P16070 (CD44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CD44
Synonyms:	LHR, MDU2, MDU3, MIC4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	742 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. 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.
Subunit structure	Interacts with PKN2 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.40
Subcellular location	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.38 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 process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Blood group antigen Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara branching involved in prostate gland morphogenesis Inferred from electronic annotation. Source: Compara branching involved in ureteric bud morphogenesis Inferred from electronic annotation. Source: Compara carbohydrate metabolic process Traceable author statement. Source: Reactome cartilage development Inferred from expression pattern PubMed 11944887. 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 hyaluronan catabolic process Inferred from direct assay PubMed 17170110. Source: UniProtKB interferon-gamma-mediated signaling pathway 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 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: Compara 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: Compara
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 17170110. Source: UniProtKB external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Non-traceable author statement Ref.3. Source: UniProtKB
Molecular_function	collagen 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
ipaB	P18011	4	EBI-490245,EBI-490239	From a different organism.
SLC7A11	Q9UPY5	4	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

By similarity

Chain

21 – 742

722

CD44 antigen

PRO_0000026687

Regions

Topological domain

21 – 649

629

Extracellular Potential

Transmembrane

650 – 670

21

Helical; Potential

Topological domain

671 – 742

72

Cytoplasmic Potential

Domain

32 – 120

89

Link

Region

224 – 649

426

Stem

Compositional bias

150 – 158

9

Arg/Lys-rich (basic)

Sites

Binding site

41

1

Hyaluronan By similarity

Binding site

78

1

Hyaluronan By similarity

Binding site

79

1

Hyaluronan By similarity

Binding site

105

1

Hyaluronan By similarity

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid Probable

Modified residue

672

1

Phosphoserine; by PKC Ref.27

Modified residue

686

1

Phosphoserine Ref.30 Ref.36

Modified residue

697

1

Phosphoserine By similarity

Modified residue

706

1

Phosphoserine Ref.26 Ref.30 Ref.31 Ref.32 Ref.36 Ref.39

Glycosylation

25

1

N-linked (GlcNAc...) Potential

Glycosylation

57

1

N-linked (GlcNAc...) Ref.29 Ref.34

Glycosylation

100

1

N-linked (GlcNAc...) Potential

Glycosylation

110

1

N-linked (GlcNAc...) Ref.34

Glycosylation

120

1

N-linked (GlcNAc...) Potential

Glycosylation

350

1

N-linked (GlcNAc...) Potential

Glycosylation

548

1

N-linked (GlcNAc...) Potential

Glycosylation

599

1

N-linked (GlcNAc...) Potential

Glycosylation

636

1

N-linked (GlcNAc...) Potential

Glycosylation

637

1

O-linked (GalNAc...); or Thr-638 Ref.38

Glycosylation

638

1

O-linked (GalNAc...); or Thr-637 Ref.38

Disulfide bond

28 ↔ 129

By similarity

Disulfide bond

53 ↔ 118

By similarity

Disulfide bond

77 ↔ 97

By similarity

Natural variations

Alternative sequence

23 – 29

7

DLNITCR → GVGRRKS in isoform 2.

VSP_005303

Alternative sequence

30 – 742

713

Missing in isoform 2.

VSP_005304

Alternative sequence

78 – 139

62

RYGFI…LPNAF → SLHCSQQSKKVWAEEKASDQ QWQWSCGGQKAKWTQRRGQQ VSGNGAFGEQGVVRNSRPVY DS in isoform 19.

VSP_043870

Alternative sequence

140 – 742

603

Missing in isoform 19.

VSP_043871

Alternative sequence

192

1

G → A in isoform 3 and isoform 16.

VSP_005305

Alternative sequence

193 – 223

31

Missing in isoform 3 and isoform 16.

VSP_005306

Alternative sequence

223 – 535

313

Missing in isoform 11.

VSP_022797

Alternative sequence

223

1

T → N in isoform 10, isoform 13 and isoform 14.

VSP_005309

Alternative sequence

223

1

T → R in isoform 12, isoform 15 and isoform 18.

VSP_005311

Alternative sequence

223

1

T → S in isoform 4.

VSP_005307

Alternative sequence

224 – 604

381

Missing in isoform 12, isoform 15 and isoform 18.

VSP_005312

Alternative sequence

224 – 472

249

Missing in isoform 10, isoform 13 and isoform 14.

VSP_005310

Alternative sequence

224 – 266

43

Missing in isoform 4.

VSP_005308

Alternative sequence

266 – 273

8

Missing in isoform 5 and isoform 17.

VSP_005313

Alternative sequence

385

1

I → T in isoform 6, isoform 16 and isoform 17.

VSP_005314

Alternative sequence

386 – 428

43

Missing in isoform 6, isoform 16 and isoform 17.

VSP_005315

Alternative sequence

506

1

Q → R in isoform 7 and isoform 14.

VSP_005316

Alternative sequence

507 – 535

29

Missing in isoform 7 and isoform 14.

VSP_005317

Alternative sequence

536

1

N → R in isoform 8, isoform 13 and isoform 14.

VSP_005318

Alternative sequence

537 – 604

68

Missing in isoform 8, isoform 13 and isoform 14.

VSP_005319

Alternative sequence

605 – 625

21

Missing in isoform 18.

VSP_043575

Alternative sequence

675

1

R → S in isoform 9 and isoform 15.

VSP_005320

Alternative sequence

676 – 742

67

Missing in isoform 9 and isoform 15.

VSP_005321

Natural variant

46

1

R → P in In(A) antigen. Ref.42

VAR_006490

Natural variant

393

1

T → M.
Corresponds to variant rs11607491 [ dbSNP | Ensembl ].

VAR_030325

Natural variant

417

1

K → R. Ref.6 Ref.7 Ref.17 Ref.24
Corresponds to variant rs9666607 [ dbSNP | Ensembl ].

VAR_021147

Natural variant

479

1

I → 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 variant

494

1

D → H. Ref.7
Corresponds to variant rs12273397 [ dbSNP | Ensembl ].

VAR_030327

Experimental info

Sequence conflict

26

1

I → M in AAA82949. Ref.10

Sequence conflict

109

1

S → Y in AAA35674. Ref.1

Sequence conflict

109

1

S → Y in AAA51950. Ref.2

Sequence conflict

109

1

S → Y in CAA38951. Ref.3

Sequence conflict

109

1

S → Y in CAB61878. Ref.7

Sequence conflict

221

1

A → R in CAA38951. Ref.3

Sequence conflict

241

1

T → A in CAB61878. Ref.7

Sequence conflict

410

1

E → V in CAA47271. Ref.5

Sequence conflict

494

1

D → N in CAB61878. Ref.7

Sequence conflict

555

1

T → H in CAA38951. Ref.3

Sequence conflict

620

1

G → E in AAA35674. Ref.1

Sequence conflict

697

1

S → I in AAM50041. Ref.11

Sequence conflict

697

1

S → I in AAH67348. Ref.16

Secondary structure

1

.

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742

Helix Strand Turn

Details...

Beta strand

21 – 26

6

Beta strand

33 – 38

6

Helix

46 – 55

10

Beta strand

57 – 59

3

Helix

63 – 70

8

Turn

71 – 73

3

Beta strand

80 – 82

3

Beta strand

85 – 92

8

Helix

98 – 100

3

Beta strand

103 – 106

4

Beta strand

109 – 111

3

Beta strand

114 – 119

6

Beta strand

121 – 123

3

Beta strand

125 – 128

4

Beta strand

130 – 132

3

Beta strand

139 – 148

10

Turn

150 – 152

3

Beta strand

154 – 160

7

Helix

165 – 168

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CD44) [UniParc]. Last modified October 5, 2010. Version 3. Checksum: BB9B66B19B970349	FASTA	742	81,538
	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
	Isoform 2 (CD44SP) [UniParc]. Checksum: FD28FA0E33AB08B9	FASTA	29	3,327
	10 20 MDKFWWHAAW GLCLVPLSLA QIGVGRRKS
	Isoform 3 [UniParc]. Checksum: EF48BFB8E4478B97	FASTA	711	77,983
	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 GALMSTSATA TETATKRQET WDWFSWLFLP SESKNHLHTT TQMAGTSSNT 250 260 270 280 290 300 ISAGWEPNEE NEDERDRHLS FSGSGIDDDE DFISSTISTT PRAFDHTKQN QDWTQWNPSH 310 320 330 340 350 360 SNPEVLLQTT TRMTDVDRNG TTAYEGNWNP EAHPPLIHHE HHEEEETPHS TSTIQATPSS 370 380 390 400 410 420 TTEETATQKE QWFGNRWHEG YRQTPKEDSH STTGTAAASA HTSHPMQGRT TPSPEDSSWT 430 440 450 460 470 480 DFFNPISHPM GRGHQAGRRM DMDSSHSITL QPTANPNTGL VEDLDRTGPL SMTTQQSNSQ 490 500 510 520 530 540 SFSTSHEGLE EDKDHPTTST LTSSNRNDVT GGRRDPNHSE GSTTLLEGYT SHYPHTKESR 550 560 570 580 590 600 TFIPVTSAKT GSFGVTAVTV GDSNSNVNRS LSGDQDTFHP SGGSHTTHGS ESDGHSHGSQ 610 620 630 640 650 660 EGGANTTSGP IRTPQIPEWL IILASLLALA LILAVCIAVN SRRRCGQKKK LVINSGNGAV 670 680 690 700 710 EDRKPSGLNG EASKSQEMVH LVNKESSETP DQFMTADETR NLQNVDMKIG V
	Isoform 4 (Epidermal) [UniParc]. Checksum: CEC79496379F44FF	FASTA	699	76,612
	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 ATSTSSNTIS AGWEPNEENE 250 260 270 280 290 300 DERDRHLSFS GSGIDDDEDF ISSTISTTPR AFDHTKQNQD WTQWNPSHSN PEVLLQTTTR 310 320 330 340 350 360 MTDVDRNGTT AYEGNWNPEA HPPLIHHEHH EEEETPHSTS TIQATPSSTT EETATQKEQW 370 380 390 400 410 420 FGNRWHEGYR QTPKEDSHST TGTAAASAHT SHPMQGRTTP SPEDSSWTDF FNPISHPMGR 430 440 450 460 470 480 GHQAGRRMDM DSSHSITLQP TANPNTGLVE DLDRTGPLSM TTQQSNSQSF STSHEGLEED 490 500 510 520 530 540 KDHPTTSTLT SSNRNDVTGG RRDPNHSEGS TTLLEGYTSH YPHTKESRTF IPVTSAKTGS 550 560 570 580 590 600 FGVTAVTVGD SNSNVNRSLS GDQDTFHPSG GSHTTHGSES DGHSHGSQEG GANTTSGPIR 610 620 630 640 650 660 TPQIPEWLII LASLLALALI LAVCIAVNSR RRCGQKKKLV INSGNGAVED RKPSGLNGEA 670 680 690 SKSQEMVHLV NKESSETPDQ FMTADETRNL QNVDMKIGV
	Isoform 5 [UniParc]. Checksum: 48D27AD91375BCDC	FASTA	734	80,790
	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 TTQMAAGWEP NEENEDERDR HLSFSGSGID DDEDFISSTI 310 320 330 340 350 360 STTPRAFDHT KQNQDWTQWN PSHSNPEVLL QTTTRMTDVD RNGTTAYEGN WNPEAHPPLI 370 380 390 400 410 420 HHEHHEEEET PHSTSTIQAT PSSTTEETAT QKEQWFGNRW HEGYRQTPKE DSHSTTGTAA 430 440 450 460 470 480 ASAHTSHPMQ GRTTPSPEDS SWTDFFNPIS HPMGRGHQAG RRMDMDSSHS ITLQPTANPN 490 500 510 520 530 540 TGLVEDLDRT GPLSMTTQQS NSQSFSTSHE GLEEDKDHPT TSTLTSSNRN DVTGGRRDPN 550 560 570 580 590 600 HSEGSTTLLE GYTSHYPHTK ESRTFIPVTS AKTGSFGVTA VTVGDSNSNV NRSLSGDQDT 610 620 630 640 650 660 FHPSGGSHTT HGSESDGHSH GSQEGGANTT SGPIRTPQIP EWLIILASLL ALALILAVCI 670 680 690 700 710 720 AVNSRRRCGQ KKKLVINSGN GAVEDRKPSG LNGEASKSQE MVHLVNKESS ETPDQFMTAD 730 ETRNLQNVDM KIGV
	Isoform 6 [UniParc]. Checksum: A150D6FA11DAABD6	FASTA	699	76,705
	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 STSTTASAHT SHPMQGRTTP SPEDSSWTDF FNPISHPMGR 430 440 450 460 470 480 GHQAGRRMDM DSSHSITLQP TANPNTGLVE DLDRTGPLSM TTQQSNSQSF STSHEGLEED 490 500 510 520 530 540 KDHPTTSTLT SSNRNDVTGG RRDPNHSEGS TTLLEGYTSH YPHTKESRTF IPVTSAKTGS 550 560 570 580 590 600 FGVTAVTVGD SNSNVNRSLS GDQDTFHPSG GSHTTHGSES DGHSHGSQEG GANTTSGPIR 610 620 630 640 650 660 TPQIPEWLII LASLLALALI LAVCIAVNSR RRCGQKKKLV INSGNGAVED RKPSGLNGEA 670 680 690 SKSQEMVHLV NKESSETPDQ FMTADETRNL QNVDMKIGV
	Isoform 7 [UniParc]. Checksum: 2C2098B56FF4F30E	FASTA	713	78,446
	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 LSMTTRNRND VTGGRRDPNH SEGSTTLLEG YTSHYPHTKE 550 560 570 580 590 600 SRTFIPVTSA KTGSFGVTAV TVGDSNSNVN RSLSGDQDTF HPSGGSHTTH GSESDGHSHG 610 620 630 640 650 660 SQEGGANTTS GPIRTPQIPE WLIILASLLA LALILAVCIA VNSRRRCGQK KKLVINSGNG 670 680 690 700 710 AVEDRKPSGL NGEASKSQEM VHLVNKESSE TPDQFMTADE TRNLQNVDMK IGV
	Isoform 8 [UniParc]. Checksum: 538CB559E671CF23	FASTA	674	74,388
	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 TLTSSRDQDT 550 560 570 580 590 600 FHPSGGSHTT HGSESDGHSH GSQEGGANTT SGPIRTPQIP EWLIILASLL ALALILAVCI 610 620 630 640 650 660 AVNSRRRCGQ KKKLVINSGN GAVEDRKPSG LNGEASKSQE MVHLVNKESS ETPDQFMTAD 670 ETRNLQNVDM KIGV
	Isoform 9 [UniParc]. Checksum: 3891F679BC733F89	FASTA	675	74,196
	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 ALILAVCIAV NSRRS
	Isoform 10 (CD44E) (CD44R1) (Epithelial) (Keratinocyte) [UniParc]. Checksum: A494CCC37F161EF2	FASTA	493	53,411
	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 ATNMDSSHSI TLQPTANPNT 250 260 270 280 290 300 GLVEDLDRTG PLSMTTQQSN SQSFSTSHEG LEEDKDHPTT STLTSSNRND VTGGRRDPNH 310 320 330 340 350 360 SEGSTTLLEG YTSHYPHTKE SRTFIPVTSA KTGSFGVTAV TVGDSNSNVN RSLSGDQDTF 370 380 390 400 410 420 HPSGGSHTTH GSESDGHSHG SQEGGANTTS GPIRTPQIPE WLIILASLLA LALILAVCIA 430 440 450 460 470 480 VNSRRRCGQK KKLVINSGNG AVEDRKPSGL NGEASKSQEM VHLVNKESSE TPDQFMTADE 490 TRNLQNVDMK IGV
	Isoform 11 (CD44R2) [UniParc]. Checksum: 557BD4FED59E0867	FASTA	429	46,565
	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 ATNRNDVTGG RRDPNHSEGS 250 260 270 280 290 300 TTLLEGYTSH YPHTKESRTF IPVTSAKTGS FGVTAVTVGD SNSNVNRSLS GDQDTFHPSG 310 320 330 340 350 360 GSHTTHGSES DGHSHGSQEG GANTTSGPIR TPQIPEWLII LASLLALALI LAVCIAVNSR 370 380 390 400 410 420 RRCGQKKKLV INSGNGAVED RKPSGLNGEA SKSQEMVHLV NKESSETPDQ FMTADETRNL QNVDMKIGV
	Isoform 12 (CDw44) (Reticulocyte) [UniParc]. Checksum: F51A746B442E0D33	FASTA	361	39,416
	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 ATRDQDTFHP SGGSHTTHGS 250 260 270 280 290 300 ESDGHSHGSQ EGGANTTSGP IRTPQIPEWL IILASLLALA LILAVCIAVN SRRRCGQKKK 310 320 330 340 350 360 LVINSGNGAV EDRKPSGLNG EASKSQEMVH LVNKESSETP DQFMTADETR NLQNVDMKIG V
	Isoform 13 (CD44R4) [UniParc]. Checksum: 47F544DD9890917B	FASTA	425	46,261
	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 ATNMDSSHSI TLQPTANPNT 250 260 270 280 290 300 GLVEDLDRTG PLSMTTQQSN SQSFSTSHEG LEEDKDHPTT STLTSSRDQD TFHPSGGSHT 310 320 330 340 350 360 THGSESDGHS HGSQEGGANT TSGPIRTPQI PEWLIILASL LALALILAVC IAVNSRRRCG 370 380 390 400 410 420 QKKKLVINSG NGAVEDRKPS GLNGEASKSQ EMVHLVNKES SETPDQFMTA DETRNLQNVD MKIGV
	Isoform 14 (CD44R5) [UniParc]. Checksum: 5118DABF71C1F7D0	FASTA	396	43,169
	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 ATNMDSSHSI TLQPTANPNT 250 260 270 280 290 300 GLVEDLDRTG PLSMTTRRDQ DTFHPSGGSH TTHGSESDGH SHGSQEGGAN TTSGPIRTPQ 310 320 330 340 350 360 IPEWLIILAS LLALALILAV CIAVNSRRRC GQKKKLVINS GNGAVEDRKP SGLNGEASKS 370 380 390 QEMVHLVNKE SSETPDQFMT ADETRNLQNV DMKIGV
	Isoform 15 (Hermes) [UniParc]. Checksum: E11B9B38F4A74817	FASTA	294	32,075
	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 ATRDQDTFHP SGGSHTTHGS 250 260 270 280 290 ESDGHSHGSQ EGGANTTSGP IRTPQIPEWL IILASLLALA LILAVCIAVN SRRS
	Isoform 16 [UniParc]. Checksum: D719820A01C4517F	FASTA	668	73,150
	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 GALMSTSATA TETATKRQET WDWFSWLFLP SESKNHLHTT TQMAGTSSNT 250 260 270 280 290 300 ISAGWEPNEE NEDERDRHLS FSGSGIDDDE DFISSTISTT PRAFDHTKQN QDWTQWNPSH 310 320 330 340 350 360 SNPEVLLQTT TRMTDVDRNG TTAYEGNWNP EAHPPLIHHE HHEEEETPHS TSTTASAHTS 370 380 390 400 410 420 HPMQGRTTPS PEDSSWTDFF NPISHPMGRG HQAGRRMDMD SSHSITLQPT ANPNTGLVED 430 440 450 460 470 480 LDRTGPLSMT TQQSNSQSFS TSHEGLEEDK DHPTTSTLTS SNRNDVTGGR RDPNHSEGST 490 500 510 520 530 540 TLLEGYTSHY PHTKESRTFI PVTSAKTGSF GVTAVTVGDS NSNVNRSLSG DQDTFHPSGG 550 560 570 580 590 600 SHTTHGSESD GHSHGSQEGG ANTTSGPIRT PQIPEWLIIL ASLLALALIL AVCIAVNSRR 610 620 630 640 650 660 RCGQKKKLVI NSGNGAVEDR KPSGLNGEAS KSQEMVHLVN KESSETPDQF MTADETRNLQ NVDMKIGV
	Isoform 17 [UniParc]. Checksum: 737967321EE8F579	FASTA	691	75,957
	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 TTQMAAGWEP NEENEDERDR HLSFSGSGID DDEDFISSTI 310 320 330 340 350 360 STTPRAFDHT KQNQDWTQWN PSHSNPEVLL QTTTRMTDVD RNGTTAYEGN WNPEAHPPLI 370 380 390 400 410 420 HHEHHEEEET PHSTSTTASA HTSHPMQGRT TPSPEDSSWT DFFNPISHPM GRGHQAGRRM 430 440 450 460 470 480 DMDSSHSITL QPTANPNTGL VEDLDRTGPL SMTTQQSNSQ SFSTSHEGLE EDKDHPTTST 490 500 510 520 530 540 LTSSNRNDVT GGRRDPNHSE GSTTLLEGYT SHYPHTKESR TFIPVTSAKT GSFGVTAVTV 550 560 570 580 590 600 GDSNSNVNRS LSGDQDTFHP SGGSHTTHGS ESDGHSHGSQ EGGANTTSGP IRTPQIPEWL 610 620 630 640 650 660 IILASLLALA LILAVCIAVN SRRRCGQKKK LVINSGNGAV EDRKPSGLNG EASKSQEMVH 670 680 690 LVNKESSETP DQFMTADETR NLQNVDMKIG V
	Isoform 18 [UniParc]. Checksum: C2E036A7DAB5717B	FASTA	340	37,278
	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 ATRHSHGSQE GGANTTSGPI 250 260 270 280 290 300 RTPQIPEWLI ILASLLALAL ILAVCIAVNS RRRCGQKKKL VINSGNGAVE DRKPSGLNGE 310 320 330 340 ASKSQEMVHL VNKESSETPD QFMTADETRN LQNVDMKIGV
	Isoform 19 (CD44RC) [UniParc]. Checksum: 4A127F5C54BB7B62	FASTA	139	15,635
	10 20 30 40 50 60 MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL 70 80 90 100 110 120 PTMAQMEKAL SIGFETCSLH CSQQSKKVWA EEKASDQQWQ WSCGGQKAKW TQRRGQQVSG 130 NGAFGEQGVV RNSRPVYDS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[31]	"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, MASS SPECTROMETRY. Tissue: T-cell.
[32]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[33]	"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.
[34]	"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, MASS SPECTROMETRY. Tissue: Liver.
[35]	"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.
[36]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"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].
[38]	"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, MASS SPECTROMETRY.
[39]	"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, MASS SPECTROMETRY.
[40]	"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.
[41]	"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.
[42]	"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

dbRBC/BGMUT

Blood group antigen gene mutation database

Wikipedia

CD44 entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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 , 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.

IPI

IPI00220678.
IPI00297160.
IPI00305064.
IPI00418465.
IPI00419219.
IPI00827555.
IPI00827650.
IPI00827795.
IPI00827893.
IPI00827937.
IPI00827982.
IPI00828056.
IPI00828064.
IPI00828108.
IPI00828192.
IPI00922478.
IPI00956122.
IPI00972926.
IPI00984539.

PIR

A47195.
I37369.
I77371.
I77372.
JH0417.
JH0518.
S13530.
S24222.

RefSeq

NP_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.

UniGene

Hs.502328.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1POZ	NMR	-	A	20-178	[»]
1UUH	X-ray	2.20	A/B	20-178	[»]
2I83	NMR	-	A	20-178	[»]

ProteinModelPortal

P16070.

SMR

P16070. Positions 20-178.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1121N.

IntAct

P16070. 14 interactions.

MINT

MINT-5000740.

PTM databases

PhosphoSite

P16070.

Polymorphism databases

DMDM

308153615.

2D gel databases

SWISS-2DPAGE

P16070.

Proteomic databases

PaxDb

P16070.

PRIDE

P16070.

Protocols and materials databases

DNASU

960.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263398; ENSP00000263398; ENSG00000026508.
ENST00000278386; ENSP00000278386; ENSG00000026508.
ENST00000352818; ENSP00000309732; ENSG00000026508.
ENST00000360158; ENSP00000353280; ENSG00000026508.
ENST00000415148; ENSP00000389830; ENSG00000026508.
ENST00000428726; ENSP00000398632; ENSG00000026508.
ENST00000433892; ENSP00000392331; ENSG00000026508.
ENST00000434472; ENSP00000404447; ENSG00000026508.
ENST00000437706; ENSP00000403990; ENSG00000026508.
ENST00000449691; ENSP00000391008; ENSG00000026508.

GeneID

960.

KEGG

hsa:960.

UCSC

uc001mvu.3. human.
uc001mvv.3. human.
uc001mvw.3. human.
uc001mvx.3. human.
uc001mvy.3. human.
uc001mwc.4. human.
uc010rer.2. human.
uc021qfw.1. human.

Organism-specific databases

CTD

960.

GeneCards

GC11P035116.

HGNC

HGNC:1681. CD44.

HPA

CAB000112.
CAB000316.
HPA005785.

MIM

107269. gene.
172290. gene.
609027. phenotype.

neXtProt

NX_P16070.

PharmGKB

PA26221.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41023.

HOVERGEN

HBG003850.

InParanoid

P16070.

KO

K06256.

OMA

EDCTSVT.

PhylomeDB

P16070.

Enzyme and pathway databases

Pathway_Interaction_DB

avb3_opn_pathway. Osteopontin-mediated events.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P16070.

Bgee

P16070.

Genevestigator

P16070.

GermOnline

ENSG00000026508. Homo sapiens.

Family and domain databases

Gene3D

3.10.100.10. 1 hit.

InterPro

IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR001231. CD44_antigen.
IPR000538. Link.
[Graphical view]

Pfam

PF00193. Xlink. 1 hit.
[Graphical view]

PRINTS

PR00658. CD44.
PR01265. LINKMODULE.

SMART

SM00445. LINK. 1 hit.
[Graphical view]

SUPFAM

SSF56436. C-type_lectin_fold. 1 hit.

PROSITE

PS01241. LINK_1. 1 hit.
PS50963. LINK_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CD44. human.

DrugBank

DB00070. Hyaluronidase.

EvolutionaryTrace

P16070.

GenomeRNAi

960.

NextBio

4000.

SOURCE

Search...

Entry information

Entry name

CD44_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	October 5, 2010
Last modified:	May 29, 2013
This is version 169 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.