGQKLR LEPLEVQHTG SYRCKGTNGI GTGESPPSTL TVYYSPETIG
710 720 730 740 750
KRVALGLGFC LTICILAIWG MKIQKKWKQN RSQQGLQENS SGQSFFVRNK
760 770 780 790 800
KARRTPLSEG PQSQGCYNPA MDDTVSYAIL RFPESDMHNA GDAGTPATQA
810 820 830 840 850
PPPNNSDSVT YSVIQKRPMG DYENVNPSCP EDESIHYSEL VQFGAGKRPQ
860
AKEDVDYVTL KH
Length:862
Mass (Da):96,582
Last modified:February 1, 1994 - v1
Checksum:iA7662D6E87038E83
GO
Isoform 2 (identifier: P35329-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-115: Missing.

Show »
Length:800
Mass (Da):89,333
Checksum:i394094553D0F14E6
GO
Isoform 3 (identifier: P35329-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     100-133: Missing.

Show »
Length:828
Mass (Da):92,857
Checksum:i6C84F4BE3F0B6045
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871E → G in CAB85611. (PubMed:10975807)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151A → V in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural varianti19 – 191Q → R in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural varianti76 – 761K → T in strain: BALB/c, C57BL/6 and MRL.
Natural varianti83 – 864KAEP → ATKTEKDPES in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural varianti90 – 912PP → LS in strain: BALB/c.
Natural varianti94 – 941R → G in strain: BALB/c.
Natural varianti102 – 1021S → R in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural varianti112 – 1143PIR → LIH in strain: BXSB.
Natural varianti173 – 1731E → G in strain: BALB/c, C57BL/6 and MRL.
Natural varianti179 – 1791Q → K in strain: BALB/c, C57BL/6 and MRL.
Natural varianti186 – 1861K → E in strain: BALB/c, C57BL/6 and MRL.
Natural varianti190 – 1901V → I in strain: BALB/c, C57BL/6 and MRL.
Natural varianti192 – 1921P → S in strain: BALB/c, C57BL/6 and MRL.
Natural varianti236 – 2361E → K in strain: BALB/c, C57BL/6 and MRL.
Natural varianti241 – 2411R → C in strain: BALB/c.
Natural varianti244 – 2441R → H in strain: BALB/c and MRL.
Natural varianti273 – 2731R → Q in strain: BXSB.
Natural varianti380 – 3801T → I in strain: BXSB.
Natural varianti387 – 3871P → H in strain: BXSB.
Natural varianti403 – 4031P → L in strain: BXSB.
Natural varianti419 – 4191H → R in strain: BXSB.
Natural varianti423 – 4231D → G in strain: BXSB.
Natural varianti482 – 4821P → S in strain: BXSB.
Natural varianti548 – 5481E → K in strain: BXSB.
Natural varianti616 – 6161S → I in strain: BALB/c.
Natural varianti620 – 6201H → R in strain: BXSB.
Natural varianti714 – 7141C → F in strain: BALB/c.
Natural varianti787 – 7871M → T in strain: BALB/c, C57BL/6, BXSB and MRL.
Natural varianti790 – 7901A → T in strain: C57BL/6.
Natural varianti808 – 8081S → T in strain: BALB/c, BXSB and MRL.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 11562Missing in isoform 2. 1 PublicationVSP_002532Add
BLAST
Alternative sequencei100 – 13334Missing in isoform 3. 1 PublicationVSP_002533Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16928 mRNA. Translation: AAA02562.1.
AF115401 mRNA. Translation: AAD30392.1.
AF115400 mRNA. Translation: AAD30391.1.
AF102134 mRNA. Translation: AAF02417.1.
AJ250676 mRNA. Translation: CAB85609.1.
AJ250677 mRNA. Translation: CAB85610.1.
AJ250678 mRNA. Translation: CAB85611.1.
AJ250679 mRNA. Translation: CAB85612.1.
AJ250680 mRNA. Translation: CAB85613.1.
AJ250682 mRNA. Translation: CAB85615.1.
AJ250683 mRNA. Translation: CAB85616.1.
PIRiA46512.
I49583.
RefSeqiNP_001036782.1. NM_001043317.2.
NP_033975.3. NM_009845.3.
XP_006539556.1. XM_006539493.1.
XP_006539557.1. XM_006539494.1.
UniGeneiMm.260994.

Genome annotation databases

GeneIDi12483.
KEGGimmu:12483.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - Glycan Binding

Siglec-2

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L16928 mRNA. Translation: AAA02562.1 .
AF115401 mRNA. Translation: AAD30392.1 .
AF115400 mRNA. Translation: AAD30391.1 .
AF102134 mRNA. Translation: AAF02417.1 .
AJ250676 mRNA. Translation: CAB85609.1 .
AJ250677 mRNA. Translation: CAB85610.1 .
AJ250678 mRNA. Translation: CAB85611.1 .
AJ250679 mRNA. Translation: CAB85612.1 .
AJ250680 mRNA. Translation: CAB85613.1 .
AJ250682 mRNA. Translation: CAB85615.1 .
AJ250683 mRNA. Translation: CAB85616.1 .
PIRi A46512.
I49583.
RefSeqi NP_001036782.1. NM_001043317.2.
NP_033975.3. NM_009845.3.
XP_006539556.1. XM_006539493.1.
XP_006539557.1. XM_006539494.1.
UniGenei Mm.260994.

3D structure databases

ProteinModelPortali P35329.
SMRi P35329. Positions 38-692.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P35329. 8 interactions.
MINTi MINT-1659949.

Chemistry

BindingDBi P35329.
ChEMBLi CHEMBL1075279.

PTM databases

PhosphoSitei P35329.

Proteomic databases

MaxQBi P35329.
PaxDbi P35329.
PRIDEi P35329.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 12483.
KEGGi mmu:12483.

Organism-specific databases

CTDi 933.
MGIi MGI:88322. Cd22.

Phylogenomic databases

eggNOGi NOG287433.
HOVERGENi HBG005272.
InParanoidi P35329.
KOi K06467.
PhylomeDBi P35329.

Miscellaneous databases

NextBioi 281386.
PROi P35329.
SOURCEi Search...

Gene expression databases

CleanExi MM_CD22.
Genevestigatori P35329.

Family and domain databases

Gene3Di 2.60.40.10. 6 hits.
InterProi IPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view ]
Pfami PF08205. C2-set_2. 1 hit.
[Graphical view ]
SMARTi SM00409. IG. 2 hits.
SM00408. IGc2. 4 hits.
[Graphical view ]
PROSITEi PS50835. IG_LIKE. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Organization of the murine Cd22 locus. Mapping to chromosome 7 and characterization of two alleles."
    Law C.-L., Torres R.M., Sundberg H.A., Parkhouse R.M., Brannan C.I., Copeland N.G., Jenkins N.A., Clark E.A.
    J. Immunol. 151:175-187(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c and DBA/2J.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BXSB, C57BL/6 and MRL.
  3. "Dysregulated expression of the Cd22 gene as a result of a short interspersed nucleotide element insertion in Cd22alpha lupus-prone mice."
    Mary C., Laporte C., Parzy D., Santiago M.L., Stefani F., Lajaunias F., Parkhouse M.E., O'Keefe T.L., Neuberger M.S., Izui S., Reininger L.
    J. Immunol. 165:2987-2996(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-178 (ISOFORMS 1; 2 AND 3).
    Strain: NZW.
    Tissue: Spleen.
  4. "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily."
    Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E., Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.
    Curr. Biol. 4:965-972(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIALIC ACID-BINDING.
  5. "Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes."
    Chan V.W., Lowell C.A., DeFranco A.L.
    Curr. Biol. 8:545-553(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY LYN.
  6. "Analysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22."
    Yohannan J., Wienands J., Coggeshall K.M., Justement L.B.
    J. Biol. Chem. 274:18769-18776(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB2; SYK; PIK3R1/PIK3R2 AND PLCG1, PHOSPHORYLATION AT TYR-777; TYR-822; TYR-837 AND TYR-857, MUTAGENESIS OF TYR-822.
  7. "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for regulation of B lymphocyte antigen receptor-induced calcium flux."
    Poe J.C., Fujimoto M., Jansen P.J., Miller A.S., Tedder T.F.
    J. Biol. Chem. 275:17420-17427(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB2; SHC1 AND INPP5D, PHOSPHORYLATION BY LYN.

Entry informationi

Entry nameiCD22_MOUSE
AccessioniPrimary (citable) accession number: P35329
Secondary accession number(s): Q9JHL2
, Q9JJX9, Q9JJY0, Q9JJY1, Q9R056, Q9R094, Q9WU51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3