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P16070 (CD44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CD44 antigen
Alternative name(s):
CDw44
Epican
Extracellular matrix receptor III
Short name=ECMR-III
GP90 lymphocyte homing/adhesion receptor
HUTCH-I
Heparan sulfate proteoglycan
Hermes antigen
Hyaluronate receptor
Phagocytic glycoprotein 1
Short name=PGP-1
Phagocytic glycoprotein I
Short name=PGP-I
CD_antigen=CD44
Gene names
Name:CD44
Synonyms:LHR, MDU2, MDU3, MIC4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events. Ref.31

Subunit structure

Interacts with PKN2. Interacts with TIAM1 and TIAM2 By similarity. Interacts with HA, as well as other glycosaminoglycans, collagen, laminin, and fibronectin via its N-terminal segment. Interacts with ANK, the ERM proteins (VIL2, RDX and MSN), and NF2 via its C-terminal segment. Ref.41

Subcellular location

Cell membrane; Single-pass type I membrane protein. Note: Colocalizes with actin in membrane protrusions at wounding edges By similarity.

Tissue specificity

Isoform 10 (epithelial isoform) is expressed by cells of epithelium and highly expressed by carcinomas. Expression is repressed in neuroblastoma cells.

Domain

The lectin-like LINK domain is responsible for hyaluronan binding By similarity.

Post-translational modification

Proteolytically cleaved in the extracellular matrix by specific proteinases (possibly MMPs) in several cell lines and tumors. Ref.28

N- and O-glycosylated. O-glycosylation contains more-or-less-sulfated chondroitin sulfate glycans, whose number may affect the accessibility of specific proteinases to their cleavage site(s). It is uncertain if O-glycosylation occurs on Thr-637 or Thr-638. Ref.28 Ref.39

Phosphorylated; activation of PKC results in the dephosphorylation of Ser-706 (constitutive phosphorylation site), and the phosphorylation of Ser-672. Ref.26 Ref.27

Polymorphism

CD44 is responsible for the Indian blood group system. The molecular basis of the In(A)=In1/In(B)=In2 blood group antigens is a single variation in position 46; In(B), the most frequent allele, has Arg-46.

Sequence similarities

Contains 1 Link domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionBlood group antigen
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

branching involved in prostate gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cartilage development

Inferred from expression pattern PubMed 11944887. Source: UniProtKB

cell-cell adhesion

Non-traceable author statement Ref.18. Source: UniProtKB

cell-matrix adhesion

Non-traceable author statement Ref.18. Source: UniProtKB

cellular response to fibroblast growth factor stimulus

Inferred from direct assay PubMed 19577615. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

hyaluronan catabolic process

Inferred from direct assay PubMed 17170110. Source: UniProtKB

hyaluronan metabolic process

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

monocyte aggregation

Inferred from mutant phenotype PubMed 15100360. Source: UniProtKB

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 19047049. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 19047049. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of heterotypic cell-cell adhesion

Inferred from mutant phenotype PubMed 15100360. Source: UniProtKB

positive regulation of monocyte aggregation

Inferred from mutant phenotype PubMed 20522558. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 17045821. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

wound healing involved in inflammatory response

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 17170110. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337. Source: UniProt

integral component of plasma membrane

Non-traceable author statement Ref.3. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functioncollagen binding

Non-traceable author statement PubMed 2471973. Source: UniProtKB

hyaluronic acid binding

Inferred from direct assay PubMed 17170110PubMed 17324121. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from direct assay PubMed 17170110. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ipaBP180114EBI-490245,EBI-490239From a different organism.
MSNP260386EBI-490245,EBI-528768
SLC7A11Q9UPY54EBI-490245,EBI-3843348

Alternative products

This entry describes 19 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Additional isoforms are produced by alternative splicing of 10 out of 19 exons within the extracellular domain. Additional diversity is generated through the utilization of internal splice donor and acceptor sites within 2 of the exons. A variation in the cytoplasmic domain was shown to result from the alternative splicing of 2 exons. Isoform CD44 is expected to be expressed in normal cells. Splice variants have been found in many tumor cell lines. Exons 5, 6, 7, 8, 9, 10, 11, 13, 14 and 19 are alternatively spliced. Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P16070-1)

Also known as: CD44;

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.
Note: Corresponds to the largest isoform.
Isoform 2 (identifier: P16070-2)

Also known as: CD44SP;

The sequence of this isoform differs from the canonical sequence as follows:
     23-29: DLNITCR → GVGRRKS
     30-742: Missing.
Isoform 3 (identifier: P16070-3)

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: G → A
     193-223: Missing.
Note: Alternative splice donor/acceptor on exon 5.
Isoform 4 (identifier: P16070-4)

Also known as: Epidermal;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → S
     224-266: Missing.
Note: Lacks exon 6.
Isoform 5 (identifier: P16070-5)

The sequence of this isoform differs from the canonical sequence as follows:
     266-273: Missing.
Note: Alternative splice donor/acceptor on exon 7.
Isoform 6 (identifier: P16070-6)

The sequence of this isoform differs from the canonical sequence as follows:
     385-385: I → T
     386-428: Missing.
Note: Lacks exon 10.
Isoform 7 (identifier: P16070-7)

The sequence of this isoform differs from the canonical sequence as follows:
     506-506: Q → R
     507-535: Missing.
Note: Lacks exon 13.
Isoform 8 (identifier: P16070-8)

The sequence of this isoform differs from the canonical sequence as follows:
     536-536: N → R
     537-604: Missing.
Note: Lacks exon 14.
Isoform 9 (identifier: P16070-9)

The sequence of this isoform differs from the canonical sequence as follows:
     675-675: R → S
     676-742: Missing.
Note: Lacks exon 19.
Isoform 10 (identifier: P16070-10)

Also known as: CD44E; CD44R1; Epithelial; Keratinocyte;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → N
     224-472: Missing.
Note: Lacks exons 6-11.
Isoform 11 (identifier: P16070-11)

Also known as: CD44R2;

The sequence of this isoform differs from the canonical sequence as follows:
     223-535: Missing.
Note: Lacks exons 6-13.
Isoform 12 (identifier: P16070-12)

Also known as: CDw44; Reticulocyte;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → R
     224-604: Missing.
Note: Lacks exons 6-14.
Isoform 13 (identifier: P16070-13)

Also known as: CD44R4;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → N
     224-472: Missing.
     536-536: N → R
     537-604: Missing.
Note: Lacks exons 6-11 and exon 14.
Isoform 14 (identifier: P16070-14)

Also known as: CD44R5;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → N
     224-472: Missing.
     506-506: Q → R
     507-535: Missing.
     536-536: N → R
     537-604: Missing.
Note: Lacks exons 6-11, exon 13 and exon 14.
Isoform 15 (identifier: P16070-15)

Also known as: Hermes;

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → R
     224-604: Missing.
     675-675: R → S
     676-742: Missing.
Note: Lacks exons 6-14 and exon 19.
Isoform 16 (identifier: P16070-16)

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: G → A
     193-223: Missing.
     385-385: I → T
     386-428: Missing.
Note: Alternative splice donor/acceptor on exon 5 and lacks exon 10.
Isoform 17 (identifier: P16070-17)

The sequence of this isoform differs from the canonical sequence as follows:
     266-273: Missing.
     385-385: I → T
     386-428: Missing.
Note: Alternative splice donor/acceptor on exon 7 and lacks exon 10.
Isoform 18 (identifier: P16070-18)

The sequence of this isoform differs from the canonical sequence as follows:
     223-223: T → R
     224-604: Missing.
     605-625: Missing.
Note: No experimental confirmation available.
Isoform 19 (identifier: P16070-19)

Also known as: CD44RC;

The sequence of this isoform differs from the canonical sequence as follows:
     78-139: RYGFIEGHVV...TSVTDLPNAF → SLHCSQQSKK...VRNSRPVYDS
     140-742: Missing.
Note: Soluble isoform, has enhanced hyaluronan binding.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 742722CD44 antigen
PRO_0000026687

Regions

Topological domain21 – 649629Extracellular Potential
Transmembrane650 – 67021Helical; Potential
Topological domain671 – 74272Cytoplasmic Potential
Domain32 – 12089Link
Region224 – 649426Stem
Compositional bias150 – 1589Arg/Lys-rich (basic)

Sites

Binding site411Hyaluronan By similarity
Binding site781Hyaluronan By similarity
Binding site791Hyaluronan By similarity
Binding site1051Hyaluronan By similarity

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid Probable
Modified residue6721Phosphoserine; by PKC Ref.27
Modified residue6861Phosphoserine Ref.30 Ref.37
Modified residue6971Phosphoserine By similarity
Modified residue7061Phosphoserine Ref.26 Ref.30 Ref.32 Ref.33 Ref.37 Ref.40
Glycosylation251N-linked (GlcNAc...) Potential
Glycosylation571N-linked (GlcNAc...) Ref.29 Ref.35
Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation1101N-linked (GlcNAc...) Ref.35
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation3501N-linked (GlcNAc...) Potential
Glycosylation5481N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Glycosylation6361N-linked (GlcNAc...) Potential
Glycosylation6371O-linked (GalNAc...); or Thr-638 Ref.39
Glycosylation6381O-linked (GalNAc...); or Thr-637 Ref.39
Disulfide bond28 ↔ 129 By similarity
Disulfide bond53 ↔ 118 By similarity
Disulfide bond77 ↔ 97 By similarity

Natural variations

Alternative sequence23 – 297DLNITCR → GVGRRKS in isoform 2.
VSP_005303
Alternative sequence30 – 742713Missing in isoform 2.
VSP_005304
Alternative sequence78 – 13962RYGFI…LPNAF → SLHCSQQSKKVWAEEKASDQ QWQWSCGGQKAKWTQRRGQQ VSGNGAFGEQGVVRNSRPVY DS in isoform 19.
VSP_043870
Alternative sequence140 – 742603Missing in isoform 19.
VSP_043871
Alternative sequence1921G → A in isoform 3 and isoform 16.
VSP_005305
Alternative sequence193 – 22331Missing in isoform 3 and isoform 16.
VSP_005306
Alternative sequence223 – 535313Missing in isoform 11.
VSP_022797
Alternative sequence2231T → N in isoform 10, isoform 13 and isoform 14.
VSP_005309
Alternative sequence2231T → R in isoform 12, isoform 15 and isoform 18.
VSP_005311
Alternative sequence2231T → S in isoform 4.
VSP_005307
Alternative sequence224 – 604381Missing in isoform 12, isoform 15 and isoform 18.
VSP_005312
Alternative sequence224 – 472249Missing in isoform 10, isoform 13 and isoform 14.
VSP_005310
Alternative sequence224 – 26643Missing in isoform 4.
VSP_005308
Alternative sequence266 – 2738Missing in isoform 5 and isoform 17.
VSP_005313
Alternative sequence3851I → T in isoform 6, isoform 16 and isoform 17.
VSP_005314
Alternative sequence386 – 42843Missing in isoform 6, isoform 16 and isoform 17.
VSP_005315
Alternative sequence5061Q → R in isoform 7 and isoform 14.
VSP_005316
Alternative sequence507 – 53529Missing in isoform 7 and isoform 14.
VSP_005317
Alternative sequence5361N → R in isoform 8, isoform 13 and isoform 14.
VSP_005318
Alternative sequence537 – 60468Missing in isoform 8, isoform 13 and isoform 14.
VSP_005319
Alternative sequence605 – 62521Missing in isoform 18.
VSP_043575
Alternative sequence6751R → S in isoform 9 and isoform 15.
VSP_005320
Alternative sequence676 – 74267Missing in isoform 9 and isoform 15.
VSP_005321
Natural variant461R → P in In(A) antigen. Ref.43
VAR_006490
Natural variant3931T → M.
Corresponds to variant rs11607491 [ dbSNP | Ensembl ].
VAR_030325
Natural variant4171K → R. Ref.6 Ref.7 Ref.17 Ref.24
Corresponds to variant rs9666607 [ dbSNP | Ensembl ].
VAR_021147
Natural variant4791I → T. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.11 Ref.17 Ref.22
Corresponds to variant rs1467558 [ dbSNP | Ensembl ].
VAR_030326
Natural variant4941D → H. Ref.7
Corresponds to variant rs12273397 [ dbSNP | Ensembl ].
VAR_030327

Experimental info

Sequence conflict261I → M in AAA82949. Ref.10
Sequence conflict1091S → Y in AAA35674. Ref.1
Sequence conflict1091S → Y in AAA51950. Ref.2
Sequence conflict1091S → Y in CAA38951. Ref.3
Sequence conflict1091S → Y in CAB61878. Ref.7
Sequence conflict2211A → R in CAA38951. Ref.3
Sequence conflict2411T → A in CAB61878. Ref.7
Sequence conflict4101E → V in CAA47271. Ref.5
Sequence conflict4941D → N in CAB61878. Ref.7
Sequence conflict5551T → H in CAA38951. Ref.3
Sequence conflict6201G → E in AAA35674. Ref.1
Sequence conflict6971S → I in AAM50041. Ref.11
Sequence conflict6971S → I in AAH67348. Ref.16

Secondary structure

...................................... 742
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CD44) [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: BB9B66B19B970349

FASTA74281,538
        10         20         30         40         50         60 
MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL 

        70         80         90        100        110        120 
PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN 

       130        140        150        160        170        180 
ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS 

       190        200        210        220        230        240 
GSSSERSSTS GGYIFYTFST VHPIPDEDSP WITDSTDRIP ATTLMSTSAT ATETATKRQE 

       250        260        270        280        290        300 
TWDWFSWLFL PSESKNHLHT TTQMAGTSSN TISAGWEPNE ENEDERDRHL SFSGSGIDDD 

       310        320        330        340        350        360 
EDFISSTIST TPRAFDHTKQ NQDWTQWNPS HSNPEVLLQT TTRMTDVDRN GTTAYEGNWN 

       370        380        390        400        410        420 
PEAHPPLIHH EHHEEEETPH STSTIQATPS STTEETATQK EQWFGNRWHE GYRQTPKEDS 

       430        440        450        460        470        480 
HSTTGTAAAS AHTSHPMQGR TTPSPEDSSW TDFFNPISHP MGRGHQAGRR MDMDSSHSIT 

       490        500        510        520        530        540 
LQPTANPNTG LVEDLDRTGP LSMTTQQSNS QSFSTSHEGL EEDKDHPTTS TLTSSNRNDV 

       550        560        570        580        590        600 
TGGRRDPNHS EGSTTLLEGY TSHYPHTKES RTFIPVTSAK TGSFGVTAVT VGDSNSNVNR 

       610        620        630        640        650        660 
SLSGDQDTFH PSGGSHTTHG SESDGHSHGS QEGGANTTSG PIRTPQIPEW LIILASLLAL 

       670        680        690        700        710        720 
ALILAVCIAV NSRRRCGQKK KLVINSGNGA VEDRKPSGLN GEASKSQEMV HLVNKESSET 

       730        740 
PDQFMTADET RNLQNVDMKI GV 

« Hide

Isoform 2 (CD44SP) [UniParc].

Checksum: FD28FA0E33AB08B9
Show »

FASTA293,327
Isoform 3 [UniParc].

Checksum: EF48BFB8E4478B97
Show »

FASTA71177,983
Isoform 4 (Epidermal) [UniParc].

Checksum: CEC79496379F44FF
Show »

FASTA69976,612
Isoform 5 [UniParc].

Checksum: 48D27AD91375BCDC
Show »

FASTA73480,790
Isoform 6 [UniParc].

Checksum: A150D6FA11DAABD6
Show »

FASTA69976,705
Isoform 7 [UniParc].

Checksum: 2C2098B56FF4F30E
Show »

FASTA71378,446
Isoform 8 [UniParc].

Checksum: 538CB559E671CF23
Show »

FASTA67474,388
Isoform 9 [UniParc].

Checksum: 3891F679BC733F89
Show »

FASTA67574,196
Isoform 10 (CD44E) (CD44R1) (Epithelial) (Keratinocyte) [UniParc].

Checksum: A494CCC37F161EF2
Show »

FASTA49353,411
Isoform 11 (CD44R2) [UniParc].

Checksum: 557BD4FED59E0867
Show »

FASTA42946,565
Isoform 12 (CDw44) (Reticulocyte) [UniParc].

Checksum: F51A746B442E0D33
Show »

FASTA36139,416
Isoform 13 (CD44R4) [UniParc].

Checksum: 47F544DD9890917B
Show »

FASTA42546,261
Isoform 14 (CD44R5) [UniParc].

Checksum: 5118DABF71C1F7D0
Show »

FASTA39643,169
Isoform 15 (Hermes) [UniParc].

Checksum: E11B9B38F4A74817
Show »

FASTA29432,075
Isoform 16 [UniParc].

Checksum: D719820A01C4517F
Show »

FASTA66873,150
Isoform 17 [UniParc].

Checksum: 737967321EE8F579
Show »

FASTA69175,957
Isoform 18 [UniParc].

Checksum: C2E036A7DAB5717B
Show »

FASTA34037,278
Isoform 19 (CD44RC) [UniParc].

Checksum: 4A127F5C54BB7B62
Show »

FASTA13915,635

References

« Hide 'large scale' references
[1]"A lymphocyte molecule implicated in lymph node homing is a member of the cartilage link protein family."
Stamenkovic I., Amiot M., Pesando J.M., Seed B.
Cell 56:1057-1062(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
[2]"The multispecific cell adhesion molecule CD44 is represented in reticulocyte cDNA."
Harn H.-J., Isola N., Cooper D.L.
Biochem. Biophys. Res. Commun. 178:1127-1134(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
Tissue: Reticulocyte.
[3]"The hematopoietic and epithelial forms of CD44 are distinct polypeptides with different adhesion potentials for hyaluronate-bearing cells."
Stamenkovic I., Aruffo A., Amiot M., Seed B.
EMBO J. 10:343-348(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), VARIANT THR-479.
[4]"Molecular cloning of CD44R1 and CD44R2, two novel isoforms of the human CD44 lymphocyte 'homing' receptor expressed by hemopoietic cells."
Dougherty G.J., Lansdorp P.M., Cooper D.L., Humphries R.K.
J. Exp. Med. 174:1-5(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11), VARIANT THR-479.
Tissue: Myeloid leukemia cell.
[5]"The core protein of epican, a heparan sulfate proteoglycan on keratinocytes, is an alternative form of CD44."
Kugelman L.C., Ganguly S., Haggerty J.G., Weissman S.M., Milstone L.M.
J. Invest. Dermatol. 99:886-891(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT THR-479.
Tissue: Keratinocyte.
[6]"Genomic structure of DNA encoding the lymphocyte homing receptor CD44 reveals at least 12 alternatively spliced exons."
Screaton G.R., Bell M.V., Jackson D.G., Cornelis F.B., Gerth U., Bell J.I.
Proc. Natl. Acad. Sci. U.S.A. 89:12160-12164(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS ARG-417 AND THR-479.
Tissue: Lymphoblast.
[7]"CD44: a multitude of isoforms with diverse functions."
Gunthert U.
Curr. Top. Microbiol. Immunol. 184:47-63(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-417; THR-479 AND HIS-494.
[8]"Novel variants of CD44 arising from alternative splicing: changes in the CD44 alternative splicing pattern of MCF-7 breast carcinoma cells treated with hyaluronidase."
Tanabe K.K., Nishi T., Saya H.
Mol. Carcinog. 7:212-220(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 13 AND 14), VARIANT THR-479.
Tissue: Mammary carcinoma.
[9]"Identification and characterization of CD44RC, a novel alternatively spliced soluble CD44 isoform that can potentiate the hyaluronan binding activity of cell surface CD44."
Chiu R.K., Carpenito C., Dougherty S.T., Hayes G.M., Dougherty G.J.
Neoplasia 1:446-452(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19).
[10]"CD44 in normal and neoplastic human cartilage."
Bosch P.P., Stevens J.W., Buckwalter J.A., Midura R.J.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
Tissue: Articular cartilage.
[11]"Sequence analysis of the human CD44 antigen."
Wiebe G.J., Freund D., Corbeil D.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 12), VARIANT THR-479.
Tissue: Colon adenocarcinoma and Retinal pigment epithelium.
[12]"Sequence analysis of a novel human CD44 variant."
Xiang Q., Wang J., Fan C., He X., Huang L., Zhu H., Qiu X., Luo W.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11).
[13]"Construction of human CD44 eukaryotic vector and its expression in mammary carcinoma cells MCF-7."
Fang X., Xu W., Zhang X.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18).
[14]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
Tissue: Spinal cord.
[15]"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].
[16]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[17]"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] (ISOFORMS 4 AND 12), VARIANTS ARG-417 AND THR-479.
Tissue: Pancreas and Retinal pigment epithelium.
[18]"Expression of CD44 is repressed in neuroblastoma cells."
Shtivelman E., Bishop J.M.
Mol. Cell. Biol. 11:5446-5453(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
Tissue: Lymphoblast.
[19]"A human lymphocyte homing receptor, the hermes antigen, is related to cartilage proteoglycan core and link proteins."
Goldstein L.A., Zhou D.F.H., Picker L.J., Minty C.N., Bargatze R.F., Ding J.F., Butcher E.C.
Cell 56:1063-1072(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-742 (ISOFORM 15).
[20]"Anti-(glioma surface antigen) monoclonal antibody G-22 recognizes overexpressed CD44 in glioma cells."
Okada H., Yoshida J., Seo H., Wakabayashi T., Sugita K., Hagiwara M.
Cancer Immunol. Immunother. 39:313-317(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 55-108.
Tissue: Glial tumor.
[21]"A monoclonal antibody that blocks poliovirus attachment recognizes the lymphocyte homing receptor CD44."
Shepley M.P., Racaniello V.R.
J. Virol. 68:1301-1308(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 67-89.
Tissue: Peripheral blood.
[22]"Human keratinocytes express a new CD44 core protein (CD44E) as a heparan-sulfate intrinsic membrane proteoglycan with additional exons."
Brown T.A., Bouchard T., St John T., Wayner E., Carter W.G.
J. Cell Biol. 113:207-221(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 184-625 (ISOFORM 10), VARIANT THR-479.
Tissue: Foreskin.
[23]"Non-invasive detection of malignancy by identification of unusual CD44 gene activity in exfoliated cancer cells."
Matsumura Y., Hanbury D., Smith J., Tarin D.
BMJ 308:619-624(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-267.
[24]"CD44 splice variants confer metastatic behavior in rats: homologous sequences are expressed in human tumor cell lines."
Hofmann M., Rudy W., Zoeller M., Toelg C., Ponta H., Herrlich P., Guenthert U.
Cancer Res. 51:5292-5297(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 267-603 (ISOFORM 1), VARIANT ARG-417.
Tissue: Lung.
[25]"CD44: from adhesion molecules to signalling regulators."
Ponta H., Sherman L., Herrlich P.A.
Nat. Rev. Mol. Cell Biol. 4:33-45(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION, POST-TRANSLATIONAL MODIFICATIONS.
[26]"Hyaluronan-dependent cell migration can be blocked by a CD44 cytoplasmic domain peptide containing a phosphoserine at position 325."
Peck D., Isacke C.M.
J. Cell Sci. 111:1595-1601(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-706.
[27]"A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility."
Legg J.W., Lewis C.A., Parsons M., Ng T., Isacke C.M.
Nat. Cell Biol. 4:399-407(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-672.
[28]"CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage are regulated at post-translational level in cells of melanocytic lineage."
Bartolazzi A.
Melanoma Res. 13:325-337(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION, PROTEOLYTIC PROCESSING.
[29]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57.
Tissue: Plasma.
[30]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[31]"RNA-binding IMPs promote cell adhesion and invadopodia formation."
Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., Nielsen F.C.
EMBO J. 25:1456-1468(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[33]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[34]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-110.
Tissue: Liver.
[36]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[37]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-637 AND THR-638, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
[40]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"Structure of the regulatory hyaluronan binding domain in the inflammatory leukocyte homing receptor CD44."
Teriete P., Banerji S., Noble M., Blundell C.D., Wright A.J., Pickford A.R., Lowe E., Mahoney D.J., Tammi M.I., Kahmann J.D., Campbell I.D., Day A.J., Jackson D.G.
Mol. Cell 13:483-496(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-178, STRUCTURE BY NMR OF 20-178, INTERACTION WITH HA.
[42]"Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR."
Takeda M., Ogino S., Umemoto R., Sakakura M., Kajiwara M., Sugahara K.N., Hayasaka H., Miyasaka M., Terasawa H., Shimada I.
J. Biol. Chem. 281:40089-40095(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 20-178 IN COMPLEX WITH HA.
[43]"A blood group-related polymorphism of CD44 abolishes a hyaluronan-binding consensus sequence without preventing hyaluronan binding."
Telen M.J., Udani M., Washington M.K., Levesque M.C., Lloyd E., Rao N.
J. Biol. Chem. 271:7147-7153(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BLOOD GROUP INDIAN PRO-46.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24915 mRNA. Translation: AAA35674.1.
M59040 mRNA. Translation: AAA51950.1.
X55150 mRNA. Translation: CAA38951.1.
X56794 mRNA. Translation: CAA40133.1.
X66733 mRNA. Translation: CAA47271.1.
L05423 expand/collapse EMBL AC list , L05407, L05408, L05409, L05410, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13622.1.
L05423 expand/collapse EMBL AC list , L05407, L05408, L05410, L05411, L05412, L05414, L05415, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13623.1.
L05424 expand/collapse EMBL AC list , L05407, L05408, L05410, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13624.1.
L05424 expand/collapse EMBL AC list , L05407, L05408, L05410, L05411, L05412, L05414, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13625.1.
L05424 expand/collapse EMBL AC list , L05407, L05408, L05410, L05411, L05412, L05414, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13626.1.
L05424 expand/collapse EMBL AC list , L05407, L05408, L05410, L05417, L05418, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13627.1.
L05424 expand/collapse EMBL AC list , L05407, L05408, L05410, L05411, L05412, L05414, L05415, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13628.1.
AJ251595 mRNA. Translation: CAB61878.1.
S66400 mRNA. Translation: AAB27917.1.
S66400 mRNA. Translation: AAB27918.2.
S66400 mRNA. Translation: AAB27919.1.
AF098641 mRNA. Translation: AAC70782.1.
U40373 mRNA. Translation: AAA82949.1.
AY101192 mRNA. Translation: AAM50040.1.
AY101193 mRNA. Translation: AAM50041.1.
EF581837 mRNA. Translation: ABQ59315.1.
FJ216964 mRNA. Translation: ACI46596.1.
AL832642 mRNA. Translation: CAD89965.1.
AL133330 Genomic DNA. Translation: CAC10347.1.
AL136989 Genomic DNA. No translation available.
AL356215 Genomic DNA. No translation available.
CH471064 Genomic DNA. Translation: EAW68147.1.
CH471064 Genomic DNA. Translation: EAW68148.1.
CH471064 Genomic DNA. Translation: EAW68149.1.
CH471064 Genomic DNA. Translation: EAW68151.1.
CH471064 Genomic DNA. Translation: EAW68152.1.
BC004372 mRNA. Translation: AAH04372.1.
BC067348 mRNA. Translation: AAH67348.1.
M25078 mRNA. Translation: AAA36138.1.
X55938 mRNA. Translation: CAA39404.1.
S72928 Genomic DNA. Translation: AAB30429.1.
X62739 mRNA. Translation: CAA44602.1.
PIRA47195.
I37369.
I77371.
I77372.
JH0417.
JH0518.
S13530.
S24222.
RefSeqNP_000601.3. NM_000610.3.
NP_001001389.1. NM_001001389.1.
NP_001001390.1. NM_001001390.1.
NP_001001391.1. NM_001001391.1.
NP_001001392.1. NM_001001392.1.
NP_001189484.1. NM_001202555.1.
NP_001189485.1. NM_001202556.1.
NP_001189486.1. NM_001202557.1.
UniGeneHs.502328.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1POZNMR-A20-178[»]
1UUHX-ray2.20A/B20-178[»]
2I83NMR-A20-178[»]
ProteinModelPortalP16070.
SMRP16070. Positions 20-178.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107398. 36 interactions.
DIPDIP-1121N.
IntActP16070. 15 interactions.
MINTMINT-5000740.

Chemistry

DrugBankDB00070. Hyaluronidase.

PTM databases

PhosphoSiteP16070.

Polymorphism databases

DMDM308153615.

2D gel databases

SWISS-2DPAGEP16070.

Proteomic databases

PaxDbP16070.
PRIDEP16070.

Protocols and materials databases

DNASU960.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263398; ENSP00000263398; ENSG00000026508. [P16070-12]
ENST00000278386; ENSP00000278386; ENSG00000026508. [P16070-19]
ENST00000352818; ENSP00000309732; ENSG00000026508. [P16070-18]
ENST00000360158; ENSP00000353280; ENSG00000026508. [P16070-14]
ENST00000415148; ENSP00000389830; ENSG00000026508. [P16070-4]
ENST00000428726; ENSP00000398632; ENSG00000026508. [P16070-1]
ENST00000433892; ENSP00000392331; ENSG00000026508. [P16070-10]
ENST00000434472; ENSP00000404447; ENSG00000026508. [P16070-11]
ENST00000437706; ENSP00000403990; ENSG00000026508. [P16070-8]
ENST00000449691; ENSP00000391008; ENSG00000026508. [P16070-6]
GeneID960.
KEGGhsa:960.
UCSCuc001mvu.3. human. [P16070-1]
uc001mvv.3. human. [P16070-4]
uc001mvw.3. human. [P16070-10]
uc001mvx.3. human. [P16070-12]
uc001mvy.3. human. [P16070-19]
uc001mwc.4. human. [P16070-11]
uc010rer.2. human. [P16070-18]
uc021qfw.1. human. [P16070-15]

Organism-specific databases

CTD960.
GeneCardsGC11P035116.
HGNCHGNC:1681. CD44.
HPACAB000112.
CAB000316.
HPA005785.
MIM107269. gene.
172290. gene.
609027. phenotype.
neXtProtNX_P16070.
PharmGKBPA26221.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41023.
HOVERGENHBG003850.
InParanoidP16070.
KOK06256.
OMASHPMGRG.
OrthoDBEOG77HDFT.
PhylomeDBP16070.
TreeFamTF334173.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP16070.
BgeeP16070.
GenevestigatorP16070.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR001231. CD44_antigen.
IPR000538. Link.
[Graphical view]
PfamPF00193. Xlink. 1 hit.
[Graphical view]
PRINTSPR00658. CD44.
PR01265. LINKMODULE.
SMARTSM00445. LINK. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCD44. human.
EvolutionaryTraceP16070.
GeneWikiCD44.
GenomeRNAi960.
NextBio4000.
PROP16070.
SOURCESearch...

Entry information

Entry nameCD44_HUMAN
AccessionPrimary (citable) accession number: P16070
Secondary accession number(s): A5YRN9 expand/collapse secondary AC list , B6EAT9, D3DR12, D3DR13, O95370, P22511, Q04858, Q13419, Q13957, Q13958, Q13959, Q13960, Q13961, Q13967, Q13968, Q13980, Q15861, Q16064, Q16065, Q16066, Q16208, Q16522, Q86T72, Q86Z27, Q8N694, Q92493, Q96J24, Q9H5A5, Q9UC28, Q9UC29, Q9UC30, Q9UCB0, Q9UJ36
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 178 of the entry and version 3 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

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries