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P06127

- CD5_HUMAN

UniProt

P06127 - CD5_HUMAN

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Protein

T-cell surface glycoprotein CD5

Gene

CD5

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

Functioni

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

GO - Molecular functioni

  1. receptor activity Source: UniProtKB
  2. scavenger receptor activity Source: InterPro
  3. transmembrane signaling receptor activity Source: UniProtKB

GO - Biological processi

  1. apoptotic signaling pathway Source: Ensembl
  2. cell proliferation Source: UniProtKB
  3. cell recognition Source: UniProtKB
  4. T cell costimulation Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
T-cell surface glycoprotein CD5
Alternative name(s):
Lymphocyte antigen T1/Leu-1
CD_antigen: CD5
Gene namesi
Name:CD5
Synonyms:LEU1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:1685. CD5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26224.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Add
BLAST
Chaini25 – 495471T-cell surface glycoprotein CD5PRO_0000033222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi44 ↔ 861 PublicationPROSITE-ProRule annotation
Disulfide bondi60 ↔ 1251 PublicationPROSITE-ProRule annotation
Disulfide bondi81 ↔ 1321 PublicationPROSITE-ProRule annotation
Disulfide bondi107 ↔ 1171 PublicationPROSITE-ProRule annotation
Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi201 ↔ 267PROSITE-ProRule annotation
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi244 ↔ 250PROSITE-ProRule annotation
Disulfide bondi285 ↔ 3211 PublicationPROSITE-ProRule annotation
Disulfide bondi301 ↔ 3601 PublicationPROSITE-ProRule annotation
Disulfide bondi316 ↔ 3671 PublicationPROSITE-ProRule annotation
Disulfide bondi342 ↔ 3501 PublicationPROSITE-ProRule annotation
Modified residuei439 – 4391Phosphoserine2 Publications
Modified residuei453 – 4531Phosphotyrosine1 Publication
Modified residuei460 – 4601Phosphoserine1 Publication
Modified residuei483 – 4831Phosphoserine1 Publication
Modified residuei485 – 4851Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP06127.
PaxDbiP06127.
PRIDEiP06127.

PTM databases

PhosphoSiteiP06127.
UniCarbKBiP06127.

Expressioni

Gene expression databases

BgeeiP06127.
CleanExiHS_CD5.
ExpressionAtlasiP06127. baseline and differential.
GenevestigatoriP06127.

Organism-specific databases

HPAiCAB015392.
CAB020308.

Interactioni

Subunit structurei

Interacts with CD72/LYB-2. Interacts with PTPN6/SHP-1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi107359. 14 interactions.
DIPiDIP-21N.
IntActiP06127. 3 interactions.
MINTiMINT-4656212.
STRINGi9606.ENSP00000342681.

Structurei

Secondary structure

1
495
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 373
Beta strandi39 – 424
Beta strandi45 – 528
Beta strandi55 – 584
Helixi75 – 773
Helixi78 – 836
Beta strandi86 – 883
Beta strandi90 – 945
Turni101 – 1033
Beta strandi104 – 1107
Beta strandi117 – 1193
Beta strandi122 – 1243
Beta strandi126 – 1327
Beta strandi275 – 2806
Beta strandi286 – 29510
Beta strandi298 – 3014
Helixi310 – 3189
Beta strandi323 – 3319
Beta strandi339 – 3413
Beta strandi344 – 3463
Helixi347 – 3493
Beta strandi354 – 3563
Beta strandi362 – 3676

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA4X-ray2.21A270-369[»]
2JOPNMR-A25-134[»]
2JP0NMR-A25-134[»]
2OTTX-ray2.50X/Y276-368[»]
ProteinModelPortaliP06127.
SMRiP06127. Positions 25-134, 269-369.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06127.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 372348ExtracellularSequence AnalysisAdd
BLAST
Topological domaini403 – 49593CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei373 – 40230HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 13399SRCR 1PROSITE-ProRule annotationAdd
BLAST
Domaini159 – 268110SRCR 2PROSITE-ProRule annotationAdd
BLAST
Domaini276 – 36893SRCR 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 SRCR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG86650.
GeneTreeiENSGT00390000017536.
HOGENOMiHOG000111490.
HOVERGENiHBG005286.
InParanoidiP06127.
KOiK06455.
OMAiMSFHRNH.
OrthoDBiEOG7TF792.
PhylomeDBiP06127.
TreeFamiTF329295.

Family and domain databases

Gene3Di3.10.250.10. 2 hits.
InterProiIPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR003566. Tcell_CD5.
[Graphical view]
PfamiPF00530. SRCR. 2 hits.
[Graphical view]
PRINTSiPR00258. SPERACTRCPTR.
PR01409. TCELLCD5.
SMARTiSM00202. SR. 2 hits.
[Graphical view]
SUPFAMiSSF56487. SSF56487. 2 hits.
PROSITEiPS50287. SRCR_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06127-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPMGSLQPLA TLYLLGMLVA SCLGRLSWYD PDFQARLTRS NSKCQGQLEV
60 70 80 90 100
YLKDGWHMVC SQSWGRSSKQ WEDPSQASKV CQRLNCGVPL SLGPFLVTYT
110 120 130 140 150
PQSSIICYGQ LGSFSNCSHS RNDMCHSLGL TCLEPQKTTP PTTRPPPTTT
160 170 180 190 200
PEPTAPPRLQ LVAQSGGQHC AGVVEFYSGS LGGTISYEAQ DKTQDLENFL
210 220 230 240 250
CNNLQCGSFL KHLPETEAGR AQDPGEPREH QPLPIQWKIQ NSSCTSLEHC
260 270 280 290 300
FRKIKPQKSG RVLALLCSGF QPKVQSRLVG GSSICEGTVE VRQGAQWAAL
310 320 330 340 350
CDSSSARSSL RWEEVCREQQ CGSVNSYRVL DAGDPTSRGL FCPHQKLSQC
360 370 380 390 400
HELWERNSYC KKVFVTCQDP NPAGLAAGTV ASIILALVLL VVLLVVCGPL
410 420 430 440 450
AYKKLVKKFR QKKQRQWIGP TGMNQNMSFH RNHTATVRSH AENPTASHVD
460 470 480 490
NEYSQPPRNS HLSAYPALEG ALHRSSMQPD NSSDSDYDLH GAQRL
Length:495
Mass (Da):54,578
Last modified:November 30, 2010 - v2
Checksum:i9131AEC9683EE1D3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti289 – 2891V → E in BAF85387. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241P → L.1 Publication
Corresponds to variant rs2241002 [ dbSNP | Ensembl ].
VAR_020411
Natural varianti461 – 4611H → R.6 Publications
Corresponds to variant rs637186 [ dbSNP | Ensembl ].
VAR_024649
Natural varianti471 – 4711A → V.4 Publications
Corresponds to variant rs2229177 [ dbSNP | Ensembl ].
VAR_058203

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04391 mRNA. Translation: CAA27979.1.
X89405
, 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.
CCDSiCCDS8000.1.
PIRiA26396.
RefSeqiNP_055022.2. NM_014207.3.
UniGeneiHs.58685.

Genome annotation databases

EnsembliENST00000347785; ENSP00000342681; ENSG00000110448.
GeneIDi921.
KEGGihsa:921.
UCSCiuc009ynk.3. human.

Polymorphism databases

DMDMi313104090.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04391 mRNA. Translation: CAA27979.1 .
X89405
, 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 .
CCDSi CCDS8000.1.
PIRi A26396.
RefSeqi NP_055022.2. NM_014207.3.
UniGenei Hs.58685.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JA4 X-ray 2.21 A 270-369 [» ]
2JOP NMR - A 25-134 [» ]
2JP0 NMR - A 25-134 [» ]
2OTT X-ray 2.50 X/Y 276-368 [» ]
ProteinModelPortali P06127.
SMRi P06127. Positions 25-134, 269-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107359. 14 interactions.
DIPi DIP-21N.
IntActi P06127. 3 interactions.
MINTi MINT-4656212.
STRINGi 9606.ENSP00000342681.

PTM databases

PhosphoSitei P06127.
UniCarbKBi P06127.

Polymorphism databases

DMDMi 313104090.

Proteomic databases

MaxQBi P06127.
PaxDbi P06127.
PRIDEi P06127.

Protocols and materials databases

DNASUi 921.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000347785 ; ENSP00000342681 ; ENSG00000110448 .
GeneIDi 921.
KEGGi hsa:921.
UCSCi uc009ynk.3. human.

Organism-specific databases

CTDi 921.
GeneCardsi GC11P060869.
H-InvDB HIX0009680.
HGNCi HGNC:1685. CD5.
HPAi CAB015392.
CAB020308.
MIMi 153340. gene.
neXtProti NX_P06127.
PharmGKBi PA26224.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG86650.
GeneTreei ENSGT00390000017536.
HOGENOMi HOG000111490.
HOVERGENi HBG005286.
InParanoidi P06127.
KOi K06455.
OMAi MSFHRNH.
OrthoDBi EOG7TF792.
PhylomeDBi P06127.
TreeFami TF329295.

Miscellaneous databases

EvolutionaryTracei P06127.
GeneWikii CD5_(protein).
GenomeRNAii 921.
NextBioi 3810.
PROi P06127.
SOURCEi Search...

Gene expression databases

Bgeei P06127.
CleanExi HS_CD5.
ExpressionAtlasi P06127. baseline and differential.
Genevestigatori P06127.

Family and domain databases

Gene3Di 3.10.250.10. 2 hits.
InterProi IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR003566. Tcell_CD5.
[Graphical view ]
Pfami PF00530. SRCR. 2 hits.
[Graphical view ]
PRINTSi PR00258. SPERACTRCPTR.
PR01409. TCELLCD5.
SMARTi SM00202. SR. 2 hits.
[Graphical view ]
SUPFAMi SSF56487. SSF56487. 2 hits.
PROSITEi PS50287. SRCR_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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. 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.

Entry informationi

Entry nameiCD5_HUMAN
AccessioniPrimary (citable) accession number: P06127
Secondary accession number(s): A0N0P4, A8K9I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 30, 2010
Last modified: October 29, 2014
This is version 149 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 11
    Human chromosome 11: 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