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BICC1_HUMAN
ID   BICC1_HUMAN             Reviewed;         974 AA.
AC   Q9H694;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Protein bicaudal C homolog 1;
DE            Short=Bic-C;
GN   Name=BICC1;
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).
RA   Ferreira E.N., Pires L.C., Parmigiani R.B., Bettoni F., Puga R.D.,
RA   Pinheiro D.G., Andrade L.E.C., Cruz L.O., Degaki T.L., Faria M. Jr.,
RA   Festa F., Giannella-Neto D., Giorgi R.R., Goldman G.H., Granja F.,
RA   Gruber A., Hackel C., Henrique-Silva F., Malnic B., Manzini C.V.B.,
RA   Marie S.K.N., Martinez-Rossi N.M., Oba-Shinjo S.M., Pardini M.I.M.C.,
RA   Rahal P., Rainho C.A., Rogatto S.R., Romano C.M., Rodrigues V., Sales M.M.,
RA   Savoldi M., da Silva I.D.C.G., da Silva N.P., de Souza S.J., Tajara E.H.,
RA   Silva W.A. Jr., Simpson A.J.G., Sogayar M.C., Camargo A.A., Carraro D.M.;
RT   "Identification and complete sequencing of novel human transcripts through
RT   the use of mouse orthologs and testis cDNA sequences.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 367-974 (ISOFORM 2).
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-398, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6]
RP   FUNCTION AS NEGATIVE REGULATOR OF WNT SIGNALING, VARIANT CYSRD GLY-932,
RP   VARIANT THR-711, AND CHARACTERIZATION OF VARIANT CYSRD GLY-932.
RX   PubMed=21922595; DOI=10.1002/humu.21610;
RA   Kraus M.R., Clauin S., Pfister Y., Di Maio M., Ulinski T., Constam D.,
RA   Bellanne-Chantelot C., Grapin-Botton A.;
RT   "Two mutations in human BICC1 resulting in Wnt pathway hyperactivity
RT   associated with cystic renal dysplasia.";
RL   Hum. Mutat. 33:86-90(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8]
RP   VARIANT VAL-270.
RX   PubMed=24501278; DOI=10.1093/hmg/ddu056;
RA   Lee H., Lin M.C., Kornblum H.I., Papazian D.M., Nelson S.F.;
RT   "Exome sequencing identifies de novo gain of function missense mutation in
RT   KCND2 in identical twins with autism and seizures that slows potassium
RT   channel inactivation.";
RL   Hum. Mol. Genet. 23:3481-3489(2014).
CC   -!- FUNCTION: Putative RNA-binding protein. Acts as a negative regulator of
CC       Wnt signaling. May be involved in regulating gene expression during
CC       embryonic development. {ECO:0000269|PubMed:21922595}.
CC   -!- SUBUNIT: Interacts (via KH domains) with ANKS6 (via SAM domain) in an
CC       RNA-dependent manner (By similarity). Interacts with ANKS3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q99MQ1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H694-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H694-2; Sequence=VSP_021949;
CC   -!- DISEASE: Renal dysplasia, cystic (CYSRD) [MIM:601331]: An anomaly of
CC       the kidney characterized by numerous renal cysts and apparent disorder
CC       of differentiation of the renal parenchyma. Kidney of affected
CC       individuals lack the normal renal bean shape, and the collection
CC       drainage system. The cystic, dysplastic kidney contains
CC       undifferentiated mesenchyme, cartilaginous tissue, and immature
CC       collecting ducts. {ECO:0000269|PubMed:21922595}. Note=Disease
CC       susceptibility is associated with variants affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the BicC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY726586; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK026129; BAB15369.1; ALT_INIT; mRNA.
DR   CCDS; CCDS31206.1; -. [Q9H694-1]
DR   RefSeq; NP_001073981.1; NM_001080512.2. [Q9H694-1]
DR   PDB; 4RQM; X-ray; 1.75 A; A/B/C=870-939.
DR   PDB; 4RQN; X-ray; 2.00 A; A/B/C=870-939.
DR   PDB; 6GY4; X-ray; 1.99 A; A/B/C/D=47-130.
DR   PDBsum; 4RQM; -.
DR   PDBsum; 4RQN; -.
DR   PDBsum; 6GY4; -.
DR   AlphaFoldDB; Q9H694; -.
DR   SMR; Q9H694; -.
DR   BioGRID; 123119; 20.
DR   IntAct; Q9H694; 5.
DR   MINT; Q9H694; -.
DR   STRING; 9606.ENSP00000362993; -.
DR   iPTMnet; Q9H694; -.
DR   PhosphoSitePlus; Q9H694; -.
DR   BioMuta; BICC1; -.
DR   DMDM; 119367815; -.
DR   EPD; Q9H694; -.
DR   jPOST; Q9H694; -.
DR   MassIVE; Q9H694; -.
DR   MaxQB; Q9H694; -.
DR   PaxDb; Q9H694; -.
DR   PeptideAtlas; Q9H694; -.
DR   PRIDE; Q9H694; -.
DR   ProteomicsDB; 80965; -. [Q9H694-1]
DR   ProteomicsDB; 80966; -. [Q9H694-2]
DR   Antibodypedia; 51885; 166 antibodies from 26 providers.
DR   DNASU; 80114; -.
DR   Ensembl; ENST00000373886.8; ENSP00000362993.3; ENSG00000122870.12. [Q9H694-1]
DR   GeneID; 80114; -.
DR   KEGG; hsa:80114; -.
DR   MANE-Select; ENST00000373886.8; ENSP00000362993.3; NM_001080512.3; NP_001073981.1.
DR   UCSC; uc001jki.2; human. [Q9H694-1]
DR   CTD; 80114; -.
DR   DisGeNET; 80114; -.
DR   GeneCards; BICC1; -.
DR   HGNC; HGNC:19351; BICC1.
DR   HPA; ENSG00000122870; Tissue enhanced (kidney).
DR   MalaCards; BICC1; -.
DR   MIM; 601331; phenotype.
DR   MIM; 614295; gene.
DR   neXtProt; NX_Q9H694; -.
DR   OpenTargets; ENSG00000122870; -.
DR   Orphanet; 730; Autosomal dominant polycystic kidney disease.
DR   PharmGKB; PA134878124; -.
DR   VEuPathDB; HostDB:ENSG00000122870; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   eggNOG; KOG4374; Eukaryota.
DR   GeneTree; ENSGT00940000156276; -.
DR   HOGENOM; CLU_008040_0_0_1; -.
DR   InParanoid; Q9H694; -.
DR   OMA; ATHIHFP; -.
DR   OrthoDB; 201055at2759; -.
DR   PhylomeDB; Q9H694; -.
DR   TreeFam; TF323767; -.
DR   PathwayCommons; Q9H694; -.
DR   SignaLink; Q9H694; -.
DR   BioGRID-ORCS; 80114; 6 hits in 1072 CRISPR screens.
DR   ChiTaRS; BICC1; human.
DR   GenomeRNAi; 80114; -.
DR   Pharos; Q9H694; Tbio.
DR   PRO; PR:Q9H694; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q9H694; protein.
DR   Bgee; ENSG00000122870; Expressed in germinal epithelium of ovary and 156 other tissues.
DR   ExpressionAtlas; Q9H694; baseline and differential.
DR   Genevisible; Q9H694; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR   CDD; cd09520; SAM_BICC1; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   Gene3D; 3.30.1370.10; -; 1.
DR   InterPro; IPR037974; BICC1_SAM_dom.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00322; KH; 3.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   SUPFAM; SSF54791; SSF54791; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Developmental protein; Disease variant; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding.
FT   CHAIN           1..974
FT                   /note="Protein bicaudal C homolog 1"
FT                   /id="PRO_0000267714"
FT   DOMAIN          132..199
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          284..348
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          873..936
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..846
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MQ1"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MQ1"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MQ1"
FT   MOD_RES         398
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         576
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MQ1"
FT   MOD_RES         679
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99MQ1"
FT   VAR_SEQ         845..974
FT                   /note="TEHYLSSSNYMDCISSLTGSNGCNLNSSFKGSDLPELFSKLGLGKYTDVFQQ
FT                   QEIDLQTFLTLTDQDLKELGITTFGARRKMLLAISELNKNRRKLFESPNARTSFLEGGA
FT                   SGRLPRQYHSDIASVSGRW -> SELCVLCTLLGIPRLECVYLGWSITDCGLSDFKCLV
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_021949"
FT   VARIANT         8
FT                   /note="G -> D (in dbSNP:rs7905025)"
FT                   /id="VAR_029658"
FT   VARIANT         270
FT                   /note="M -> V (found in a family with atypical autism and
FT                   severe epilepsy; unknown pathological significance;
FT                   dbSNP:rs753582128)"
FT                   /evidence="ECO:0000269|PubMed:24501278"
FT                   /id="VAR_072077"
FT   VARIANT         711
FT                   /note="N -> T (in dbSNP:rs138916713)"
FT                   /evidence="ECO:0000269|PubMed:21922595"
FT                   /id="VAR_066759"
FT   VARIANT         932
FT                   /note="E -> G (in CYSRD; may impair splicing; hypomorphic
FT                   mutation; dbSNP:rs387907124)"
FT                   /evidence="ECO:0000269|PubMed:21922595"
FT                   /id="VAR_066760"
FT   VARIANT         943
FT                   /note="S -> P (in dbSNP:rs4948550)"
FT                   /id="VAR_033542"
FT   VARIANT         945
FT                   /note="N -> S (in dbSNP:rs7895817)"
FT                   /id="VAR_060133"
FT   STRAND          47..52
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   HELIX           55..67
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   HELIX           76..84
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   HELIX           93..97
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   HELIX           112..125
FT                   /evidence="ECO:0007829|PDB:6GY4"
FT   HELIX           875..877
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           878..884
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           888..890
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           891..896
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           901..904
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           909..915
FT                   /evidence="ECO:0007829|PDB:4RQM"
FT   HELIX           920..935
FT                   /evidence="ECO:0007829|PDB:4RQM"
SQ   SEQUENCE   974 AA;  104844 MW;  D2DB194BD3C8266D CRC64;
     MAAQGEPGYL AAQSDPGSNS ERSTDSPVPG SEDDLVAGAT LHSPEWSEER FRVDRKKLEA
     MLQAAAEGKG RSGEDFFQKI MEETNTQIAW PSKLKIGAKS KKDPHIKVSG KKEDVKEAKE
     MIMSVLDTKS NRVTLKMDVS HTEHSHVIGK GGNNIKKVME ETGCHIHFPD SNRNNQAEKS
     NQVSIAGQPA GVESARVRIR ELLPLVLMFE LPIAGILQPV PDPNSPSIQH ISQTYNISVS
     FKQRSRMYGA TVIVRGSQNN TSAVKEGTAM LLEHLAGSLA SAIPVSTQLD IAAQHHLFMM
     GRNGSNIKHI MQRTGAQIHF PDPSNPQKKS TVYLQGTIES VCLARQYLMG CLPLVLMFDM
     KEEIEVDPQF IAQLMEQLDV FISIKPKPKQ PSKSVIVKSV ERNALNMYEA RKCLLGLESS
     GVTIATSPSP ASCPAGLACP SLDILASAGL GLTGLGLLGP TTLSLNTSTT PNSLLNALNS
     SVSPLQSPSS GTPSPTLWAP PLANTSSATG FSAIPHLMIP STAQATLTNI LLSGVPTYGH
     TAPSPPPGLT PVDVHINSMQ TEGKKISAAL NGHAQSPDIK YGAISTSSLG EKVLSANHGD
     PSIQTSGSEQ TSPKSSPTEG CNDAFVEVGM PRSPSHSGNA GDLKQMMCPS KVSCAKRQTV
     ELLQGTKNSH LHSTDRLLSD PELSATESPL ADKKAPGSER AAERAAAAQQ NSERAHLAPR
     SSYVNMQAFD YEQKKLLATK AMLKKPVVTE VRTPTNTWSG LGFSKSMPAE TIKELRRANH
     VSYKPTMTTT YEGSSMSLSR SNSREHLGGG SESDNWRDRN GIGPGSHSEF AASIGSPKRK
     QNKSTEHYLS SSNYMDCISS LTGSNGCNLN SSFKGSDLPE LFSKLGLGKY TDVFQQQEID
     LQTFLTLTDQ DLKELGITTF GARRKMLLAI SELNKNRRKL FESPNARTSF LEGGASGRLP
     RQYHSDIASV SGRW
 
 
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