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Protein

T-cell surface antigen CD2

Gene

CD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

CD2 interacts with lymphocyte function-associated antigen (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.

GO - Molecular functioni

  1. receptor activity Source: UniProtKB
  2. receptor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. blood coagulation Source: Reactome
  3. cell surface receptor signaling pathway Source: UniProtKB
  4. heterotypic cell-cell adhesion Source: UniProtKB
  5. leukocyte migration Source: Reactome
  6. membrane raft polarization Source: UniProtKB
  7. natural killer cell activation Source: UniProtKB
  8. positive regulation of interferon-gamma secretion Source: UniProtKB
  9. positive regulation of interleukin-8 secretion Source: UniProtKB
  10. positive regulation of myeloid dendritic cell activation Source: UniProtKB
  11. positive regulation of tumor necrosis factor production Source: UniProtKB
  12. regulation of T cell differentiation Source: UniProtKB
  13. single organismal cell-cell adhesion Source: UniProtKB
  14. T cell activation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
SignaLinkiP06729.

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface antigen CD2
Alternative name(s):
Erythrocyte receptor
LFA-2
LFA-3 receptor
Rosette receptor
T-cell surface antigen T11/Leu-5
CD_antigen: CD2
Gene namesi
Name:CD2
Synonyms:SRBC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1639. CD2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 209185ExtracellularSequence AnalysisAdd
BLAST
Transmembranei210 – 23526HelicalSequence AnalysisAdd
BLAST
Topological domaini236 – 351116CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. anchored component of plasma membrane Source: Ensembl
  2. cell-cell junction Source: Ensembl
  3. cell surface Source: UniProtKB
  4. cytoplasmic side of plasma membrane Source: Ensembl
  5. external side of plasma membrane Source: MGI
  6. extracellular region Source: Ensembl
  7. integral component of plasma membrane Source: UniProtKB
  8. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671K → R: Loss of LFA-3 binding. 1 Publication
Mutagenesisi70 – 701Q → K: Loss of LFA-3 binding. 1 Publication
Mutagenesisi110 – 1101Y → D: Loss of LFA-3 and CD59 binding. 1 Publication
Mutagenesisi111 – 1111D → H: Loss of LFA-3 and CD59 binding. 1 Publication

Organism-specific databases

PharmGKBiPA26198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 351327T-cell surface antigen CD2PRO_0000014600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)
Disulfide bondi139 ↔ 2031 Publication
Glycosylationi141 – 1411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi146 ↔ 1861 Publication
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP06729.
PaxDbiP06729.
PRIDEiP06729.

PTM databases

PhosphoSiteiP06729.
UniCarbKBiP06729.

Expressioni

Gene expression databases

BgeeiP06729.
CleanExiHS_CD2.
ExpressionAtlasiP06729. baseline and differential.
GenevestigatoriP06729.

Organism-specific databases

HPAiCAB002430.
HPA003883.

Interactioni

Subunit structurei

Interacts with CD2AP (By similarity). Interacts with PSTPIP1.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CD2APQ9Y5K64EBI-3912464,EBI-298152
CD2BP2O954003EBI-3912464,EBI-768015
SH3KBP1Q96B973EBI-3912464,EBI-346595

Protein-protein interaction databases

BioGridi107352. 16 interactions.
IntActiP06729. 7 interactions.
MINTiMINT-99488.
STRINGi9606.ENSP00000358490.

Structurei

Secondary structure

1
351
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 366Combined sources
Beta strandi41 – 433Combined sources
Beta strandi52 – 6110Combined sources
Helixi62 – 643Combined sources
Beta strandi67 – 715Combined sources
Helixi73 – 753Combined sources
Beta strandi77 – 804Combined sources
Beta strandi84 – 863Combined sources
Turni88 – 903Combined sources
Beta strandi92 – 943Combined sources
Helixi99 – 1013Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi116 – 12712Combined sources
Beta strandi134 – 1385Combined sources
Turni139 – 1424Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi155 – 1628Combined sources
Beta strandi164 – 1707Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi180 – 18910Combined sources
Beta strandi194 – 20310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDBNMR-A25-129[»]
1GYANMR-A25-129[»]
1HNFX-ray2.50A25-206[»]
1L2ZNMR-B294-304[»]
1QA9X-ray3.20A/C28-129[»]
2J6OX-ray2.22C324-333[»]
2J7IX-ray2.90C/D324-333[»]
ProteinModelPortaliP06729.
SMRiP06729. Positions 28-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06729.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 128104Ig-like V-typeAdd
BLAST
Domaini129 – 20981Ig-like C2-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni61 – 7515LFA-3 (CD58) binding region 1Add
BLAST
Regioni106 – 12015LFA-3 (CD58) binding region 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi282 – 33857Pro-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47564.
HOGENOMiHOG000276890.
HOVERGENiHBG000262.
InParanoidiP06729.
KOiK06449.
OMAiGTQVHQQ.
OrthoDBiEOG7KSX9X.
PhylomeDBiP06729.
TreeFamiTF335971.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR015632. CD2.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERiPTHR12080. PTHR12080. 1 hit.
PTHR12080:SF10. PTHR12080:SF10. 1 hit.
PfamiPF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01870. CD2ANTIGEN.

Sequencei

Sequence statusi: Complete.

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

P06729-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFPCKFVAS FLLIFNVSSK GAVSKEITNA LETWGALGQD INLDIPSFQM
60 70 80 90 100
SDDIDDIKWE KTSDKKKIAQ FRKEKETFKE KDTYKLFKNG TLKIKHLKTD
110 120 130 140 150
DQDIYKVSIY DTKGKNVLEK IFDLKIQERV SKPKISWTCI NTTLTCEVMN
160 170 180 190 200
GTDPELNLYQ DGKHLKLSQR VITHKWTTSL SAKFKCTAGN KVSKESSVEP
210 220 230 240 250
VSCPEKGLDI YLIIGICGGG SLLMVFVALL VFYITKRKKQ RSRRNDEELE
260 270 280 290 300
TRAHRVATEE RGRKPHQIPA STPQNPATSQ HPPPPPGHRS QAPSHRPPPP
310 320 330 340 350
GHRVQHQPQK RPPAPSGTQV HQQKGPPLPR PRVQPKPPHG AAENSLSPSS

N
Length:351
Mass (Da):39,448
Last modified:October 23, 2007 - v2
Checksum:iA03D853C3B618917
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871G → A (PubMed:3490670).Curated
Sequence conflicti339 – 35113HGAAE…SPSSN → MGQQKTHCPLPLIKKDRNCL FQ in AAA51946 (PubMed:3490670).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti217 – 2171C → Y in a breast cancer sample; somatic mutation. 1 Publication
VAR_035504
Natural varianti266 – 2661H → Q.3 Publications
Corresponds to variant rs699738 [ dbSNP | Ensembl ].
VAR_017104
Natural varianti339 – 3391H → N.
Corresponds to variant rs35880225 [ dbSNP | Ensembl ].
VAR_033608

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19806
, M19798, M19800, M19802, M19804 Genomic DNA. Translation: AAA53095.1.
M16445 mRNA. Translation: AAA51738.1.
M14362 mRNA. Translation: AAA35571.1.
M16336 mRNA. Translation: AAA51946.1.
X07871
, X07872, X07873, X07874 Genomic DNA. Translation: CAA30721.1.
AL135798 Genomic DNA. Translation: CAC14840.1.
BC033583 mRNA. Translation: AAH33583.1.
CCDSiCCDS889.1.
PIRiA28967. RWHUC2.
RefSeqiNP_001758.2. NM_001767.3.
UniGeneiHs.523500.

Genome annotation databases

EnsembliENST00000369478; ENSP00000358490; ENSG00000116824.
GeneIDi914.
KEGGihsa:914.
UCSCiuc001egu.4. human.

Polymorphism databases

DMDMi160370002.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

CD2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19806
, M19798, M19800, M19802, M19804 Genomic DNA. Translation: AAA53095.1.
M16445 mRNA. Translation: AAA51738.1.
M14362 mRNA. Translation: AAA35571.1.
M16336 mRNA. Translation: AAA51946.1.
X07871
, X07872, X07873, X07874 Genomic DNA. Translation: CAA30721.1.
AL135798 Genomic DNA. Translation: CAC14840.1.
BC033583 mRNA. Translation: AAH33583.1.
CCDSiCCDS889.1.
PIRiA28967. RWHUC2.
RefSeqiNP_001758.2. NM_001767.3.
UniGeneiHs.523500.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CDBNMR-A25-129[»]
1GYANMR-A25-129[»]
1HNFX-ray2.50A25-206[»]
1L2ZNMR-B294-304[»]
1QA9X-ray3.20A/C28-129[»]
2J6OX-ray2.22C324-333[»]
2J7IX-ray2.90C/D324-333[»]
ProteinModelPortaliP06729.
SMRiP06729. Positions 28-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107352. 16 interactions.
IntActiP06729. 7 interactions.
MINTiMINT-99488.
STRINGi9606.ENSP00000358490.

Chemistry

BindingDBiP06729.
ChEMBLiCHEMBL2040.
DrugBankiDB00092. Alefacept.
GuidetoPHARMACOLOGYi2600.

PTM databases

PhosphoSiteiP06729.
UniCarbKBiP06729.

Polymorphism databases

DMDMi160370002.

Proteomic databases

MaxQBiP06729.
PaxDbiP06729.
PRIDEiP06729.

Protocols and materials databases

DNASUi914.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369478; ENSP00000358490; ENSG00000116824.
GeneIDi914.
KEGGihsa:914.
UCSCiuc001egu.4. human.

Organism-specific databases

CTDi914.
GeneCardsiGC01P117297.
H-InvDBHIX0000931.
HGNCiHGNC:1639. CD2.
HPAiCAB002430.
HPA003883.
MIMi186990. gene.
neXtProtiNX_P06729.
PharmGKBiPA26198.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47564.
HOGENOMiHOG000276890.
HOVERGENiHBG000262.
InParanoidiP06729.
KOiK06449.
OMAiGTQVHQQ.
OrthoDBiEOG7KSX9X.
PhylomeDBiP06729.
TreeFamiTF335971.

Enzyme and pathway databases

ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
SignaLinkiP06729.

Miscellaneous databases

EvolutionaryTraceiP06729.
GeneWikiiCD2.
GenomeRNAii914.
NextBioi3780.
PROiP06729.
SOURCEiSearch...

Gene expression databases

BgeeiP06729.
CleanExiHS_CD2.
ExpressionAtlasiP06729. baseline and differential.
GenevestigatoriP06729.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR015632. CD2.
IPR013783. Ig-like_fold.
IPR008424. Ig_C2-set.
IPR013106. Ig_V-set.
IPR015631. SLAM_fam_rcpts.
[Graphical view]
PANTHERiPTHR12080. PTHR12080. 1 hit.
PTHR12080:SF10. PTHR12080:SF10. 1 hit.
PfamiPF05790. C2-set. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSiPR01870. CD2ANTIGEN.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Exon-intron organization and sequence comparison of human and murine T11 (CD2) genes."
    Diamond D.J., Clayton L.K., Sayre P.H., Reinherz E.L.
    Proc. Natl. Acad. Sci. U.S.A. 85:1615-1619(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Molecular cloning of the CD2 antigen, the T-cell erythrocyte receptor, by a rapid immunoselection procedure."
    Seed B., Aruffo A.
    Proc. Natl. Acad. Sci. U.S.A. 84:3365-3369(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-266.
  3. "Molecular cloning of the human T-lymphocyte surface CD2 (T11) antigen."
    Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
    Proc. Natl. Acad. Sci. U.S.A. 83:8718-8722(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Erratum
    Sewell W.A., Brown M.H., Dunne J., Owen M.J., Crumpton M.J.
    Proc. Natl. Acad. Sci. U.S.A. 84:7256-7256(1987)
    Cited for: SEQUENCE REVISION.
  5. "Molecular cloning and expression of T11 cDNAs reveal a receptor-like structure on human T lymphocytes."
    Sayre P.H., Chang H.-C., Hussey R.E., Brown N.R., Richardson N.E., Spagnoli G., Clayton L.K., Reinherz E.L.
    Proc. Natl. Acad. Sci. U.S.A. 84:2941-2945(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "The structure of the human CD2 gene and its expression in transgenic mice."
    Lang G., Wotton D., Owen M.J., Sewell W.A., Brown M.H., Mason D.Y., Crumpton M.J., Kioussis D.
    EMBO J. 7:1675-1682(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-266.
  7. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-266.
    Tissue: Pancreas and Spleen.
  9. "Monoclonal antibody and ligand binding sites of the T cell erythrocyte receptor (CD2)."
    Peterson A., Seed B.
    Nature 329:842-846(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  10. "Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59."
    Hahn W.C., Menu E., Bothwell A.L.M., Sims P.J., Bierer B.E.
    Science 256:1805-1807(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CD59-BINDING DATA.
  11. "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion."
    Li J., Nishizawa K., An W., Hussey R.E., Lialios F.E., Salgia R., Sunder-Plassmann R., Reinherz E.L.
    EMBO J. 17:7320-7336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSTPIP1.
  12. "Crystal structure of the extracellular region of the human cell adhesion molecule CD2 at 2.5-A resolution."
    Bodian D.L., Jones E.Y., Harlos K., Stuart D.I., Davis S.J.
    Structure 2:755-766(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-206, DISULFIDE BONDS.
  13. "Structure of the glycosylated adhesion domain of human T lymphocyte glycoprotein CD2."
    Withka J.M., Wyss D.F., Wagner G., Arulanandam A.R.N., Reinherz E.L., Recny M.A.
    Structure 1:69-81(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-129.
  14. "Conformation and function of the N-linked glycan in the adhesion domain of human CD2."
    Wyss D.F., Choi J.S., Li J., Knoppers M.H., Willis K.J., Arulanandam A.R., Smolyar A., Reinherz E.L., Wagner G.
    Science 269:1273-1278(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-129.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-217.

Entry informationi

Entry nameiCD2_HUMAN
AccessioniPrimary (citable) accession number: P06729
Secondary accession number(s): Q96TE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: October 23, 2007
Last modified: January 7, 2015
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.