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P55290

- CAD13_HUMAN

UniProt

P55290 - CAD13_HUMAN

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Protein
Cadherin-13
Gene
CDH13, CDHH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth.1 Publication

GO - Molecular functioni

  1. adiponectin binding Source: BHF-UCL
  2. cadherin binding Source: BHF-UCL
  3. calcium ion binding Source: InterPro
  4. lipoprotein particle binding Source: UniProtKB
  5. low-density lipoprotein particle binding Source: BHF-UCL

GO - Biological processi

  1. Rac protein signal transduction Source: BHF-UCL
  2. Rho protein signal transduction Source: BHF-UCL
  3. adherens junction organization Source: Reactome
  4. calcium-dependent cell-cell adhesion Source: BHF-UCL
  5. cell junction assembly Source: Reactome
  6. cell-cell junction organization Source: Reactome
  7. endothelial cell migration Source: BHF-UCL
  8. homophilic cell adhesion Source: BHF-UCL
  9. keratinocyte proliferation Source: BHF-UCL
  10. lamellipodium assembly Source: BHF-UCL
  11. localization within membrane Source: BHF-UCL
  12. low-density lipoprotein particle mediated signaling Source: BHF-UCL
  13. mitotic cell cycle Source: Ensembl
  14. negative regulation of cell adhesion Source: BHF-UCL
  15. negative regulation of cell proliferation Source: BHF-UCL
  16. positive regulation of calcium-mediated signaling Source: BHF-UCL
  17. positive regulation of cell migration Source: BHF-UCL
  18. positive regulation of cell-matrix adhesion Source: BHF-UCL
  19. positive regulation of endothelial cell proliferation Source: BHF-UCL
  20. positive regulation of positive chemotaxis Source: BHF-UCL
  21. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  22. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  23. regulation of cell growth Source: Ensembl
  24. regulation of endocytosis Source: BHF-UCL
  25. regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
  26. sprouting angiogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-13
Alternative name(s):
Heart cadherin
Short name:
H-cadherin
P105
Truncated cadherin
Short name:
T-cad
Short name:
T-cadherin
Gene namesi
Name:CDH13
Synonyms:CDHH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:1753. CDH13.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. caveola Source: BHF-UCL
  3. cytoplasm Source: BHF-UCL
  4. external side of plasma membrane Source: Ensembl
  5. extracellular space Source: BHF-UCL
  6. extracellular vesicular exosome Source: UniProt
  7. neuron projection Source: BHF-UCL
  8. perinuclear region of cytoplasm Source: Ensembl
  9. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26287.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 Reviewed prediction
Add
BLAST
Propeptidei23 – 138116
PRO_0000003793Add
BLAST
Chaini139 – 693555Cadherin-13
PRO_0000003794Add
BLAST
Propeptidei694 – 71320Removed in mature form Inferred
PRO_0000003795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi86 – 861N-linked (GlcNAc...)1 Publication
Glycosylationi382 – 3821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi500 – 5001N-linked (GlcNAc...)1 Publication
Glycosylationi530 – 5301N-linked (GlcNAc...)1 Publication
Glycosylationi598 – 5981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi638 – 6381N-linked (GlcNAc...)2 Publications
Glycosylationi671 – 6711N-linked (GlcNAc...) Reviewed prediction
Lipidationi693 – 6931GPI-anchor amidated glycine Inferred

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiP55290.
PaxDbiP55290.
PeptideAtlasiP55290.
PRIDEiP55290.

PTM databases

PhosphoSiteiP55290.

Expressioni

Tissue specificityi

Highly expressed in heart. In the CNS, expressed in cerebral cortex, medulla, hippocampus, amygdala, thalamus and substantia nigra. No expression detected in cerebellum or spinal cord.2 Publications

Developmental stagei

Expressed at higher levels in adult brain than in developing brain.1 Publication

Gene expression databases

ArrayExpressiP55290.
BgeeiP55290.
CleanExiHS_CDH13.
GenevestigatoriP55290.

Organism-specific databases

HPAiCAB025863.
HPA001380.

Interactioni

Subunit structurei

By contrast to classical cadherins, homodimerization in trans is not mediated by cadherin EC1 domain strand-swapping, but instead through a homophilic adhesive interface which joins two elongated EC1-EC2 domains through a region near their Ca2+-binding sites to form a tetrahedral, X-like shape By similarity.

Protein-protein interaction databases

BioGridi107447. 1 interaction.
IntActiP55290. 1 interaction.
MINTiMINT-7004770.
STRINGi9606.ENSP00000268613.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi145 – 1484
Beta strandi157 – 1615
Beta strandi163 – 1675
Beta strandi172 – 1787
Turni179 – 1813
Beta strandi182 – 1843
Beta strandi187 – 1904
Turni192 – 1943
Beta strandi196 – 1994
Turni205 – 2073
Beta strandi209 – 21810
Beta strandi224 – 23613
Beta strandi238 – 2414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V37NMR-A139-243[»]
ProteinModelPortaliP55290.
SMRiP55290. Positions 21-111, 139-680.

Miscellaneous databases

EvolutionaryTraceiP55290.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 245107Cadherin 1
Add
BLAST
Domaini246 – 363118Cadherin 2
Add
BLAST
Domaini364 – 477114Cadherin 3
Add
BLAST
Domaini478 – 585108Cadherin 4
Add
BLAST
Domaini584 – 694111Cadherin 5
Add
BLAST

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain By similarity.

Sequence similaritiesi

Contains 5 cadherin domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG304703.
HOGENOMiHOG000169079.
HOVERGENiHBG106438.
InParanoidiP55290.
KOiK06808.
OMAiTIATYQL.
OrthoDBiEOG7MH0XG.
PhylomeDBiP55290.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P55290-1) [UniParc]FASTAAdd to Basket

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

MQPRTPLVLC VLLSQVLLLT SAEDLDCTPG FQQKVFHINQ PAEFIEDQSI    50
LNLTFSDCKG NDKLRYEVSS PYFKVNSDGG LVALRNITAV GKTLFVHART 100
PHAEDMAELV IVGGKDIQGS LQDIFKFART SPVPRQKRSI VVSPILIPEN 150
QRQPFPRDVG KVVDSDRPER SKFRLTGKGV DQEPKGIFRI NENTGSVSVT 200
RTLDREVIAV YQLFVETTDV NGKTLEGPVP LEVIVIDQND NRPIFREGPY 250
IGHVMEGSPT GTTVMRMTAF DADDPATDNA LLRYNIRQQT PDKPSPNMFY 300
IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT 350
IMIDDKNDHS PKFTKKEFQA TVEEGAVGVI VNLTVEDKDD PTTGAWRAAY 400
TIINGNPGQS FEIHTNPQTN EGMLSVVKPL DYEISAFHTL LIKVENEDPL 450
VPDVSYGPSS TATVHITVLD VNEGPVFYPD PMMVTRQEDL SVGSVLLTVN 500
ATDPDSLQHQ TIRYSVYKDP AGWLNINPIN GTVDTTAVLD RESPFVDNSV 550
YTALFLAIDS GNPPATGTGT LLITLEDVND NAPFIYPTVA EVCDDAKNLS 600
VVILGASDKD LHPNTDPFKF EIHKQAVPDK VWKISKINNT HALVSLLQNL 650
NKANYNLPIM VTDSGKPPMT NITDLRVQVC SCRNSKVDCN AAGALRFSLP 700
SVLLLSLFSL ACL 713
Length:713
Mass (Da):78,287
Last modified:October 1, 1996 - v1
Checksum:iCEB662D77824CB60
GO
Isoform 2 (identifier: P55290-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-190: VVDSDRPERSKFRLTGKGVDQEPKGIFRI → RTHNPINSELLLNEGITADLNPCITILAI
     191-713: Missing.

Show »
Length:190
Mass (Da):21,058
Checksum:iC7DA89A2C0C036E9
GO
Isoform 3 (identifier: P55290-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     162-175: VVDSDRPERSKFRL → MKIWQVLCLARWLT
     176-713: Missing.

Show »
Length:175
Mass (Da):19,660
Checksum:i0038FABE744ECAE0
GO
Isoform 4 (identifier: P55290-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MQPRTPLVLCVLLS → MKTPPGASSRTKCSRELRSFCAFSCPRAKQPTCTAWFPQQEHPSENGPQMPGRDPPAASTM

Note: Gene prediction based on EST data.

Show »
Length:760
Mass (Da):83,397
Checksum:iB4BB30012F3D4560
GO
Isoform 5 (identifier: P55290-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-161: Missing.

Note: No experimental confirmation available.

Show »
Length:674
Mass (Da):73,787
Checksum:i4C15F7C62AE5B0AA
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651R → C in a patient with amyotrophic lateral sclerosis. 1 Publication
VAR_065747
Natural varianti103 – 1031A → V in a patient with amyotrophic lateral sclerosis. 1 Publication
VAR_065748
Natural varianti113 – 1131G → R in a patient with amyotrophic lateral sclerosis. 1 Publication
Corresponds to variant rs183971768 [ dbSNP | Ensembl ].
VAR_065749
Natural varianti121 – 1211L → S.
Corresponds to variant rs7197352 [ dbSNP | Ensembl ].
VAR_030632
Natural varianti246 – 2461R → W in a patient with amyotrophic lateral sclerosis. 1 Publication
VAR_065750
Natural varianti367 – 3671E → Q in a patient with amyotrophic lateral sclerosis. 1 Publication
VAR_065751
Natural varianti376 – 3761A → T.1 Publication
Corresponds to variant rs35549391 [ dbSNP | Ensembl ].
VAR_065752
Natural varianti643 – 6431L → R.1 Publication
Corresponds to variant rs34106627 [ dbSNP | Ensembl ].
VAR_065753

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1414MQPRT…CVLLS → MKTPPGASSRTKCSRELRSF CAFSCPRAKQPTCTAWFPQQ EHPSENGPQMPGRDPPAAST M in isoform 4.
VSP_046714Add
BLAST
Alternative sequencei123 – 16139Missing in isoform 5.
VSP_053739Add
BLAST
Alternative sequencei162 – 19029VVDSD…GIFRI → RTHNPINSELLLNEGITADL NPCITILAI in isoform 2.
VSP_042696Add
BLAST
Alternative sequencei162 – 17514VVDSD…SKFRL → MKIWQVLCLARWLT in isoform 3.
VSP_042794Add
BLAST
Alternative sequencei176 – 713538Missing in isoform 3.
VSP_042795Add
BLAST
Alternative sequencei191 – 713523Missing in isoform 2.
VSP_042697Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti199 – 1991V → M in AAH28624. 1 Publication
Sequence conflicti199 – 1991V → M in AAH30653. 1 Publication
Sequence conflicti288 – 2881Q → R in AAH28624. 1 Publication
Sequence conflicti288 – 2881Q → R in AAH30653. 1 Publication
Sequence conflicti392 – 3921T → A in AAH28624. 1 Publication
Sequence conflicti392 – 3921T → A in AAH30653. 1 Publication
Sequence conflicti544 – 5441P → T in AAH28624. 1 Publication
Sequence conflicti544 – 5441P → T in AAH30653. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34058 mRNA. Translation: AAA35624.1.
U59289 mRNA. Translation: AAB18912.1.
U59288 mRNA. Translation: AAB18911.1.
AB001103 Genomic DNA. Translation: BAA32411.1.
EU190357 mRNA. Translation: ABW97440.1.
EU190358 mRNA. Translation: ABW97441.1.
AK298612 mRNA. Translation: BAH12826.1.
AC009028 Genomic DNA. No translation available.
AC009063 Genomic DNA. No translation available.
AC009119 Genomic DNA. No translation available.
AC009142 Genomic DNA. No translation available.
AC087189 Genomic DNA. No translation available.
AC092340 Genomic DNA. No translation available.
AC092351 Genomic DNA. No translation available.
AC098804 Genomic DNA. No translation available.
AC099506 Genomic DNA. No translation available.
AC106814 Genomic DNA. No translation available.
AC125793 Genomic DNA. No translation available.
BC028624 mRNA. Translation: AAH28624.1.
BC030653 mRNA. Translation: AAH30653.1.
CCDSiCCDS56009.1. [P55290-3]
CCDS56010.1. [P55290-2]
CCDS58485.1. [P55290-4]
CCDS58486.1. [P55290-1]
CCDS58487.1. [P55290-5]
PIRiB38992.
RefSeqiNP_001207418.1. NM_001220489.1. [P55290-5]
NP_001207420.1. NM_001220491.1. [P55290-2]
NP_001207421.1. NM_001220492.1. [P55290-3]
NP_001248.1. NM_001257.4. [P55290-1]
UniGeneiHs.654386.
Hs.661776.

Genome annotation databases

EnsembliENST00000268613; ENSP00000268613; ENSG00000140945. [P55290-4]
ENST00000428848; ENSP00000394557; ENSG00000140945. [P55290-5]
ENST00000431540; ENSP00000408632; ENSG00000140945. [P55290-2]
ENST00000446376; ENSP00000388804; ENSG00000140945. [P55290-3]
ENST00000565636; ENSP00000456491; ENSG00000140945. [P55290-3]
ENST00000566620; ENSP00000454435; ENSG00000140945. [P55290-1]
GeneIDi1012.
KEGGihsa:1012.
UCSCiuc002fgx.3. human. [P55290-1]
uc010chh.3. human. [P55290-2]
uc021tlw.1. human. [P55290-3]

Polymorphism databases

DMDMi1705552.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L34058 mRNA. Translation: AAA35624.1 .
U59289 mRNA. Translation: AAB18912.1 .
U59288 mRNA. Translation: AAB18911.1 .
AB001103 Genomic DNA. Translation: BAA32411.1 .
EU190357 mRNA. Translation: ABW97440.1 .
EU190358 mRNA. Translation: ABW97441.1 .
AK298612 mRNA. Translation: BAH12826.1 .
AC009028 Genomic DNA. No translation available.
AC009063 Genomic DNA. No translation available.
AC009119 Genomic DNA. No translation available.
AC009142 Genomic DNA. No translation available.
AC087189 Genomic DNA. No translation available.
AC092340 Genomic DNA. No translation available.
AC092351 Genomic DNA. No translation available.
AC098804 Genomic DNA. No translation available.
AC099506 Genomic DNA. No translation available.
AC106814 Genomic DNA. No translation available.
AC125793 Genomic DNA. No translation available.
BC028624 mRNA. Translation: AAH28624.1 .
BC030653 mRNA. Translation: AAH30653.1 .
CCDSi CCDS56009.1. [P55290-3 ]
CCDS56010.1. [P55290-2 ]
CCDS58485.1. [P55290-4 ]
CCDS58486.1. [P55290-1 ]
CCDS58487.1. [P55290-5 ]
PIRi B38992.
RefSeqi NP_001207418.1. NM_001220489.1. [P55290-5 ]
NP_001207420.1. NM_001220491.1. [P55290-2 ]
NP_001207421.1. NM_001220492.1. [P55290-3 ]
NP_001248.1. NM_001257.4. [P55290-1 ]
UniGenei Hs.654386.
Hs.661776.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V37 NMR - A 139-243 [» ]
ProteinModelPortali P55290.
SMRi P55290. Positions 21-111, 139-680.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107447. 1 interaction.
IntActi P55290. 1 interaction.
MINTi MINT-7004770.
STRINGi 9606.ENSP00000268613.

PTM databases

PhosphoSitei P55290.

Polymorphism databases

DMDMi 1705552.

Proteomic databases

MaxQBi P55290.
PaxDbi P55290.
PeptideAtlasi P55290.
PRIDEi P55290.

Protocols and materials databases

DNASUi 1012.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268613 ; ENSP00000268613 ; ENSG00000140945 . [P55290-4 ]
ENST00000428848 ; ENSP00000394557 ; ENSG00000140945 . [P55290-5 ]
ENST00000431540 ; ENSP00000408632 ; ENSG00000140945 . [P55290-2 ]
ENST00000446376 ; ENSP00000388804 ; ENSG00000140945 . [P55290-3 ]
ENST00000565636 ; ENSP00000456491 ; ENSG00000140945 . [P55290-3 ]
ENST00000566620 ; ENSP00000454435 ; ENSG00000140945 . [P55290-1 ]
GeneIDi 1012.
KEGGi hsa:1012.
UCSCi uc002fgx.3. human. [P55290-1 ]
uc010chh.3. human. [P55290-2 ]
uc021tlw.1. human. [P55290-3 ]

Organism-specific databases

CTDi 1012.
GeneCardsi GC16P082660.
HGNCi HGNC:1753. CDH13.
HPAi CAB025863.
HPA001380.
MIMi 601364. gene.
neXtProti NX_P55290.
PharmGKBi PA26287.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304703.
HOGENOMi HOG000169079.
HOVERGENi HBG106438.
InParanoidi P55290.
KOi K06808.
OMAi TIATYQL.
OrthoDBi EOG7MH0XG.
PhylomeDBi P55290.

Enzyme and pathway databases

Reactomei REACT_19195. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSi CDH13. human.
EvolutionaryTracei P55290.
GeneWikii T-cadherin.
GenomeRNAii 1012.
NextBioi 35534829.
PROi P55290.
SOURCEi Search...

Gene expression databases

ArrayExpressi P55290.
Bgeei P55290.
CleanExi HS_CDH13.
Genevestigatori P55290.

Family and domain databases

Gene3Di 2.60.40.60. 6 hits.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR014868. Cadherin_pro_dom.
[Graphical view ]
Pfami PF00028. Cadherin. 5 hits.
PF08758. Cadherin_pro. 1 hit.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 6 hits.
PROSITEi PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin."
    Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.
    Cell Adhes. Commun. 2:15-26(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "H-cadherin, a novel cadherin with growth inhibitory functions and diminished expression in human breast cancer."
    Lee S.W.
    Nat. Med. 2:776-782(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. "The H-cadherin (CDH13) gene is inactivated in human lung cancer."
    Sato M., Mori Y., Sakurada A., Fujimura S., Horii A.
    Hum. Genet. 103:96-101(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Differential alternative splicing of Cadherin 13 gene in aging and Alzheimer's disease."
    Liu Q.-R., Liu J.J., Zhu X.-G., Uhl G.R.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  6. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Brain and Testis.
  8. "Identification of an atypical lipoprotein-binding protein from human aortic smooth muscle as T-cadherin."
    Tkachuk V.A., Bochkov V.N., Philippova M.P., Stambolsky D.V., Kuzmenko E.S., Sidorova M.V., Molokoedov A.S., Spirov V.G., Resink T.J.
    FEBS Lett. 421:208-212(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 140-149; 162-169 AND 284-287 (ISOFORM 1).
    Tissue: Aorta.
  9. "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its characteristics as a negative growth regulator of epidermal growth factor in neuroblastoma cells."
    Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N., Sonobe H., Ohtsuki Y.
    J. Neurochem. 74:1489-1497(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Brain.
  10. "The glycosyl phosphatidylinositol anchor of human T-cadherin binds lipoproteins."
    Niermann T., Kern F., Erne P., Resink T.
    Biochem. Biophys. Res. Commun. 276:1240-1247(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  11. "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-86; ASN-500 AND ASN-638.
    Tissue: Plasma.
  12. "Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."
    Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., Brodbeck U., Peck S.C., Jensen O.N.
    J. Proteome Res. 5:935-943(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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-530 AND ASN-638.
    Tissue: Liver.
  14. "Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis."
    Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A.
    Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CYS-65; VAL-103; ARG-113; TRP-246; GLN-367; THR-376 AND ARG-643.

Entry informationi

Entry nameiCAD13_HUMAN
AccessioniPrimary (citable) accession number: P55290
Secondary accession number(s): A8W476
, A8W477, B7Z590, C9JRI6, J3KN62, Q6GTW4, Q8TBX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 141 of the entry and version 1 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. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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