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PCDBE_HUMAN
ID   PCDBE_HUMAN             Reviewed;         798 AA.
AC   Q9Y5E9; B4DPE2; Q4FZA4; Q4KN11;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Protocadherin beta-14;
DE            Short=PCDH-beta-14;
DE   Flags: Precursor;
GN   Name=PCDHB14;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA   Wu Q., Maniatis T.;
RT   "A striking organization of a large family of human neural cadherin-like
RT   cell adhesion genes.";
RL   Cell 97:779-790(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11322959; DOI=10.1016/s0014-5793(01)02372-9;
RA   Vanhalst K., Kools P., Vanden Eynde E., van Roy F.;
RT   "The human and murine protocadherin-beta one-exon gene families show high
RT   evolutionary conservation, despite the difference in gene number.";
RL   FEBS Lett. 495:120-125(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May be
CC       involved in the establishment and maintenance of specific neuronal
CC       connections in the brain.
CC   -!- INTERACTION:
CC       Q9Y5E9; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-10329013, EBI-357530;
CC       Q9Y5E9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10329013, EBI-5916454;
CC       Q9Y5E9; P61978: HNRNPK; NbExp=6; IntAct=EBI-10329013, EBI-304185;
CC       Q9Y5E9; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-10329013, EBI-7060731;
CC       Q9Y5E9; O43390-2: HNRNPR; NbExp=3; IntAct=EBI-10329013, EBI-12236340;
CC       Q9Y5E9; O75525: KHDRBS3; NbExp=3; IntAct=EBI-10329013, EBI-722504;
CC       Q9Y5E9; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-10329013, EBI-3044087;
CC       Q9Y5E9; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10329013, EBI-11522433;
CC       Q9Y5E9; O43586: PSTPIP1; NbExp=6; IntAct=EBI-10329013, EBI-1050964;
CC       Q9Y5E9; Q96QR8: PURB; NbExp=3; IntAct=EBI-10329013, EBI-2880222;
CC       Q9Y5E9; P38159: RBMX; NbExp=3; IntAct=EBI-10329013, EBI-743526;
CC       Q9Y5E9; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-10329013, EBI-8638511;
CC       Q9Y5E9; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-10329013, EBI-11994018;
CC       Q9Y5E9; Q15415: RBMY1J; NbExp=6; IntAct=EBI-10329013, EBI-8642021;
CC       Q9Y5E9; P84103: SRSF3; NbExp=3; IntAct=EBI-10329013, EBI-372557;
CC       Q9Y5E9; P62995: TRA2B; NbExp=3; IntAct=EBI-10329013, EBI-725485;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y5E9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y5E9-2; Sequence=VSP_055932;
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DR   EMBL; AF152493; AAD43754.1; -; mRNA.
DR   EMBL; AF217744; AAK51612.1; -; mRNA.
DR   EMBL; AK298296; BAG60554.1; -; mRNA.
DR   EMBL; AC005752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC098144; AAH98144.1; -; mRNA.
DR   EMBL; BC099728; AAH99728.1; -; mRNA.
DR   CCDS; CCDS4256.1; -. [Q9Y5E9-1]
DR   RefSeq; NP_061757.1; NM_018934.3. [Q9Y5E9-1]
DR   AlphaFoldDB; Q9Y5E9; -.
DR   SMR; Q9Y5E9; -.
DR   BioGRID; 121062; 20.
DR   IntAct; Q9Y5E9; 14.
DR   STRING; 9606.ENSP00000239449; -.
DR   GlyConnect; 1678; 1 N-Linked glycan (1 site).
DR   GlyGen; Q9Y5E9; 6 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9Y5E9; -.
DR   PhosphoSitePlus; Q9Y5E9; -.
DR   BioMuta; PCDHB14; -.
DR   DMDM; 13431380; -.
DR   EPD; Q9Y5E9; -.
DR   jPOST; Q9Y5E9; -.
DR   MassIVE; Q9Y5E9; -.
DR   PaxDb; Q9Y5E9; -.
DR   PeptideAtlas; Q9Y5E9; -.
DR   PRIDE; Q9Y5E9; -.
DR   ProteomicsDB; 4778; -.
DR   ProteomicsDB; 86348; -. [Q9Y5E9-1]
DR   Antibodypedia; 27242; 104 antibodies from 20 providers.
DR   DNASU; 56122; -.
DR   Ensembl; ENST00000239449.7; ENSP00000239449.4; ENSG00000120327.7. [Q9Y5E9-1]
DR   Ensembl; ENST00000624896.1; ENSP00000485055.1; ENSG00000120327.7. [Q9Y5E9-2]
DR   GeneID; 56122; -.
DR   KEGG; hsa:56122; -.
DR   MANE-Select; ENST00000239449.7; ENSP00000239449.4; NM_018934.4; NP_061757.1.
DR   UCSC; uc003ljb.5; human. [Q9Y5E9-1]
DR   CTD; 56122; -.
DR   GeneCards; PCDHB14; -.
DR   HGNC; HGNC:8685; PCDHB14.
DR   HPA; ENSG00000120327; Low tissue specificity.
DR   MIM; 604967; gene.
DR   MIM; 606340; gene.
DR   neXtProt; NX_Q9Y5E9; -.
DR   OpenTargets; ENSG00000120327; -.
DR   PharmGKB; PA33030; -.
DR   VEuPathDB; HostDB:ENSG00000120327; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000163362; -.
DR   HOGENOM; CLU_006480_3_0_1; -.
DR   InParanoid; Q9Y5E9; -.
DR   OMA; SWIVTIS; -.
DR   OrthoDB; 300321at2759; -.
DR   PhylomeDB; Q9Y5E9; -.
DR   TreeFam; TF332299; -.
DR   PathwayCommons; Q9Y5E9; -.
DR   SignaLink; Q9Y5E9; -.
DR   BioGRID-ORCS; 56122; 17 hits in 1029 CRISPR screens.
DR   ChiTaRS; PCDHB14; human.
DR   GeneWiki; PCDHB14; -.
DR   GenomeRNAi; 56122; -.
DR   Pharos; Q9Y5E9; Tdark.
DR   PRO; PR:Q9Y5E9; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9Y5E9; protein.
DR   Bgee; ENSG00000120327; Expressed in cortical plate and 148 other tissues.
DR   Genevisible; Q9Y5E9; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0007416; P:synapse assembly; TAS:UniProtKB.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR032455; Cadherin_C.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF16492; Cadherin_C_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; SSF49313; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..798
FT                   /note="Protocadherin beta-14"
FT                   /id="PRO_0000003940"
FT   TOPO_DOM        27..686
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        687..711
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        712..798
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          35..133
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          138..242
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          247..347
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          352..451
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          456..561
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          568..671
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        436
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        567
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        96..102
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..153
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055932"
SQ   SEQUENCE   798 AA;  87548 MW;  65151C1A423BB52E CRC64;
     MEIRGALDLR KRQVLIFLVL LGLSRAGTES AHYSVAEETE IGSFVANLAR DLGLGVEELS
     SREARVVSDD NKKYLHLDLL TGNLLLNEKL DRDELCGSTE PCVLHFQVVL ENPLQFFRFE
     LCVKDINDHS PTFLDKEILI KISEGTTVGA TFLMESAQDL DVGSNSLQNY TISPNSHFYI
     KIPDSSDRKI YPELVLDRAL DYEQEAELRL TLTAVDGGSP PKSGTTLVLI KVLDINDNAP
     EFPQSLYEVQ VPEDRPLGSW IATISAKDLD AGNYGKISYT FFHASEDIRK TFEINPISGE
     VNLRSPLDFE VIQSYTINIQ ATDGGGLSGK CTLLVKVMDI NDNPPEVTIS SITKRIPENA
     SETLVALFSI LDQDSGDNGR MICSIQDNLP FFLKPTFKNF FTLVSEKALD RESQAEYNIT
     ITVTDLGTPR LKTEYNITVL LSDVNDNAPT FTQTSYTLFV RENNSPALHI GSVSATDRDS
     GTNAQVNYSL LPPQDRHLPL ASLVSINADN GHLFALRSLD YEALQEFEFR VGATDRGSPA
     LSSEALVRVL VLDANDNSPF VLYPLQNGSA PCTELVPRAA EPGYLVTKVV AVDGDSGQNA
     WLSYQLLKAT EPGLFGVWAH NGEVRTARLL SERDAAKHRL VVLVKDNGEP PRSATATLHV
     LLVDGFSQPY LPLPEAAPAQ AQADSLTVYL VVALASVSSL FLFSVLLFVA VRLCRRSRAA
     SVGRCSVPEG PFPGHLVDVS GTGTLSQSYQ YEVCLTGGSG TNEFKFLKPI IPNFQVHDTG
     RNMGEIENFR NSFGLNIQ
 
 
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