CD99_HUMAN
ID CD99_HUMAN Reviewed; 185 AA.
AC P14209; A6NIW1; O00518; Q6ICV7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=CD99 antigen;
DE AltName: Full=12E7;
DE AltName: Full=E2 antigen;
DE AltName: Full=Protein MIC2;
DE AltName: Full=T-cell surface glycoprotein E2;
DE AltName: CD_antigen=CD99;
DE Flags: Precursor;
GN Name=CD99; Synonyms=MIC2, MIC2X, MIC2Y;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I), AND PROTEIN SEQUENCE OF 23-39.
RC TISSUE=T-cell;
RX PubMed=2479542; DOI=10.1002/j.1460-2075.1989.tb08485.x;
RA Gelin C., Aubrit F., Phalipon A., Raynal B., Cole S., Kaczorek M.,
RA Bernard A.;
RT "The E2 antigen, a 32 kd glycoprotein involved in T-cell adhesion
RT processes, is the MIC2 gene product.";
RL EMBO J. 8:3253-3259(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
RA Park S.H., Hahn J.H., Kim M.K., Sohn H.W., Choi E.Y., Kim S.H.;
RT "An alternative splicing form of CD99 (MIC2).";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS I AND 3).
RC TISSUE=Brain, Kidney, Lung carcinoma, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-105.
RX PubMed=3472717; DOI=10.1101/sqb.1986.051.01.025;
RA Darling S.M., Goodfellow P.J., Pym B., Banting G.S., Pritchard C.,
RA Goodfellow P.N.;
RT "Molecular genetics of MIC2: a gene shared by the human X and Y
RT chromosomes.";
RL Cold Spring Harb. Symp. Quant. Biol. 51:205-212(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=2456574; DOI=10.1073/pnas.85.15.5605;
RA Goodfellow P.J., Mondello C., Darling S.M., Pym B., Little P.,
RA Goodfellow P.N.;
RT "Absence of methylation of a CpG-rich region at the 5' end of the MIC2 gene
RT on the active X, the inactive X, and the Y chromosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5605-5609(1988).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND THR-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in T-cell adhesion processes and in spontaneous
CC rosette formation with erythrocytes. Plays a role in a late step of
CC leukocyte extravasation helping leukocytes to overcome the endothelial
CC basement membrane. Acts at the same site as, but independently of,
CC PECAM1. Involved in T-cell adhesion processes (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=I;
CC IsoId=P14209-1; Sequence=Displayed;
CC Name=II;
CC IsoId=P14209-2; Sequence=VSP_004324;
CC Name=3;
CC IsoId=P14209-3; Sequence=VSP_046315;
CC -!- PTM: Extensively O-glycosylated.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SIMILARITY: Belongs to the CD99 family. {ECO:0000305}.
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DR EMBL; X16996; CAA34863.1; -; mRNA.
DR EMBL; U82164; AAB58501.1; -; mRNA.
DR EMBL; CR450286; CAG29282.1; -; mRNA.
DR EMBL; AC006209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98697.1; -; Genomic_DNA.
DR EMBL; CH471074; EAW98698.1; -; Genomic_DNA.
DR EMBL; BC002584; AAH02584.1; -; mRNA.
DR EMBL; BC003147; AAH03147.1; -; mRNA.
DR EMBL; BC010109; AAH10109.1; -; mRNA.
DR EMBL; BC021620; AAH21620.1; -; mRNA.
DR EMBL; BC024310; AAH24310.1; -; mRNA.
DR EMBL; BQ948496; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M16279; AAA02999.1; -; mRNA.
DR EMBL; J03841; AAA59848.1; -; Genomic_DNA.
DR CCDS; CCDS14119.1; -. [P14209-1]
DR CCDS; CCDS48071.1; -. [P14209-3]
DR CCDS; CCDS75947.1; -. [P14209-2]
DR PIR; S06786; A60592.
DR RefSeq; NP_001116370.1; NM_001122898.2. [P14209-3]
DR RefSeq; NP_001308296.1; NM_001321367.1. [P14209-2]
DR RefSeq; NP_001308297.1; NM_001321368.1.
DR RefSeq; NP_001308298.1; NM_001321369.1.
DR RefSeq; NP_002405.1; NM_002414.4. [P14209-1]
DR PDB; 7SFX; X-ray; 3.10 A; E/F=63-76.
DR PDBsum; 7SFX; -.
DR AlphaFoldDB; P14209; -.
DR SMR; P14209; -.
DR BioGRID; 110420; 70.
DR IntAct; P14209; 14.
DR MINT; P14209; -.
DR STRING; 9606.ENSP00000370588; -.
DR GlyConnect; 2923; 1 O-Linked glycan (1 site).
DR GlyGen; P14209; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; P14209; -.
DR PhosphoSitePlus; P14209; -.
DR SwissPalm; P14209; -.
DR BioMuta; CD99; -.
DR DMDM; 119049; -.
DR EPD; P14209; -.
DR jPOST; P14209; -.
DR MassIVE; P14209; -.
DR MaxQB; P14209; -.
DR PaxDb; P14209; -.
DR PeptideAtlas; P14209; -.
DR PRIDE; P14209; -.
DR ProteomicsDB; 1291; -.
DR ProteomicsDB; 53032; -. [P14209-1]
DR ProteomicsDB; 53033; -. [P14209-2]
DR ABCD; P14209; 1 sequenced antibody.
DR Antibodypedia; 3499; 1778 antibodies from 48 providers.
DR DNASU; 4267; -.
DR Ensembl; ENST00000381187.8; ENSP00000370582.3; ENSG00000002586.20. [P14209-3]
DR Ensembl; ENST00000381192.10; ENSP00000370588.3; ENSG00000002586.20. [P14209-1]
DR Ensembl; ENST00000482405.7; ENSP00000494027.1; ENSG00000002586.20. [P14209-2]
DR Ensembl; ENST00000611428.5; ENSP00000479999.1; ENSG00000002586.20. [P14209-2]
DR Ensembl; ENST00000623253.4; ENSP00000485545.1; ENSG00000002586.20. [P14209-2]
DR GeneID; 4267; -.
DR KEGG; hsa:4267; -.
DR MANE-Select; ENST00000381192.10; ENSP00000370588.3; NM_002414.5; NP_002405.1.
DR UCSC; uc004cqm.4; human. [P14209-1]
DR CTD; 4267; -.
DR DisGeNET; 4267; -.
DR GeneCards; CD99; -.
DR HGNC; HGNC:7082; CD99.
DR HPA; ENSG00000002586; Low tissue specificity.
DR MIM; 313470; gene.
DR MIM; 450000; gene.
DR neXtProt; NX_P14209; -.
DR OpenTargets; ENSG00000002586; -.
DR PharmGKB; PA30804; -.
DR VEuPathDB; HostDB:ENSG00000002586; -.
DR eggNOG; ENOG502S70S; Eukaryota.
DR GeneTree; ENSGT00940000154344; -.
DR HOGENOM; CLU_092825_1_1_1; -.
DR InParanoid; P14209; -.
DR OMA; EEGEVNM; -.
DR OrthoDB; 1435553at2759; -.
DR PhylomeDB; P14209; -.
DR TreeFam; TF336273; -.
DR PathwayCommons; P14209; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P14209; -.
DR BioGRID-ORCS; 4267; 6 hits in 579 CRISPR screens.
DR ChiTaRS; CD99; human.
DR GeneWiki; CD99; -.
DR GenomeRNAi; 4267; -.
DR Pharos; P14209; Tbio.
DR PRO; PR:P14209; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P14209; protein.
DR Bgee; ENSG00000002586; Expressed in type B pancreatic cell and 209 other tissues.
DR ExpressionAtlas; P14209; baseline and differential.
DR Genevisible; P14209; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IBA:GO_Central.
DR GO; GO:2000391; P:positive regulation of neutrophil extravasation; IBA:GO_Central.
DR GO; GO:0072683; P:T cell extravasation; IBA:GO_Central.
DR InterPro; IPR022078; CD99L2.
DR PANTHER; PTHR15076; PTHR15076; 1.
DR Pfam; PF12301; CD99L2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:2479542"
FT CHAIN 23..185
FT /note="CD99 antigen"
FT /id="PRO_0000021726"
FT TOPO_DOM 23..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 27..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 34..49
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046315"
FT VAR_SEQ 159..185
FT /note="AEQGEVDMESHRNANAEPAVQRTLLEK -> DG (in isoform II)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_004324"
FT VARIANT 166
FT /note="M -> V (in dbSNP:rs4793)"
FT /id="VAR_014733"
FT VARIANT 173
FT /note="N -> I (in dbSNP:rs4717)"
FT /id="VAR_014734"
SQ SEQUENCE 185 AA; 18848 MW; C302E09E6B022EAB CRC64;
MARGAALALL LFGLLGVLVA APDGGFDLSD ALPDNENKKP TAIPKKPSAG DDFDLGDAVV
DGENDDPRPP NPPKPMPNPN PNHPSSSGSF SDADLADGVS GGEGKGGSDG GGSHRKEGEE
ADAPGVIPGI VGAVVVAVAG AISSFIAYQK KKLCFKENAE QGEVDMESHR NANAEPAVQR
TLLEK
