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Protein

Cadherin-related family member 2

Gene

CDHR2

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 CDHR5 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 (PubMed:24725409). May also play a role in cell-cell adhesion and contact inhibition in epithelial cells (PubMed:12117771).2 Publications

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • cell adhesion molecule binding Source: UniProtKB

GO - Biological processi

  • cell-cell adhesion mediated by cadherin Source: UniProtKB
  • epithelial cell differentiation Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • intermicrovillar adhesion Source: UniProtKB
  • negative regulation of cell growth involved in contact inhibition Source: UniProtKB
  • regulation of microvillus length Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Differentiation

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-related family member 2Curated
Alternative name(s):
Protocadherin LKC1 Publication
Short name:
PC-LKC1 Publication
Protocadherin-241 Publication
Gene namesi
Name:CDHR2Imported
Synonyms:PCDH241 Publication, PCLKC1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:18231. CDHR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 11541134ExtracellularSequence analysisAdd
BLAST
Transmembranei1155 – 117521HelicalSequence analysisAdd
BLAST
Topological domaini1176 – 1310135CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB
  • brush border Source: UniProtKB
  • brush border membrane Source: UniProtKB
  • cell junction Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • microvillus membrane Source: UniProtKB
  • spanning component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1310 – 13101L → R: Loss of interaction with USH1C. 1 Publication

Organism-specific databases

PharmGKBiPA165660231.

Polymorphism and mutation databases

BioMutaiCDHR2.
DMDMi209572658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 13101290Cadherin-related family member 2PRO_0000004011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence analysis
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence analysis
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence analysis
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence analysis
Glycosylationi565 – 5651N-linked (GlcNAc...)Sequence analysis
Glycosylationi600 – 6001N-linked (GlcNAc...)Sequence analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence analysis
Glycosylationi632 – 6321N-linked (GlcNAc...)Sequence analysis
Glycosylationi680 – 6801N-linked (GlcNAc...)Sequence analysis
Glycosylationi696 – 6961N-linked (GlcNAc...)Sequence analysis
Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence analysis
Glycosylationi775 – 7751N-linked (GlcNAc...)Sequence analysis
Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence analysis
Glycosylationi871 – 8711N-linked (GlcNAc...)Sequence analysis
Glycosylationi877 – 8771N-linked (GlcNAc...)Sequence analysis
Glycosylationi911 – 9111N-linked (GlcNAc...)Sequence analysis
Glycosylationi932 – 9321N-linked (GlcNAc...)Sequence analysis
Glycosylationi1107 – 11071N-linked (GlcNAc...)Sequence analysis
Modified residuei1248 – 12481PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9BYE9.
PaxDbiQ9BYE9.
PRIDEiQ9BYE9.

PTM databases

iPTMnetiQ9BYE9.
PhosphoSiteiQ9BYE9.

Expressioni

Tissue specificityi

Highly expressed in liver, kidney and colon. Moderately expressed in small intestine. Down-regulated in a number of liver and colon cancers (PubMed:12117771, PubMed:15534908). Expressed in duodenum with higher expression in enterocytes along the villus axis and lower expression in crypts (at protein level) (PubMed:24725409).3 Publications

Gene expression databases

BgeeiQ9BYE9.
CleanExiHS_PCDH24.
ExpressionAtlasiQ9BYE9. baseline and differential.
GenevisibleiQ9BYE9. HS.

Organism-specific databases

HPAiHPA012569.
HPA017053.

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 with MAST2 (PubMed:12117771). Interacts (via cytoplasmic domain) with USH1C and MYO7B; required for proper localization of CDHR2 to microvilli tips and its function in brush border differentiation (PubMed:24725409, PubMed:26812017).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDHR5Q9HBB8-13EBI-493793,EBI-9540729
CDHR5Q9HBB8-23EBI-493793,EBI-9629917
MAST2Q6P0Q84EBI-493793,EBI-493777
MYO7BQ6PIF63EBI-493793,EBI-4400912
USH1CQ9Y6N9-12EBI-493793,EBI-9541226

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120179. 1 interaction.
IntActiQ9BYE9. 4 interactions.
STRINGi9606.ENSP00000261944.

Structurei

3D structure databases

ProteinModelPortaliQ9BYE9.
SMRiQ9BYE9. Positions 31-1044.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 12498Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 241117Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini242 – 353112Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini368 – 480113Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 586106Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini586 – 695110Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini696 – 808113Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini810 – 928119Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini930 – 1058129Cadherin 9PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1180 – 1310131Mediates interaction with USH1C and MYO7B and is required for proper localization to microvilli tips and function in microvilli organization1 PublicationAdd
BLAST

Domaini

The cadherin 1 domain is required for binding to CDHR5.1 Publication

Sequence similaritiesi

Contains 9 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00840000129706.
HOGENOMiHOG000115467.
HOVERGENiHBG053524.
InParanoidiQ9BYE9.
KOiK16502.
OMAiCSLPACT.
OrthoDBiEOG712TVF.
PhylomeDBiQ9BYE9.
TreeFamiTF332908.

Family and domain databases

Gene3Di2.60.40.60. 9 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030276. CDHR2.
[Graphical view]
PANTHERiPTHR24027:SF312. PTHR24027:SF312. 3 hits.
PfamiPF00028. Cadherin. 6 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 9 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 9 hits.
PROSITEiPS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BYE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQLWLSCFL LPALVVSVAA NVAPKFLANM TSVILPEDLP VGAQAFWLVA
60 70 80 90 100
EDQDNDPLTY GMSGPNAYFF AVTPKTGEVK LASALDYETL YTFKVTISVS
110 120 130 140 150
DPYIQVQREM LVIVEDRNDN APVFQNTAFS TSINETLPVG SVVFSVLAVD
160 170 180 190 200
KDMGSAGMVV YSIEKVIPST GDSEHLFRIL ANGSIVLNGS LSYNNKSAFY
210 220 230 240 250
QLELKACDLG GMYHNTFTIQ CSLPVFLSIS VVDQPDLDPQ FVREFYSASV
260 270 280 290 300
AEDAAKGTSV LTVEAVDGDK GINDPVIYSI SYSTRPGWFD IGADGVIRVN
310 320 330 340 350
GSLDREQLLE ADEEVQLQVT ATETHLNIYG QEAKVSIWVT VRVMDVNDHK
360 370 380 390 400
PEFYNCSLPA CTFTPEEAQV NFTGYVDEHA SPRIPIDDLT MVVYDPDKGS
410 420 430 440 450
NGTFLLSLGG PDAEAFSVSP ERAVGSASVQ VLVRVSALVD YERQTAMAVQ
460 470 480 490 500
VVATDSVSQN FSVAMVTIHL RDINDHRPTF PQSLYVLTVP EHSATGSVVT
510 520 530 540 550
DSIHATDPDT GAWGQITYSL LPGNGADLFQ VDPVSGTVTV RNGELLDRES
560 570 580 590 600
QAVYYLTLQA TDGGNLSSST TLQIHLLDIN DNAPVVSGSY NIFVQEEEGN
610 620 630 640 650
VSVTIQAHDN DEPGTNNSRL LFNLLPGPYS HNFSLDPDTG LLRNLGPLDR
660 670 680 690 700
EAIDPALEGR IVLTVLVSDC GEPVLGTKVN VTITVEDIND NLPIFNQSSY
710 720 730 740 750
NFTVKEEDPG VLVGVVKAWD ADQTEANNRI SFSLSGSGAN YFMIRGLVLG
760 770 780 790 800
AGWAEGYLRL PPDVSLDYET QPVFNLTVSA ENPDPQGGET IVDVCVNVKD
810 820 830 840 850
VNDNPPTLDV ASLRGIRVAE NGSQHGQVAV VVASDVDTSA QLEIQLVNIL
860 870 880 890 900
CTKAGVDVGS LCWGWFSVAA NGSVYINQSK AIDYEACDLV TLVVRACDLA
910 920 930 940 950
TDPGFQAYSN NGSLLITIED VNDNAPYFLP ENKTFVIIPE LVLPNREVAS
960 970 980 990 1000
VRARDDDSGN NGVILFSILR VDFISKDGAT IPFQGVFSIF TSSEADVFAG
1010 1020 1030 1040 1050
SIQPVTSLDS TLQGTYQVTV QARDRPSLGP FLEATTTLNL FTVDQSYRSR
1060 1070 1080 1090 1100
LQFSTPKEEV GANRQAINAA LTQATRTTVY IVDIQDIDSA ARARPHSYLD
1110 1120 1130 1140 1150
AYFVFPNGSA LTLDELSVMI RNDQDSLTQL LQLGLVVLGS QESQESDLSK
1160 1170 1180 1190 1200
QLISVIIGLG VALLLVLVIM TMAFVCVRKS YNRKLQAMKA AKEARKTAAG
1210 1220 1230 1240 1250
VMPSAPAIPG TNMYNTERAN PMLNLPNKDL GLEYLSPSND LDSVSVNSLD
1260 1270 1280 1290 1300
DNSVDVDKNS QEIKEHRPPH TPPEPDPEPL SVVLLGRQAG ASGQLEGPSY
1310
TNAGLDTTDL
Length:1,310
Mass (Da):141,543
Last modified:October 14, 2008 - v2
Checksum:iE0BC8AEEF8D9E1F2
GO

Sequence cautioni

The sequence BAA90962.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641G → S in BAB40777 (PubMed:12117771).Curated
Sequence conflicti1229 – 12291D → G in BAA90962 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071Q → H.
Corresponds to variant rs6886860 [ dbSNP | Ensembl ].
VAR_046695
Natural varianti415 – 4151A → G.
Corresponds to variant rs3762960 [ dbSNP | Ensembl ].
VAR_046696
Natural varianti424 – 4241V → A.3 Publications
Corresponds to variant rs11134982 [ dbSNP | Ensembl ].
VAR_046697
Natural varianti766 – 7661L → P.
Corresponds to variant rs752138 [ dbSNP | Ensembl ].
VAR_046698
Natural varianti901 – 9011T → M.
Corresponds to variant rs35018750 [ dbSNP | Ensembl ].
VAR_046699
Natural varianti948 – 9481V → M.
Corresponds to variant rs3749625 [ dbSNP | Ensembl ].
VAR_046700
Natural varianti1004 – 10041P → L Found in an acute myeloid leukemia sample; somatic mutation. 1 Publication
VAR_054148
Natural varianti1128 – 11281T → M.3 Publications
Corresponds to variant rs2291442 [ dbSNP | Ensembl ].
VAR_046701
Natural varianti1164 – 11641L → M.1 Publication
Corresponds to variant rs17078347 [ dbSNP | Ensembl ].
VAR_021548

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047004 mRNA. Translation: BAB40777.1.
AK000131 mRNA. Translation: BAA90962.1. Different initiation.
AK315055 mRNA. Translation: BAG37531.1.
AC091934 Genomic DNA. No translation available.
BC130282 mRNA. Translation: AAI30283.1.
CCDSiCCDS34297.1.
RefSeqiNP_001165447.1. NM_001171976.1.
NP_060145.3. NM_017675.4.
UniGeneiHs.4205.

Genome annotation databases

EnsembliENST00000261944; ENSP00000261944; ENSG00000074276.
ENST00000506348; ENSP00000421078; ENSG00000074276.
ENST00000510636; ENSP00000424565; ENSG00000074276.
GeneIDi54825.
KEGGihsa:54825.
UCSCiuc003mem.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB047004 mRNA. Translation: BAB40777.1.
AK000131 mRNA. Translation: BAA90962.1. Different initiation.
AK315055 mRNA. Translation: BAG37531.1.
AC091934 Genomic DNA. No translation available.
BC130282 mRNA. Translation: AAI30283.1.
CCDSiCCDS34297.1.
RefSeqiNP_001165447.1. NM_001171976.1.
NP_060145.3. NM_017675.4.
UniGeneiHs.4205.

3D structure databases

ProteinModelPortaliQ9BYE9.
SMRiQ9BYE9. Positions 31-1044.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120179. 1 interaction.
IntActiQ9BYE9. 4 interactions.
STRINGi9606.ENSP00000261944.

PTM databases

iPTMnetiQ9BYE9.
PhosphoSiteiQ9BYE9.

Polymorphism and mutation databases

BioMutaiCDHR2.
DMDMi209572658.

Proteomic databases

MaxQBiQ9BYE9.
PaxDbiQ9BYE9.
PRIDEiQ9BYE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261944; ENSP00000261944; ENSG00000074276.
ENST00000506348; ENSP00000421078; ENSG00000074276.
ENST00000510636; ENSP00000424565; ENSG00000074276.
GeneIDi54825.
KEGGihsa:54825.
UCSCiuc003mem.3. human.

Organism-specific databases

CTDi54825.
GeneCardsiCDHR2.
HGNCiHGNC:18231. CDHR2.
HPAiHPA012569.
HPA017053.
neXtProtiNX_Q9BYE9.
PharmGKBiPA165660231.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00840000129706.
HOGENOMiHOG000115467.
HOVERGENiHBG053524.
InParanoidiQ9BYE9.
KOiK16502.
OMAiCSLPACT.
OrthoDBiEOG712TVF.
PhylomeDBiQ9BYE9.
TreeFamiTF332908.

Miscellaneous databases

GeneWikiiPCLKC.
GenomeRNAii54825.
NextBioi57585.
PROiQ9BYE9.

Gene expression databases

BgeeiQ9BYE9.
CleanExiHS_PCDH24.
ExpressionAtlasiQ9BYE9. baseline and differential.
GenevisibleiQ9BYE9. HS.

Family and domain databases

Gene3Di2.60.40.60. 9 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR030276. CDHR2.
[Graphical view]
PANTHERiPTHR24027:SF312. PTHR24027:SF312. 3 hits.
PfamiPF00028. Cadherin. 6 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 9 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 9 hits.
PROSITEiPS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Protocadherin LKC, a new candidate for a tumor suppressor of colon and liver cancers, its association with contact inhibition of cell proliferation."
    Okazaki N., Takahashi N., Kojima S., Masuho Y., Koga H.
    Carcinogenesis 23:1139-1148(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH MAST2, VARIANTS ALA-424 AND MET-1128.
    Tissue: KidneyImported.
  2. "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], VARIANTS ALA-424; MET-1128 AND MET-1164.
    Tissue: ColonImported and Trachea.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANTS ALA-424 AND MET-1128.
  5. "Differentially expressed genes between solitary large hepatocellular carcinoma and nodular hepatocellular carcinoma."
    Yang L.Y., Wang W., Peng J.X., Yang J.Q., Huang G.W.
    World J. Gastroenterol. 10:3569-3573(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "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, DOMAIN, INTERACTION WITH MYO7B AND USH1C, MUTAGENESIS OF LEU-1310, REGION, TISSUE SPECIFICITY.
  7. "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 SER-1248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Mechanistic basis of organization of the Harmonin/USH1C-mediated brush border microvilli tip-link complex."
    Li J., He Y., Lu Q., Zhang M.
    Dev. Cell 36:179-189(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USH1C.
  9. "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.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-1004.

Entry informationi

Entry nameiCDHR2_HUMAN
AccessioniPrimary (citable) accession number: Q9BYE9
Secondary accession number(s): A1L3U4, A6NC80, Q9NXP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 14, 2008
Last modified: May 11, 2016
This is version 128 of the entry and version 2 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 5
    Human chromosome 5: 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. 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.