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P16070

- CD44_HUMAN

UniProt

P16070 - CD44_HUMAN

Protein

CD44 antigen

Gene

CD44

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411HyaluronanBy similarity
    Binding sitei78 – 781HyaluronanBy similarity
    Binding sitei79 – 791HyaluronanBy similarity
    Binding sitei105 – 1051HyaluronanBy similarity

    GO - Molecular functioni

    1. collagen binding Source: UniProtKB
    2. hyaluronic acid binding Source: UniProtKB
    3. hyalurononglucosaminidase activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. branching involved in prostate gland morphogenesis Source: Ensembl
    3. branching involved in ureteric bud morphogenesis Source: Ensembl
    4. carbohydrate metabolic process Source: Reactome
    5. cartilage development Source: UniProtKB
    6. cell-matrix adhesion Source: UniProtKB
    7. cellular response to fibroblast growth factor stimulus Source: UniProtKB
    8. cytokine-mediated signaling pathway Source: Reactome
    9. extracellular matrix disassembly Source: Reactome
    10. extracellular matrix organization Source: Reactome
    11. glycosaminoglycan metabolic process Source: Reactome
    12. hyaluronan catabolic process Source: UniProtKB
    13. hyaluronan metabolic process Source: Reactome
    14. interferon-gamma-mediated signaling pathway Source: Reactome
    15. leukocyte migration Source: Reactome
    16. monocyte aggregation Source: UniProtKB
    17. negative regulation of apoptotic process Source: UniProtKB
    18. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    19. negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
    20. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: BHF-UCL
    21. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
    22. positive regulation of gene expression Source: Ensembl
    23. positive regulation of heterotypic cell-cell adhesion Source: UniProtKB
    24. positive regulation of monocyte aggregation Source: BHF-UCL
    25. positive regulation of peptidyl-serine phosphorylation Source: BHF-UCL
    26. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    27. single organismal cell-cell adhesion Source: UniProtKB
    28. small molecule metabolic process Source: Reactome
    29. Wnt signaling pathway Source: Ensembl
    30. wound healing involved in inflammatory response Source: Ensembl

    Keywords - Molecular functioni

    Blood group antigen, Receptor

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CD44
    Synonyms:LHR, MDU2, MDU3, MIC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1681. CD44.

    Subcellular locationi

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

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cell surface Source: UniProtKB
    3. cytoplasm Source: HPA
    4. external side of plasma membrane Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: HPA
    7. integral component of plasma membrane Source: UniProtKB
    8. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    MIMi609027. phenotype.
    PharmGKBiPA26221.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 742722CD44 antigenPRO_0000026687Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Pyrrolidone carboxylic acidCurated
    Glycosylationi25 – 251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi28 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi53 ↔ 118PROSITE-ProRule annotation
    Glycosylationi57 – 571N-linked (GlcNAc...)3 Publications
    Disulfide bondi77 ↔ 97PROSITE-ProRule annotation
    Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi110 – 1101N-linked (GlcNAc...)2 Publications
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi350 – 3501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi636 – 6361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi637 – 6371O-linked (GalNAc...); or Thr-6382 Publications
    Glycosylationi638 – 6381O-linked (GalNAc...); or Thr-6372 Publications
    Modified residuei672 – 6721Phosphoserine; by PKC1 Publication
    Modified residuei686 – 6861Phosphoserine2 Publications
    Modified residuei697 – 6971PhosphoserineBy similarity
    Modified residuei706 – 7061Phosphoserine6 Publications

    Post-translational modificationi

    Proteolytically cleaved in the extracellular matrix by specific proteinases (possibly MMPs) in several cell lines and tumors.1 Publication
    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-638.4 Publications
    Phosphorylated; activation of PKC results in the dephosphorylation of Ser-706 (constitutive phosphorylation site), and the phosphorylation of Ser-672.7 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Proteoglycan, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP16070.
    PaxDbiP16070.
    PRIDEiP16070.

    2D gel databases

    SWISS-2DPAGEP16070.

    PTM databases

    PhosphoSiteiP16070.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP16070.
    BgeeiP16070.
    GenevestigatoriP16070.

    Organism-specific databases

    HPAiCAB000112.
    CAB000316.
    HPA005785.

    Interactioni

    Subunit structurei

    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. Interacts with UNC119.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ipaBP180114EBI-490245,EBI-490239From a different organism.
    MSNP260386EBI-490245,EBI-528768
    SLC7A11Q9UPY54EBI-490245,EBI-3843348
    SPP1P104512EBI-490245,EBI-723648

    Protein-protein interaction databases

    BioGridi107398. 37 interactions.
    DIPiDIP-1121N.
    IntActiP16070. 16 interactions.
    MINTiMINT-5000740.

    Structurei

    Secondary structure

    1
    742
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 266
    Beta strandi33 – 386
    Helixi46 – 5510
    Beta strandi57 – 593
    Helixi63 – 708
    Turni71 – 733
    Beta strandi80 – 823
    Beta strandi85 – 928
    Helixi98 – 1003
    Beta strandi103 – 1064
    Beta strandi109 – 1113
    Beta strandi114 – 1196
    Beta strandi121 – 1233
    Beta strandi125 – 1284
    Beta strandi130 – 1323
    Beta strandi139 – 14810
    Turni150 – 1523
    Beta strandi154 – 1607
    Helixi165 – 1684

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1POZNMR-A20-178[»]
    1UUHX-ray2.20A/B20-178[»]
    2I83NMR-A21-178[»]
    ProteinModelPortaliP16070.
    SMRiP16070. Positions 20-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16070.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 649629ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini671 – 74272CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei650 – 67021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 12089LinkPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni224 – 649426StemAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi150 – 1589Arg/Lys-rich (basic)

    Domaini

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

    Sequence similaritiesi

    Contains 1 Link domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG41023.
    HOVERGENiHBG003850.
    InParanoidiP16070.
    KOiK06256.
    OMAiSHPMGRG.
    OrthoDBiEOG77HDFT.
    PhylomeDBiP16070.
    TreeFamiTF334173.

    Family and domain databases

    Gene3Di3.10.100.10. 1 hit.
    InterProiIPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR001231. CD44_antigen.
    IPR000538. Link.
    [Graphical view]
    PfamiPF00193. Xlink. 1 hit.
    [Graphical view]
    PRINTSiPR00658. CD44.
    PR01265. LINKMODULE.
    SMARTiSM00445. LINK. 1 hit.
    [Graphical view]
    SUPFAMiSSF56436. SSF56436. 1 hit.
    PROSITEiPS01241. LINK_1. 1 hit.
    PS50963. LINK_2. 1 hit.
    [Graphical view]

    Sequences (19)i

    Sequence statusi: Complete.

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

    This entry describes 19 isoformsi produced by alternative splicing. Align

    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.1 Publication

    Isoform 1 (identifier: P16070-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA    50
    DLCKAFNSTL PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN 100
    NTGVYILTSN TSQYDTYCFN ASAPPEEDCT SVTDLPNAFD GPITITIVNR 150
    DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS GSSSERSSTS GGYIFYTFST 200
    VHPIPDEDSP WITDSTDRIP ATTLMSTSAT ATETATKRQE TWDWFSWLFL 250
    PSESKNHLHT TTQMAGTSSN TISAGWEPNE ENEDERDRHL SFSGSGIDDD 300
    EDFISSTIST TPRAFDHTKQ NQDWTQWNPS HSNPEVLLQT TTRMTDVDRN 350
    GTTAYEGNWN PEAHPPLIHH EHHEEEETPH STSTIQATPS STTEETATQK 400
    EQWFGNRWHE GYRQTPKEDS HSTTGTAAAS AHTSHPMQGR TTPSPEDSSW 450
    TDFFNPISHP MGRGHQAGRR MDMDSSHSIT LQPTANPNTG LVEDLDRTGP 500
    LSMTTQQSNS QSFSTSHEGL EEDKDHPTTS TLTSSNRNDV TGGRRDPNHS 550
    EGSTTLLEGY TSHYPHTKES RTFIPVTSAK TGSFGVTAVT VGDSNSNVNR 600
    SLSGDQDTFH PSGGSHTTHG SESDGHSHGS QEGGANTTSG PIRTPQIPEW 650
    LIILASLLAL ALILAVCIAV NSRRRCGQKK KLVINSGNGA VEDRKPSGLN 700
    GEASKSQEMV HLVNKESSET PDQFMTADET RNLQNVDMKI GV 742

    Note: Corresponds to the largest isoform.

    Length:742
    Mass (Da):81,538
    Last modified:October 5, 2010 - v3
    Checksum:iBB9B66B19B970349
    GO
    Isoform 2 (identifier: P16070-2) [UniParc]FASTAAdd to Basket

    Also known as: CD44SP

    The sequence of this isoform differs from the canonical sequence as follows:
         23-29: DLNITCR → GVGRRKS
         30-742: Missing.

    Show »
    Length:29
    Mass (Da):3,327
    Checksum:iFD28FA0E33AB08B9
    GO
    Isoform 3 (identifier: P16070-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:711
    Mass (Da):77,983
    Checksum:iEF48BFB8E4478B97
    GO
    Isoform 4 (identifier: P16070-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:699
    Mass (Da):76,612
    Checksum:iCEC79496379F44FF
    GO
    Isoform 5 (identifier: P16070-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         266-273: Missing.

    Note: Alternative splice donor/acceptor on exon 7.

    Show »
    Length:734
    Mass (Da):80,790
    Checksum:i48D27AD91375BCDC
    GO
    Isoform 6 (identifier: P16070-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-385: I → T
         386-428: Missing.

    Note: Lacks exon 10.

    Show »
    Length:699
    Mass (Da):76,705
    Checksum:iA150D6FA11DAABD6
    GO
    Isoform 7 (identifier: P16070-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         506-506: Q → R
         507-535: Missing.

    Note: Lacks exon 13.

    Show »
    Length:713
    Mass (Da):78,446
    Checksum:i2C2098B56FF4F30E
    GO
    Isoform 8 (identifier: P16070-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         536-536: N → R
         537-604: Missing.

    Note: Lacks exon 14.

    Show »
    Length:674
    Mass (Da):74,388
    Checksum:i538CB559E671CF23
    GO
    Isoform 9 (identifier: P16070-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         675-675: R → S
         676-742: Missing.

    Note: Lacks exon 19.

    Show »
    Length:675
    Mass (Da):74,196
    Checksum:i3891F679BC733F89
    GO
    Isoform 10 (identifier: P16070-10) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:493
    Mass (Da):53,411
    Checksum:iA494CCC37F161EF2
    GO
    Isoform 11 (identifier: P16070-11) [UniParc]FASTAAdd to Basket

    Also known as: CD44R2

    The sequence of this isoform differs from the canonical sequence as follows:
         223-535: Missing.

    Note: Lacks exons 6-13.

    Show »
    Length:429
    Mass (Da):46,565
    Checksum:i557BD4FED59E0867
    GO
    Isoform 12 (identifier: P16070-12) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:361
    Mass (Da):39,416
    Checksum:iF51A746B442E0D33
    GO
    Isoform 13 (identifier: P16070-13) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:425
    Mass (Da):46,261
    Checksum:i47F544DD9890917B
    GO
    Isoform 14 (identifier: P16070-14) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:396
    Mass (Da):43,169
    Checksum:i5118DABF71C1F7D0
    GO
    Isoform 15 (identifier: P16070-15) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:294
    Mass (Da):32,075
    Checksum:iE11B9B38F4A74817
    GO
    Isoform 16 (identifier: P16070-16) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:668
    Mass (Da):73,150
    Checksum:iD719820A01C4517F
    GO
    Isoform 17 (identifier: P16070-17) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:691
    Mass (Da):75,957
    Checksum:i737967321EE8F579
    GO
    Isoform 18 (identifier: P16070-18) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:340
    Mass (Da):37,278
    Checksum:iC2E036A7DAB5717B
    GO
    Isoform 19 (identifier: P16070-19) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:139
    Mass (Da):15,635
    Checksum:i4A127F5C54BB7B62
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261I → M in AAA82949. 1 PublicationCurated
    Sequence conflicti109 – 1091S → Y in AAA35674. (PubMed:2466575)Curated
    Sequence conflicti109 – 1091S → Y in AAA51950. (PubMed:1840487)Curated
    Sequence conflicti109 – 1091S → Y in CAA38951. (PubMed:1991450)Curated
    Sequence conflicti109 – 1091S → Y in CAB61878. (PubMed:7508842)Curated
    Sequence conflicti221 – 2211A → R in CAA38951. (PubMed:1991450)Curated
    Sequence conflicti241 – 2411T → A in CAB61878. (PubMed:7508842)Curated
    Sequence conflicti410 – 4101E → V in CAA47271. (PubMed:1281868)Curated
    Sequence conflicti494 – 4941D → N in CAB61878. (PubMed:7508842)Curated
    Sequence conflicti555 – 5551T → H in CAA38951. (PubMed:1991450)Curated
    Sequence conflicti620 – 6201G → E in AAA35674. (PubMed:2466575)Curated
    Sequence conflicti697 – 6971S → I in AAM50041. 1 PublicationCurated
    Sequence conflicti697 – 6971S → I in AAH67348. 1 PublicationCurated

    Polymorphismi

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461R → P in In(A) antigen. 1 Publication
    VAR_006490
    Natural varianti393 – 3931T → M.
    Corresponds to variant rs11607491 [ dbSNP | Ensembl ].
    VAR_030325
    Natural varianti417 – 4171K → R.4 Publications
    Corresponds to variant rs9666607 [ dbSNP | Ensembl ].
    VAR_021147
    Natural varianti479 – 4791I → T.9 Publications
    Corresponds to variant rs1467558 [ dbSNP | Ensembl ].
    VAR_030326
    Natural varianti494 – 4941D → H.1 Publication
    Corresponds to variant rs12273397 [ dbSNP | Ensembl ].
    VAR_030327

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei23 – 297DLNITCR → GVGRRKS in isoform 2. 1 PublicationVSP_005303
    Alternative sequencei30 – 742713Missing in isoform 2. 1 PublicationVSP_005304Add
    BLAST
    Alternative sequencei78 – 13962RYGFI…LPNAF → SLHCSQQSKKVWAEEKASDQ QWQWSCGGQKAKWTQRRGQQ VSGNGAFGEQGVVRNSRPVY DS in isoform 19. 1 PublicationVSP_043870Add
    BLAST
    Alternative sequencei140 – 742603Missing in isoform 19. 1 PublicationVSP_043871Add
    BLAST
    Alternative sequencei192 – 1921G → A in isoform 3 and isoform 16. CuratedVSP_005305
    Alternative sequencei193 – 22331Missing in isoform 3 and isoform 16. CuratedVSP_005306Add
    BLAST
    Alternative sequencei223 – 535313Missing in isoform 11. 2 PublicationsVSP_022797Add
    BLAST
    Alternative sequencei223 – 2231T → N in isoform 10, isoform 13 and isoform 14. 5 PublicationsVSP_005309
    Alternative sequencei223 – 2231T → R in isoform 12, isoform 15 and isoform 18. 8 PublicationsVSP_005311
    Alternative sequencei223 – 2231T → S in isoform 4. 2 PublicationsVSP_005307
    Alternative sequencei224 – 604381Missing in isoform 12, isoform 15 and isoform 18. 8 PublicationsVSP_005312Add
    BLAST
    Alternative sequencei224 – 472249Missing in isoform 10, isoform 13 and isoform 14. 5 PublicationsVSP_005310Add
    BLAST
    Alternative sequencei224 – 26643Missing in isoform 4. 2 PublicationsVSP_005308Add
    BLAST
    Alternative sequencei266 – 2738Missing in isoform 5 and isoform 17. CuratedVSP_005313
    Alternative sequencei385 – 3851I → T in isoform 6, isoform 16 and isoform 17. CuratedVSP_005314
    Alternative sequencei386 – 42843Missing in isoform 6, isoform 16 and isoform 17. CuratedVSP_005315Add
    BLAST
    Alternative sequencei506 – 5061Q → R in isoform 7 and isoform 14. 1 PublicationVSP_005316
    Alternative sequencei507 – 53529Missing in isoform 7 and isoform 14. 1 PublicationVSP_005317Add
    BLAST
    Alternative sequencei536 – 5361N → R in isoform 8, isoform 13 and isoform 14. 1 PublicationVSP_005318
    Alternative sequencei537 – 60468Missing in isoform 8, isoform 13 and isoform 14. 1 PublicationVSP_005319Add
    BLAST
    Alternative sequencei605 – 62521Missing in isoform 18. 1 PublicationVSP_043575Add
    BLAST
    Alternative sequencei675 – 6751R → S in isoform 9 and isoform 15. 1 PublicationVSP_005320
    Alternative sequencei676 – 74267Missing in isoform 9 and isoform 15. 1 PublicationVSP_005321Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , L05407, L05408, L05409, L05410, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13622.1.
    L05423
    , L05407, L05408, L05410, L05411, L05412, L05414, L05415, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13623.1.
    L05424
    , L05407, L05408, L05410, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13624.1.
    L05424
    , L05407, L05408, L05410, L05411, L05412, L05414, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13625.1.
    L05424
    , L05407, L05408, L05410, L05411, L05412, L05414, L05416, L05417, L05418, L05419, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13626.1.
    L05424
    , L05407, L05408, L05410, L05417, L05418, L05420, L05421, L05422, M69215 Genomic DNA. Translation: AAB13627.1.
    L05424
    , 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.
    CCDSiCCDS31455.1. [P16070-4]
    CCDS31456.1. [P16070-10]
    CCDS31457.1. [P16070-12]
    CCDS31458.1. [P16070-19]
    CCDS55754.1. [P16070-11]
    CCDS55755.1. [P16070-18]
    CCDS7897.1. [P16070-1]
    PIRiA47195.
    I37369.
    I77371.
    I77372.
    JH0417.
    JH0518.
    S13530.
    S24222.
    RefSeqiNP_000601.3. NM_000610.3. [P16070-1]
    NP_001001389.1. NM_001001389.1. [P16070-4]
    NP_001001390.1. NM_001001390.1. [P16070-10]
    NP_001001391.1. NM_001001391.1. [P16070-12]
    NP_001001392.1. NM_001001392.1. [P16070-19]
    NP_001189484.1. NM_001202555.1. [P16070-11]
    NP_001189485.1. NM_001202556.1. [P16070-18]
    NP_001189486.1. NM_001202557.1. [P16070-15]
    UniGeneiHs.502328.

    Genome annotation databases

    EnsembliENST00000263398; ENSP00000263398; ENSG00000026508. [P16070-12]
    ENST00000278386; ENSP00000278386; ENSG00000026508. [P16070-19]
    ENST00000352818; ENSP00000309732; ENSG00000026508. [P16070-18]
    ENST00000415148; ENSP00000389830; ENSG00000026508. [P16070-4]
    ENST00000428726; ENSP00000398632; ENSG00000026508. [P16070-1]
    ENST00000433892; ENSP00000392331; ENSG00000026508. [P16070-10]
    ENST00000434472; ENSP00000404447; ENSG00000026508. [P16070-11]
    GeneIDi960.
    KEGGihsa:960.
    UCSCiuc001mvu.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]

    Polymorphism databases

    DMDMi308153615.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    dbRBC/BGMUT

    Blood group antigen gene mutation database

    Wikipedia

    CD44 entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , L05407 , L05408 , L05409 , L05410 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13622.1 .
    L05423
    , L05407 , L05408 , L05410 , L05411 , L05412 , L05414 , L05415 , L05416 , L05417 , L05418 , L05419 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13623.1 .
    L05424
    , L05407 , L05408 , L05410 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13624.1 .
    L05424
    , L05407 , L05408 , L05410 , L05411 , L05412 , L05414 , L05416 , L05417 , L05418 , L05419 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13625.1 .
    L05424
    , L05407 , L05408 , L05410 , L05411 , L05412 , L05414 , L05416 , L05417 , L05418 , L05419 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13626.1 .
    L05424
    , L05407 , L05408 , L05410 , L05417 , L05418 , L05420 , L05421 , L05422 , M69215 Genomic DNA. Translation: AAB13627.1 .
    L05424
    , 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 .
    CCDSi CCDS31455.1. [P16070-4 ]
    CCDS31456.1. [P16070-10 ]
    CCDS31457.1. [P16070-12 ]
    CCDS31458.1. [P16070-19 ]
    CCDS55754.1. [P16070-11 ]
    CCDS55755.1. [P16070-18 ]
    CCDS7897.1. [P16070-1 ]
    PIRi A47195.
    I37369.
    I77371.
    I77372.
    JH0417.
    JH0518.
    S13530.
    S24222.
    RefSeqi NP_000601.3. NM_000610.3. [P16070-1 ]
    NP_001001389.1. NM_001001389.1. [P16070-4 ]
    NP_001001390.1. NM_001001390.1. [P16070-10 ]
    NP_001001391.1. NM_001001391.1. [P16070-12 ]
    NP_001001392.1. NM_001001392.1. [P16070-19 ]
    NP_001189484.1. NM_001202555.1. [P16070-11 ]
    NP_001189485.1. NM_001202556.1. [P16070-18 ]
    NP_001189486.1. NM_001202557.1. [P16070-15 ]
    UniGenei Hs.502328.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1POZ NMR - A 20-178 [» ]
    1UUH X-ray 2.20 A/B 20-178 [» ]
    2I83 NMR - A 21-178 [» ]
    ProteinModelPortali P16070.
    SMRi P16070. Positions 20-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107398. 37 interactions.
    DIPi DIP-1121N.
    IntActi P16070. 16 interactions.
    MINTi MINT-5000740.

    Chemistry

    DrugBanki DB00070. Hyaluronidase.

    PTM databases

    PhosphoSitei P16070.

    Polymorphism databases

    DMDMi 308153615.

    2D gel databases

    SWISS-2DPAGE P16070.

    Proteomic databases

    MaxQBi P16070.
    PaxDbi P16070.
    PRIDEi P16070.

    Protocols and materials databases

    DNASUi 960.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263398 ; ENSP00000263398 ; ENSG00000026508 . [P16070-12 ]
    ENST00000278386 ; ENSP00000278386 ; ENSG00000026508 . [P16070-19 ]
    ENST00000352818 ; ENSP00000309732 ; ENSG00000026508 . [P16070-18 ]
    ENST00000415148 ; ENSP00000389830 ; ENSG00000026508 . [P16070-4 ]
    ENST00000428726 ; ENSP00000398632 ; ENSG00000026508 . [P16070-1 ]
    ENST00000433892 ; ENSP00000392331 ; ENSG00000026508 . [P16070-10 ]
    ENST00000434472 ; ENSP00000404447 ; ENSG00000026508 . [P16070-11 ]
    GeneIDi 960.
    KEGGi hsa:960.
    UCSCi uc001mvu.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

    CTDi 960.
    GeneCardsi GC11P035116.
    HGNCi HGNC:1681. CD44.
    HPAi CAB000112.
    CAB000316.
    HPA005785.
    MIMi 107269. gene.
    172290. gene.
    609027. phenotype.
    neXtProti NX_P16070.
    PharmGKBi PA26221.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41023.
    HOVERGENi HBG003850.
    InParanoidi P16070.
    KOi K06256.
    OMAi SHPMGRG.
    OrthoDBi EOG77HDFT.
    PhylomeDBi P16070.
    TreeFami TF334173.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_120996. Hyaluronan uptake and degradation.
    REACT_13552. Integrin cell surface interactions.
    REACT_25078. Interferon gamma signaling.

    Miscellaneous databases

    ChiTaRSi CD44. human.
    EvolutionaryTracei P16070.
    GeneWikii CD44.
    GenomeRNAii 960.
    NextBioi 4000.
    PROi P16070.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16070.
    Bgeei P16070.
    Genevestigatori P16070.

    Family and domain databases

    Gene3Di 3.10.100.10. 1 hit.
    InterProi IPR016186. C-type_lectin-like.
    IPR016187. C-type_lectin_fold.
    IPR001231. CD44_antigen.
    IPR000538. Link.
    [Graphical view ]
    Pfami PF00193. Xlink. 1 hit.
    [Graphical view ]
    PRINTSi PR00658. CD44.
    PR01265. LINKMODULE.
    SMARTi SM00445. LINK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56436. SSF56436. 1 hit.
    PROSITEi PS01241. LINK_1. 1 hit.
    PS50963. LINK_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12).
      Tissue: Spinal cord.
    15. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    16. 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. 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. "Unc119 protects from Shigella infection by inhibiting the Abl family kinases."
      Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.
      PLoS ONE 4:E5211-E5211(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UNC119.
    37. "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.
    38. "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.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "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.
    41. "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].
    42. "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.
    43. "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.
    44. "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.

    Entry informationi

    Entry nameiCD44_HUMAN
    AccessioniPrimary (citable) accession number: P16070
    Secondary accession number(s): A5YRN9
    , 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 historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 183 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Blood group antigen proteins
      Nomenclature of blood group antigens and list of entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3