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P06127 (CD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-cell surface glycoprotein CD5
Alternative name(s):
Lymphocyte antigen T1/Leu-1
CD_antigen=CD5
Gene names
Name:CD5
Synonyms:LEU1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May act as a receptor in regulating T-cell proliferation.

Subunit structure

Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 By similarity. Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Post-translational modification

Phosphorylated on tyrosine residues by LYN; this creates binding sites for PTPN6/SHP-1 By similarity.

Sequence similarities

Contains 3 SRCR domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424
Chain25 – 495471T-cell surface glycoprotein CD5
PRO_0000033222

Regions

Topological domain25 – 372348Extracellular Potential
Transmembrane373 – 40230Helical; Potential
Topological domain403 – 49593Cytoplasmic Potential
Domain35 – 13399SRCR 1
Domain159 – 268110SRCR 2
Domain276 – 36893SRCR 3

Amino acid modifications

Modified residue4391Phosphoserine Ref.8 Ref.9
Modified residue4531Phosphotyrosine Ref.10
Modified residue4601Phosphoserine Ref.8
Modified residue4831Phosphoserine Ref.10
Modified residue4851Phosphoserine Ref.10
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 86 Ref.12
Disulfide bond60 ↔ 125 Ref.12
Disulfide bond81 ↔ 132 Ref.12
Disulfide bond107 ↔ 117 Ref.12
Disulfide bond201 ↔ 267 By similarity
Disulfide bond244 ↔ 250 By similarity
Disulfide bond285 ↔ 321 Ref.12
Disulfide bond301 ↔ 360 Ref.12
Disulfide bond316 ↔ 367 Ref.12
Disulfide bond342 ↔ 350 Ref.12

Natural variations

Natural variant2241P → L. Ref.4
Corresponds to variant rs2241002 [ dbSNP | Ensembl ].
VAR_020411
Natural variant4611H → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.8
Corresponds to variant rs637186 [ dbSNP | Ensembl ].
VAR_024649
Natural variant4711A → V. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs2229177 [ dbSNP | Ensembl ].
VAR_058203

Experimental info

Sequence conflict2891V → E in BAF85387. Ref.4

Secondary structure

............................................ 495
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06127 [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 9131AEC9683EE1D3

FASTA49554,578
        10         20         30         40         50         60 
MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV YLKDGWHMVC 

        70         80         90        100        110        120 
SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT PQSSIICYGQ LGSFSNCSHS 

       130        140        150        160        170        180 
RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS 

       190        200        210        220        230        240 
LGGTISYEAQ DKTQDLENFL CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ 

       250        260        270        280        290        300 
NSSCTSLEHC FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL 

       310        320        330        340        350        360 
CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC HELWERNSYC 

       370        380        390        400        410        420 
KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL AYKKLVKKFR QKKQRQWIGP 

       430        440        450        460        470        480 
TGMNQNMSFH RNHTATVRSH AENPTASHVD NEYSQPPRNS HLSAYPALEG ALHRSSMQPD 

       490 
NSSDSDYDLH GAQRL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1."
Jones N.H., Clabby M.L., Dialynas D.P., Huag H.-J.S., Herzenberg L.A., Strominger J.L.
Nature 323:346-349(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-461 AND VAL-471.
[2]"Evolutionarily conserved transcription regulatory elements within the 5'-flanking region of the human CD5 gene."
Calvo J., Sole J., Simarro M., Vives J., Lozano F.
Tissue Antigens 47:257-261(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-461 AND VAL-471.
Tissue: Lymphocyte.
[3]Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B., Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O., Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I., Nickerson D.A.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-461 AND VAL-471.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-224 AND ARG-461.
Tissue: Thymus.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANTS ARG-461 AND VAL-471.
Tissue: Pancreas.
[7]"The B-cell surface protein CD72/Lyb-2 is the ligand for CD5."
van de Velde H., von Hoegen I., Luo W., Parnes J.R., Thielemans K.
Nature 351:662-665(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD72/LYB-2.
[8]"Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry."
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T., Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-460, VARIANT [LARGE SCALE ANALYSIS] ARG-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-453; SER-483 AND SER-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Crystal structure of the third extracellular domain of CD5 reveals the fold of a group B scavenger cysteine-rich receptor domain."
Rodamilans B., Munoz I.G., Bragado-Nilsson E., Sarrias M.R., Padilla O., Blanco F.J., Lozano F., Montoya G.
J. Biol. Chem. 282:12669-12677(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 270-369.
[12]"Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5."
Garza-Garcia A., Esposito D., Rieping W., Harris R., Briggs C., Brown M.H., Driscoll P.C.
J. Mol. Biol. 378:129-144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 25-134, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04391 mRNA. Translation: CAA27979.1.
X89405 expand/collapse EMBL AC list , AJ237927, AJ237928, AJ237929, AJ237930, AJ237931, AJ237932 Genomic DNA. Translation: CAA61584.2.
EF064752 Genomic DNA. Translation: ABK41935.1.
AK292698 mRNA. Translation: BAF85387.1.
AP000437 Genomic DNA. No translation available.
BC027901 mRNA. Translation: AAH27901.1.
PIRA26396.
RefSeqNP_055022.2. NM_014207.3.
UniGeneHs.58685.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA4X-ray2.21A270-369[»]
2JOPNMR-A25-134[»]
2JP0NMR-A25-134[»]
2OTTX-ray2.50X/Y276-369[»]
ProteinModelPortalP06127.
SMRP06127. Positions 25-134, 269-369.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107359. 14 interactions.
DIPDIP-21N.
IntActP06127. 3 interactions.
MINTMINT-4656212.
STRING9606.ENSP00000342681.

PTM databases

PhosphoSiteP06127.
UniCarbKBP06127.

Polymorphism databases

DMDM313104090.

Proteomic databases

PaxDbP06127.
PRIDEP06127.

Protocols and materials databases

DNASU921.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347785; ENSP00000342681; ENSG00000110448.
GeneID921.
KEGGhsa:921.
UCSCuc009ynk.3. human.

Organism-specific databases

CTD921.
GeneCardsGC11P060869.
H-InvDBHIX0009680.
HGNCHGNC:1685. CD5.
HPACAB015392.
CAB020308.
MIM153340. gene.
neXtProtNX_P06127.
PharmGKBPA26224.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG86650.
HOGENOMHOG000111490.
HOVERGENHBG005286.
InParanoidP06127.
KOK06455.
OMAMSFHRNH.
OrthoDBEOG7TF792.
PhylomeDBP06127.
TreeFamTF329295.

Gene expression databases

ArrayExpressP06127.
BgeeP06127.
CleanExHS_CD5.
GenevestigatorP06127.

Family and domain databases

Gene3D3.10.250.10. 2 hits.
InterProIPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR003566. Tcell_CD5.
[Graphical view]
PANTHERPTHR19331:SF6. PTHR19331:SF6. 1 hit.
PfamPF00530. SRCR. 2 hits.
[Graphical view]
PRINTSPR00258. SPERACTRCPTR.
PR01409. TCELLCD5.
SMARTSM00202. SR. 2 hits.
[Graphical view]
SUPFAMSSF56487. SSF56487. 2 hits.
PROSITEPS50287. SRCR_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06127.
GeneWikiCD5_(protein).
GenomeRNAi921.
NextBio3810.
PROP06127.
SOURCESearch...

Entry information

Entry nameCD5_HUMAN
AccessionPrimary (citable) accession number: P06127
Secondary accession number(s): A0N0P4, A8K9I3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries