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ANKY2_HUMAN
ID   ANKY2_HUMAN             Reviewed;         441 AA.
AC   Q8IV38; A4D124; Q659G1; Q96BL3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Ankyrin repeat and MYND domain-containing protein 2;
GN   Name=ANKMY2;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Prostate;
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: May be involved in the trafficking of signaling proteins to
CC       the cilia. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with the retinal-specific guanylyl cyclase GC1.
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8IV38; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-9393876, EBI-717399;
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250}.
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DR   EMBL; AL050390; CAH56419.1; -; mRNA.
DR   EMBL; CH236948; EAL24286.1; -; Genomic_DNA.
DR   EMBL; CH471073; EAW93672.1; -; Genomic_DNA.
DR   EMBL; BC015453; AAH15453.1; -; mRNA.
DR   EMBL; BC035353; AAH35353.1; -; mRNA.
DR   CCDS; CCDS5361.1; -.
DR   RefSeq; NP_064715.1; NM_020319.2.
DR   AlphaFoldDB; Q8IV38; -.
DR   SMR; Q8IV38; -.
DR   BioGRID; 121333; 55.
DR   IntAct; Q8IV38; 21.
DR   STRING; 9606.ENSP00000303570; -.
DR   iPTMnet; Q8IV38; -.
DR   PhosphoSitePlus; Q8IV38; -.
DR   BioMuta; ANKMY2; -.
DR   DMDM; 74750650; -.
DR   EPD; Q8IV38; -.
DR   jPOST; Q8IV38; -.
DR   MassIVE; Q8IV38; -.
DR   MaxQB; Q8IV38; -.
DR   PaxDb; Q8IV38; -.
DR   PeptideAtlas; Q8IV38; -.
DR   PRIDE; Q8IV38; -.
DR   ProteomicsDB; 70655; -.
DR   Antibodypedia; 43960; 193 antibodies from 19 providers.
DR   DNASU; 57037; -.
DR   Ensembl; ENST00000306999.7; ENSP00000303570.2; ENSG00000106524.9.
DR   GeneID; 57037; -.
DR   KEGG; hsa:57037; -.
DR   MANE-Select; ENST00000306999.7; ENSP00000303570.2; NM_020319.3; NP_064715.1.
DR   UCSC; uc003sti.3; human.
DR   CTD; 57037; -.
DR   GeneCards; ANKMY2; -.
DR   HGNC; HGNC:25370; ANKMY2.
DR   HPA; ENSG00000106524; Low tissue specificity.
DR   neXtProt; NX_Q8IV38; -.
DR   OpenTargets; ENSG00000106524; -.
DR   PharmGKB; PA134893861; -.
DR   VEuPathDB; HostDB:ENSG00000106524; -.
DR   eggNOG; KOG1710; Eukaryota.
DR   GeneTree; ENSGT00390000016820; -.
DR   InParanoid; Q8IV38; -.
DR   OMA; AFKYHYL; -.
DR   OrthoDB; 1413951at2759; -.
DR   PhylomeDB; Q8IV38; -.
DR   TreeFam; TF351374; -.
DR   PathwayCommons; Q8IV38; -.
DR   SignaLink; Q8IV38; -.
DR   BioGRID-ORCS; 57037; 53 hits in 1075 CRISPR screens.
DR   ChiTaRS; ANKMY2; human.
DR   GenomeRNAi; 57037; -.
DR   Pharos; Q8IV38; Tdark.
DR   PRO; PR:Q8IV38; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8IV38; protein.
DR   Bgee; ENSG00000106524; Expressed in middle temporal gyrus and 207 other tissues.
DR   ExpressionAtlas; Q8IV38; baseline and differential.
DR   Genevisible; Q8IV38; HS.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell projection; Cilium; Metal-binding; Reference proteome;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..441
FT                   /note="Ankyrin repeat and MYND domain-containing protein 2"
FT                   /id="PRO_0000247166"
FT   REPEAT          45..74
FT                   /note="ANK 1"
FT   REPEAT          79..108
FT                   /note="ANK 2"
FT   REPEAT          159..188
FT                   /note="ANK 3"
FT   ZN_FING         320..357
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   REGION          374..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         341
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         345
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   CONFLICT        273
FT                   /note="K -> KISLLMAFQCIKKRSLEKVSEK (in Ref. 1; CAH56419)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  49299 MW;  E9A5E1B9ABCBA4A6 CRC64;
     MVHIKKGELT QEEKELLEVI GKGTVQEAGT LLSSKNVRVN CLDENGMTPL MHAAYKGKLD
     MCKLLLRHGA DVNCHQHEHG YTALMFAALS GNKDITWVML EAGAETDVVN SVGRTAAQMA
     AFVGQHDCVT IINNFFPRER LDYYTKPQGL DKEPKLPPKL AGPLHKIITT TNLHPVKIVM
     LVNENPLLTE EAALNKCYRV MDLICEKCMK QRDMNEVLAM KMHYISCIFQ KCINFLKDGE
     NKLDTLIKSL LKGRASDGFP VYQEKIIRES IRKFPYCEAT LLQQLVRSIA PVEIGSDPTA
     FSVLTQAITG QVGFVDVEFC TTCGEKGASK RCSVCKMVIY CDQTCQKTHW FTHKKICKNL
     KDIYEKQQLE AAKEKRQEEN HGKLDVNSNC VNEEQPEAEV GISQKDSNPE DSGEGKKESL
     ESEAELEGLQ DAPAGPQVSE E
 
 
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