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DCDC1_HUMAN
ID   DCDC1_HUMAN             Reviewed;        1783 AA.
AC   M0R2J8; A6PVL6; B1AL47; B7WNX6; P59894; Q6ZRR9; Q6ZU04;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Doublecortin domain-containing protein 1 {ECO:0000305};
DE   AltName: Full=Doublecortin domain-containing 5 protein {ECO:0000303|PubMed:22159412};
GN   Name=DCDC1 {ECO:0000312|HGNC:HGNC:20625};
GN   Synonyms=DCDC5 {ECO:0000303|PubMed:22159412}, KIAA1493;
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 3), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   PubMed=12820024; DOI=10.1007/s10038-003-0033-3;
RA   Zeng L., Gu S., Li Y., Zhao E., Xu J., Ye X., Wu Q., Wang L., Xie Y.,
RA   Mao Y.;
RT   "Identification of a novel human doublecortin-domain-containing gene
RT   (DCDC1) expressed mainly in testis.";
RL   J. Hum. Genet. 48:393-396(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, MICROTUBULE-BINDING, AND INTERACTION WITH
RP   DYNEIN INTERMEDIATE CHAIN; TUBULIN; RAB8A; RAB3IP; NUDC; PAFAH1B1 AND
RP   DCTN1.
RX   PubMed=22159412; DOI=10.1242/jcs.085407;
RA   Kaplan A., Reiner O.;
RT   "Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody
RT   during cytokinesis by the doublecortin domain-containing 5 protein.";
RL   J. Cell Sci. 124:3989-4000(2011).
CC   -!- FUNCTION: Microtubule-binding protein which plays an important role in
CC       mediating dynein-dependent transport of RAB8A-positive vesicles to the
CC       midbody during cytokinesis (PubMed:22159412).
CC       {ECO:0000269|PubMed:22159412}.
CC   -!- SUBUNIT: Interacts with dynein intermediate chain, tubulin, RAB8A,
CC       RAB3IP, NUDC, PAFAH1B1 and DCTN1 (PubMed:22159412).
CC       {ECO:0000269|PubMed:22159412}.
CC   -!- SUBCELLULAR LOCATION: Midbody, Midbody ring
CC       {ECO:0000269|PubMed:22159412}. Midbody {ECO:0000269|PubMed:22159412}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22159412}.
CC       Note=Associated with microtubules, in particular, with stabilized
CC       microtubules of the mitotic spindle during metaphase and with midbody
CC       microtubules during cytokinesis. {ECO:0000269|PubMed:22159412}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=M0R2J8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=M0R2J8-2; Sequence=VSP_060022, VSP_060023;
CC       Name=3;
CC         IsoId=M0R2J8-3; Sequence=VSP_060024, VSP_060025;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC87240.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence and several conflicts. Sequence of unknown origin in the N-terminal part of the CDS.; Evidence={ECO:0000305};
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DR   EMBL; AY247970; AAP75563.1; -; mRNA.
DR   EMBL; AK126066; BAC86423.2; -; mRNA.
DR   EMBL; AK128035; BAC87240.1; ALT_SEQ; mRNA.
DR   EMBL; AL133296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL133376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL135932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL162614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF455358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS7872.1; -. [M0R2J8-3]
DR   RefSeq; NP_861523.2; NM_181807.3. [M0R2J8-3]
DR   AlphaFoldDB; M0R2J8; -.
DR   BioGRID; 131112; 8.
DR   IntAct; M0R2J8; 1.
DR   STRING; 9606.ENSP00000385936; -.
DR   iPTMnet; M0R2J8; -.
DR   PhosphoSitePlus; M0R2J8; -.
DR   BioMuta; DCDC1; -.
DR   BioMuta; HGNC:24799; -.
DR   DMDM; 190359182; -.
DR   jPOST; M0R2J8; -.
DR   MassIVE; M0R2J8; -.
DR   PeptideAtlas; M0R2J8; -.
DR   PRIDE; M0R2J8; -.
DR   ProteomicsDB; 57166; -.
DR   ProteomicsDB; 6281; -.
DR   ProteomicsDB; 68160; -.
DR   Antibodypedia; 48955; 59 antibodies from 8 providers.
DR   DNASU; 341019; -.
DR   Ensembl; ENST00000342355.8; ENSP00000343496.4; ENSG00000170959.15. [M0R2J8-2]
DR   Ensembl; ENST00000452803.1; ENSP00000389792.1; ENSG00000170959.15. [M0R2J8-3]
DR   Ensembl; ENST00000597505.5; ENSP00000472625.1; ENSG00000170959.15. [M0R2J8-1]
DR   GeneID; 341019; -.
DR   KEGG; hsa:341019; -.
DR   UCSC; uc058aah.1; human. [M0R2J8-1]
DR   CTD; 341019; -.
DR   DisGeNET; 341019; -.
DR   GeneCards; DCDC1; -.
DR   HGNC; HGNC:20625; DCDC1.
DR   HPA; ENSG00000170959; Tissue enhanced (choroid).
DR   MIM; 608062; gene.
DR   neXtProt; NX_M0R2J8; -.
DR   OpenTargets; ENSG00000170959; -.
DR   PharmGKB; PA134970075; -.
DR   VEuPathDB; HostDB:ENSG00000170959; -.
DR   eggNOG; ENOG502QW8Q; Eukaryota.
DR   GeneTree; ENSGT00940000163628; -.
DR   HOGENOM; CLU_067120_0_1_1; -.
DR   OMA; TNNFCLI; -.
DR   PhylomeDB; M0R2J8; -.
DR   TreeFam; TF329467; -.
DR   PathwayCommons; M0R2J8; -.
DR   SignaLink; M0R2J8; -.
DR   BioGRID-ORCS; 341019; 15 hits in 1073 CRISPR screens.
DR   ChiTaRS; DCDC1; human.
DR   GenomeRNAi; 341019; -.
DR   PRO; PR:M0R2J8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000170959; Expressed in oviduct epithelium and 106 other tissues.
DR   ExpressionAtlas; M0R2J8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:UniProtKB.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 3.10.20.230; -; 2.
DR   InterPro; IPR043188; DCDC1.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR036572; Doublecortin_dom_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR46302; PTHR46302; 3.
DR   SMART; SM00537; DCX; 3.
DR   SUPFAM; SSF50370; SSF50370; 2.
DR   SUPFAM; SSF89837; SSF89837; 5.
DR   PROSITE; PS50309; DC; 2.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW   Lectin; Microtubule; Mitosis; Reference proteome; Repeat.
FT   CHAIN           1..1783
FT                   /note="Doublecortin domain-containing protein 1"
FT                   /id="PRO_0000446088"
FT   DOMAIN          168..252
FT                   /note="Doublecortin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          702..800
FT                   /note="Ricin B-type lectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   DOMAIN          925..1015
FT                   /note="Doublecortin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          1151..1266
FT                   /note="Ricin B-type lectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT   REGION          93..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          860..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         252..270
FT                   /note="DHLLLIKKVTWTMNGLMLP -> GFRYLYNKNESKFTSQIFL (in
FT                   isoform 2)"
FT                   /id="VSP_060022"
FT   VAR_SEQ         271..1783
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060023"
FT   VAR_SEQ         352..354
FT                   /note="VPL -> GKH (in isoform 3)"
FT                   /id="VSP_060024"
FT   VAR_SEQ         355..1783
FT                   /note="Missing (in isoform 3)"
FT                   /id="VSP_060025"
FT   VARIANT         7
FT                   /note="E -> G (in dbSNP:rs11031357)"
FT                   /id="VAR_037284"
FT   VARIANT         83
FT                   /note="V -> M (in dbSNP:rs2761591)"
FT                   /id="VAR_033767"
FT   CONFLICT        192
FT                   /note="V -> A (in Ref. 1; AAP75563)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1783 AA;  200591 MW;  B4EC8D37407E6A92 CRC64;
     MAKTGAEDHR EALSQSSLSL LTEAMEVLQQ SSPEGTLDGN TVNPIYKYIL NDLPREFMSS
     QAKAVIKTTD DYLQSQFGPN RLVHSAAVSE GSGLQDCSTH QTASDHSHDE ISDLDSYKSN
     SKNNSCSISA SKRNRPVSAP VGQLRVAEFS SLKFQSARNW QKLSQRHKLQ PRVIKVTAYK
     NGSRTVFARV TVPTITLLLE ECTEKLNLNM AARRVFLADG KEALEPEDIP HEADVYVSTG
     EPFLNPFKKI KDHLLLIKKV TWTMNGLMLP TDIKRRKTKP VLSIRMKKLT ERTSVRILFF
     KNGMGQDGHE ITVGKETMKK VLDTCTIRMN LNLPARYFYD LYGRKIEDIS KVPLLEKCLQ
     NSITPLRGLL WVSKGEGFSP SGAKMYIQGV LLALYQRLKS AKKYYKQLNL VMNEQKEKIT
     EKVILSMTAK EHHKEQEEVS RLIDELQTAI KSNIGHLCKL GPQLQAEQEQ FSSYVYQHIK
     SLPANTLVPG GLQLKVFENG KNTGEISVGI SKKDLGSDSP IQTDHMMERL LLKIHQRLQG
     SSINPPGLNY SSMRLFDENG QEIKNPLSLK NEQKIWVSYG RAYRSPLNLA LGLTFDRVSA
     FARGDIMVAY KTFLDPNAVL LPGCGNWEVC EGFPINFNCT SQQIPDQFEK VDLENHFLQN
     KVDPNIVLHA SVSIGKWSFS GSEASSRSQI APSILWPVAS VWLITKTGMI LSRAITQGCL
     AIGHPIRVKA AEGTSLEGYK LILQKRHSGD DSQKWVFGTD GCIYSKAYPQ FVLTYLEELN
     AQVDVTQTEY HIHHGAWTTA HQEHGRNLAE EVLQESASNL GLKQLPEPSD THLMPEGSLE
     ETGELTVALV RKLEEKHPKA SAQRWAIKHE GTSKPGQWKH SRVENPLWNK LTYMWPVLPS
     GQLNEEFDWP IQGLLVPSSP PMKKPICKTT EPYAPVRLRV LQNGEKNKNR SVTILGPDIS
     PGRKTQCTEI LNLPSAARRL YNEKGKEIFA LKDLQRDELV YVSCGELWIN PDLSIAQQKK
     QIFLRNLESD IAKIQIFCST HKIEALVLEV QSDIVSGSKL AVHKPVAIFG EEKQVTEPEE
     KQMQEDPLTT ENASSEILDS HVRAHLRMKA CHTLPRYAWQ ETSHDFDEDD SLPKKTEKGL
     FENVEPQKKH SCSPKHSKLH KHCHQQFEYR DGQIISHAAP QLVLGVQGPN LRSGMEVVLV
     EKKSDGSHQR WIHQEDSRTF HLVSNPDLVL AVSMTKTRNE VCGYPVIVQK YKPYNNGAAN
     QKWHYMKNIK ALVAFHSTAL DKEITSANYA GVCTSSVIKE ENIDQPGYCY LSPDGKRKTM
     LCLACGQSMR TEKGLKQLLP GVPFLCISGT KTQKPFLQGP FKVISVAEVD LSCDKAEKTL
     SYYQARLLSL RMKTCTQAAS HSGMAATHQK AVKIIAYKNG DGYRNGKLIV AGTFPMLLTE
     CTEQLGLARA ASKVYTKDGT PIFTLRDLVL WALDESFLQR DSEKQKQDAA PVGKEQIIVE
     KNPRMKVKNR LFAKSVTSDS LDGIDKSLLT LILRNPIAIW VSCGEPFLPP NALQKAEKLE
     KQNWLKKDRI LADLDTMRHK MRQLKGRRVA ACQPATMVPT KSPVQPVVVE GGWTEQTQQE
     IKLMELIRHT EAHLSEIQEM ESKINFPIAT KRIAVKPSNL YKQPNTKRVW IYLNGGRPED
     GTYAWGKTIS ELLQDCSSRL KMTHPARALY TPSGEPIQSW DDIERDMVIC VSMGHGFKTP
     KELKQLMEIR ANYARIRRQQ GPQATDIVVS PSTKLLSLAH LHN
 
 
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