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Protein

Cadherin-related family member 5

Gene

CDHR5

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

Functioni

Intermicrovillar adhesion molecule that forms, via its extracellular domain, calcium-dependent heterophilic complexes with CDHR2 on adjacent microvilli. Thereby, controls the packing of microvilli at the apical membrane of epithelial cells. Through its cytoplasmic domain, interacts with microvillus cytoplasmic proteins to form the intermicrovillar adhesion complex/IMAC. This complex plays a central role in microvilli and epithelial brush border differentiation.1 Publication

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • intermicrovillar adhesion Source: UniProtKB
  • regulation of microvillus length Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-related family member 5Curated
Alternative name(s):
Mu-protocadherinImported
Mucin and cadherin-like protein1 Publication
Mucin-like protocadherin1 Publication
Short name:
MLPCDH1 Publication
Gene namesi
Name:CDHR5Imported
Synonyms:MUCDHL1 Publication, MUPCDHImported
ORF Names:UNQ2781/PRO7168Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:7521. CDHR5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 669644ExtracellularSequence analysisAdd
BLAST
Transmembranei670 – 69021HelicalSequence analysisAdd
BLAST
Topological domaini691 – 845155CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • brush border membrane Source: UniProtKB
  • coated pit Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • microvillus membrane Source: UniProtKB
  • spanning component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091R → G: Loss of binding to CDHR2. 1 Publication
Mutagenesisi845 – 8451I → R: Loss of interaction with USH1C. 1 Publication

Organism-specific databases

PharmGKBiPA165543311.

Polymorphism and mutation databases

BioMutaiCDHR5.
DMDMi296439399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 845820Cadherin-related family member 5PRO_0000004012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Curated
Glycosylationi81 – 811N-linked (GlcNAc...)1 Publication
Glycosylationi140 – 1401N-linked (GlcNAc...)Curated
Glycosylationi198 – 1981N-linked (GlcNAc...)Curated
Glycosylationi297 – 2971N-linked (GlcNAc...)Curated
Glycosylationi308 – 3081N-linked (GlcNAc...)1 Publication
Glycosylationi405 – 4051N-linked (GlcNAc...)Curated
Glycosylationi526 – 5261N-linked (GlcNAc...)Curated
Modified residuei770 – 7701PhosphoserineBy similarity
Modified residuei810 – 8101PhosphothreonineCombined sources
Modified residuei817 – 8171PhosphoserineCombined sources
Modified residuei819 – 8191PhosphoserineCombined sources
Modified residuei821 – 8211PhosphoserineCombined sources

Post-translational modificationi

N- and O-glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9HBB8.
PaxDbiQ9HBB8.
PRIDEiQ9HBB8.

PTM databases

iPTMnetiQ9HBB8.
PhosphoSiteiQ9HBB8.

Expressioni

Tissue specificityi

Highest expression in kidney, liver, colon and small intestine. In kidney, expressed apically along brush border of proximal convoluted tubule but not in cortical collecting ducts. Isoform 1 is expressed primarily in adult small intestine and colon. Isoform 2 is highly expressed in fetal liver (PubMed:12167596). Expressed in duodenum with higher expression in enterocytes along the villus axis and lower expression in crypts (at protein level) (PubMed:24725409).2 Publications

Gene expression databases

BgeeiQ9HBB8.
CleanExiHS_MUPCDH.
ExpressionAtlasiQ9HBB8. baseline and differential.
GenevisibleiQ9HBB8. HS.

Organism-specific databases

HPAiCAB025004.
HPA009081.
HPA009173.

Interactioni

Subunit structurei

Part of the IMAC/intermicrovillar adhesion complex/intermicrovillar tip-link complex composed of ANKS4B, MYO7B, USH1C, CDHR2 and CDHR5 (PubMed:26812018). Interacts (via cytoplasmic domain) with USH1C and MYO7B; required for proper localization of CDHR5 to microvilli tips and its function in brush border differentiation (PubMed:24725409).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDHR2Q9BYE93EBI-9629917,EBI-493793
USH1CQ9Y6N9-12EBI-9540696,EBI-9541226

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119810. 10 interactions.
IntActiQ9HBB8. 3 interactions.
MINTiMINT-4999634.
STRINGi9606.ENSP00000351118.

Structurei

3D structure databases

ProteinModelPortaliQ9HBB8.
SMRiQ9HBB8. Positions 112-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini71 – 12454Cadherin 1PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini125 – 237113Cadherin 2PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini249 – 354106Cadherin 3PROSITE-ProRule annotationCuratedAdd
BLAST
Domaini355 – 459105Cadherin 4PROSITE-ProRule annotationCuratedAdd
BLAST
Repeati540 – 570311CuratedAdd
BLAST
Repeati571 – 601312CuratedAdd
BLAST
Repeati602 – 631303CuratedAdd
BLAST
Repeati632 – 645144; truncatedAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni540 – 6451064 X 31 AA approximate tandem repeatsAdd
BLAST
Regioni691 – 845155Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organization1 PublicationAdd
BLAST

Sequence similaritiesi

Contains 4 cadherin domains.PROSITE-ProRule annotationCurated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00390000001008.
HOVERGENiHBG052536.
InParanoidiQ9HBB8.
KOiK16505.
OMAiPMETERT.
OrthoDBiEOG7ZD1TQ.
PhylomeDBiQ9HBB8.
TreeFamiTF350567.

Family and domain databases

Gene3Di2.60.40.60. 4 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030326. Mucdhl.
[Graphical view]
PANTHERiPTHR24027:SF313. PTHR24027:SF313. 1 hit.
SMARTiSM00112. CA. 3 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 3 hits.
PROSITEiPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1Curated1 Publication (identifier: Q9HBB8-1) [UniParc]FASTAAdd to basket

Also known as: MUCDHL-FL1 Publication

, MLPCDH-L1 Publication

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

        10         20         30         40         50
MGSWALLWPP LLFTGLLVRP PGTMAQAQYC SVNKDIFEVE ENTNVTEPLV
60 70 80 90 100
DIHVPEGQEV TLGALSTPFA FRIQGNQLFL NVTPDYEEKS LLEAQLLCQS
110 120 130 140 150
GGTLVTQLRV FVSVLDVNDN APEFPFKTKE IRVEEDTKVN STVIPETQLQ
160 170 180 190 200
AEDRDKDDIL FYTLQEMTAG ASDYFSLVSV NRPALRLDRP LDFYERPNMT
210 220 230 240 250
FWLLVRDTPG ENVEPSHTAT ATLVLNVVPA DLRPPWFLPC TFSDGYVCIQ
260 270 280 290 300
AQYHGAVPTG HILPSPLVLR PGPIYAEDGD RGINQPIIYS IFRGNVNGTF
310 320 330 340 350
IIHPDSGNLT VARSVPSPMT FLLLVKGQQA DLARYSVTQV TVEAVAAAGS
360 370 380 390 400
PPRFPQRLYR GTVARGAGAG VVVKDAAAPS QPLRIQAQDP EFSDLNSAIT
410 420 430 440 450
YRITNHSHFR MEGEVVLTTT TLAQAGAFYA EVEAHNTVTS GTATTVIEIQ
460 470 480 490 500
VSEQEPPSTD VPPSPEAGGT TGPWTSTTSE VPRPPEPSQG PSTTSSGGGT
510 520 530 540 550
GPHPPSGTTL RPPTSSTPGG PPGAENSTSH QPATPGGDTA QTPKPGTSQP
560 570 580 590 600
MPPGVGTSTS HQPATPSGGT AQTPEPGTSQ PMPPSMGTST SHQPATPGGG
610 620 630 640 650
TAQTPEAGTS QPMPPGMGTS TSHQPTTPGG GTAQTPEPGT SQPMPLSKST
660 670 680 690 700
PSSGGGPSED KRFSVVDMAA LGGVLGALLL LALLGLAVLV HKHYGPRLKC
710 720 730 740 750
CCGKAPEPQP QGFDNQAFLP DHKANWAPVP SPTHDPKPAE APMPAEPAPP
760 770 780 790 800
GPASPGGAPE PPAAARAGGS PTAVRSILTK ERRPEGGYKA VWFGEDIGTE
810 820 830 840
ADVVVLNAPT LDVDGASDSG SGDEGEGAGR GGGPYDAPGG DDSYI
Length:845
Mass (Da):88,223
Last modified:May 18, 2010 - v3
Checksum:iFD872A8D67AF6677
GO
Isoform 2Curated (identifier: Q9HBB8-2) [UniParc]FASTAAdd to basket

Also known as: MLPCDH-S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     460-653: Missing.

Show »
Length:651
Mass (Da):69,626
Checksum:i51776E20917A7B04
GO
Isoform 3 (identifier: Q9HBB8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     460-465: Missing.

Note: No experimental confirmation available.
Show »
Length:839
Mass (Da):87,631
Checksum:i414CB816397F4386
GO

Sequence cautioni

The sequence AAG16730.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAG16732.1 differs from that shown.Aberrant splicing.Curated
The sequence BAA91021.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the N-terminal part.Curated
The sequence BAA91021.1 differs from that shown. Reason: Frameshift at position 763. Curated
The sequence BAA91021.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15052.1 differs from that shown. Reason: Frameshift at position 458. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131R → S in BAA91021 (PubMed:14702039).Curated
Sequence conflicti373 – 3731V → A in BAB15052 (PubMed:14702039).Curated
Sequence conflicti476 – 4761S → G in AAG33495 (Ref. 2) Curated
Sequence conflicti476 – 4761S → G in BAA91021 (PubMed:14702039).Curated
Sequence conflicti498 – 4981G → E in AAG33495 (Ref. 2) Curated
Sequence conflicti498 – 4981G → E in BAA91021 (PubMed:14702039).Curated
Sequence conflicti571 – 5711A → V in AAG16733 (PubMed:11031102).Curated
Sequence conflicti571 – 5711A → V in AAG33495 (Ref. 2) Curated
Sequence conflicti571 – 5711A → V in BAA91021 (PubMed:14702039).Curated
Sequence conflicti807 – 8071N → S in AAG30821 (Ref. 2) Curated
Sequence conflicti807 – 8071N → S in AAG33495 (Ref. 2) Curated
Sequence conflicti807 – 8071N → S in BAA91130 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651Q → P.1 Publication
Corresponds to variant rs2740374 [ dbSNP | Ensembl ].
VAR_060412
Natural varianti357 – 3571R → S.4 Publications
Corresponds to variant rs2246614 [ dbSNP | Ensembl ].
VAR_017920
Natural varianti389 – 3891D → N.
Corresponds to variant rs2306066 [ dbSNP | Ensembl ].
VAR_017921
Natural varianti521 – 5211P → S.3 Publications
Corresponds to variant rs2740375 [ dbSNP | Ensembl ].
VAR_060413
Natural varianti702 – 7021C → S.4 Publications
Corresponds to variant rs2740379 [ dbSNP | Ensembl ].
VAR_059192

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei460 – 653194Missing in isoform 2. 2 PublicationsVSP_050693Add
BLAST
Alternative sequencei460 – 4656Missing in isoform 3. 1 PublicationVSP_050692

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF258674 Genomic DNA. Translation: AAG16730.1. Sequence problems.
AF258674 Genomic DNA. Translation: AAG16731.1.
AF258675 mRNA. Translation: AAG16732.1. Sequence problems.
AF258676 mRNA. Translation: AAG16733.1.
AF276242 mRNA. Translation: AAG30821.1.
AF301909 mRNA. Translation: AAG33495.1.
AY358368 mRNA. Translation: AAQ88734.1.
AK000226 mRNA. Translation: BAA91021.1. Sequence problems.
AK000384 mRNA. Translation: BAA91130.1.
AK025012 mRNA. Translation: BAB15052.1. Frameshift.
AP006284 Genomic DNA. No translation available.
CCDSiCCDS7707.1. [Q9HBB8-1]
CCDS7708.1. [Q9HBB8-2]
RefSeqiNP_001165439.1. NM_001171968.1.
NP_068743.2. NM_021924.4.
NP_112554.2. NM_031264.3.
UniGeneiHs.165619.

Genome annotation databases

EnsembliENST00000349570; ENSP00000345726; ENSG00000099834. [Q9HBB8-2]
ENST00000358353; ENSP00000351118; ENSG00000099834. [Q9HBB8-1]
ENST00000397542; ENSP00000380676; ENSG00000099834. [Q9HBB8-1]
GeneIDi53841.
KEGGihsa:53841.
UCSCiuc001lqj.3. human. [Q9HBB8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

A tighter mesh - Issue 178 of April 2016

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF258674 Genomic DNA. Translation: AAG16730.1. Sequence problems.
AF258674 Genomic DNA. Translation: AAG16731.1.
AF258675 mRNA. Translation: AAG16732.1. Sequence problems.
AF258676 mRNA. Translation: AAG16733.1.
AF276242 mRNA. Translation: AAG30821.1.
AF301909 mRNA. Translation: AAG33495.1.
AY358368 mRNA. Translation: AAQ88734.1.
AK000226 mRNA. Translation: BAA91021.1. Sequence problems.
AK000384 mRNA. Translation: BAA91130.1.
AK025012 mRNA. Translation: BAB15052.1. Frameshift.
AP006284 Genomic DNA. No translation available.
CCDSiCCDS7707.1. [Q9HBB8-1]
CCDS7708.1. [Q9HBB8-2]
RefSeqiNP_001165439.1. NM_001171968.1.
NP_068743.2. NM_021924.4.
NP_112554.2. NM_031264.3.
UniGeneiHs.165619.

3D structure databases

ProteinModelPortaliQ9HBB8.
SMRiQ9HBB8. Positions 112-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119810. 10 interactions.
IntActiQ9HBB8. 3 interactions.
MINTiMINT-4999634.
STRINGi9606.ENSP00000351118.

PTM databases

iPTMnetiQ9HBB8.
PhosphoSiteiQ9HBB8.

Polymorphism and mutation databases

BioMutaiCDHR5.
DMDMi296439399.

Proteomic databases

MaxQBiQ9HBB8.
PaxDbiQ9HBB8.
PRIDEiQ9HBB8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000349570; ENSP00000345726; ENSG00000099834. [Q9HBB8-2]
ENST00000358353; ENSP00000351118; ENSG00000099834. [Q9HBB8-1]
ENST00000397542; ENSP00000380676; ENSG00000099834. [Q9HBB8-1]
GeneIDi53841.
KEGGihsa:53841.
UCSCiuc001lqj.3. human. [Q9HBB8-1]

Organism-specific databases

CTDi53841.
GeneCardsiCDHR5.
HGNCiHGNC:7521. CDHR5.
HPAiCAB025004.
HPA009081.
HPA009173.
MIMi606839. gene.
neXtProtiNX_Q9HBB8.
PharmGKBiPA165543311.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00390000001008.
HOVERGENiHBG052536.
InParanoidiQ9HBB8.
KOiK16505.
OMAiPMETERT.
OrthoDBiEOG7ZD1TQ.
PhylomeDBiQ9HBB8.
TreeFamiTF350567.

Miscellaneous databases

ChiTaRSiCDHR5. human.
GeneWikiiMUPCDH.
GenomeRNAii53841.
PROiQ9HBB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBB8.
CleanExiHS_MUPCDH.
ExpressionAtlasiQ9HBB8. baseline and differential.
GenevisibleiQ9HBB8. HS.

Family and domain databases

Gene3Di2.60.40.60. 4 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030326. Mucdhl.
[Graphical view]
PANTHERiPTHR24027:SF313. PTHR24027:SF313. 1 hit.
SMARTiSM00112. CA. 3 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 3 hits.
PROSITEiPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a 500-kb contig spanning the region between c-Ha-Ras and MUC2 on chromosome 11p15.5."
    Paris M.J., Williams B.R.G.
    Genomics 69:196-202(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS PRO-165; SER-357; SER-521 AND SER-702.
  2. "Cloning and characterization of human mu-protocadherin."
    Soleiman A., Krieger S., Haase A., Hantusch B.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS SER-357; SER-521 AND SER-702.
    Tissue: KidneyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANTS SER-357 AND SER-702.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS SER-357; SER-521 AND SER-702.
    Tissue: Colon mucosaImported and Ileal mucosaImported.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Identification and expression analysis of the human mu-protocadherin gene in fetal and adult kidneys."
    Goldberg M., Wei M., Tycko B., Falikovich I., Warburton D.
    Am. J. Physiol. 283:F454-F463(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "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-81 AND ASN-308.
    Tissue: Plasma.
  8. "Intestinal brush border assembly driven by protocadherin-based intermicrovillar adhesion."
    Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E., Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A., Kachar B., Tyska M.J.
    Cell 157:433-446(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH MYO7B AND USH1C, MUTAGENESIS OF ARG-109 AND ILE-845, REGION, TISSUE SPECIFICITY.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-810; SER-817; SER-819 AND SER-821, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "ANKS4B is essential for intermicrovillar adhesion complex formation."
    Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr., Tyska M.J.
    Dev. Cell 36:190-200(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF THE IMAC COMPLEX.

Entry informationi

Entry nameiCDHR5_HUMAN
AccessioniPrimary (citable) accession number: Q9HBB8
Secondary accession number(s): C9J7X1
, Q9H746, Q9HAU3, Q9HBB5, Q9HBB6, Q9HBB7, Q9NX86, Q9NXI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: May 18, 2010
Last modified: June 8, 2016
This is version 133 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.