位置:首页 > 蛋白库 > ANKK1_MOUSE
ANKK1_MOUSE
ID   ANKK1_MOUSE             Reviewed;         745 AA.
AC   Q8BZ25;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Ankyrin repeat and protein kinase domain-containing protein 1;
DE            EC=2.7.11.1;
GN   Name=Ankk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK036872; BAC29613.1; -; mRNA.
DR   CCDS; CCDS40616.1; -.
DR   RefSeq; NP_766510.1; NM_172922.3.
DR   AlphaFoldDB; Q8BZ25; -.
DR   SMR; Q8BZ25; -.
DR   STRING; 10090.ENSMUSP00000034792; -.
DR   iPTMnet; Q8BZ25; -.
DR   PhosphoSitePlus; Q8BZ25; -.
DR   MaxQB; Q8BZ25; -.
DR   PaxDb; Q8BZ25; -.
DR   PRIDE; Q8BZ25; -.
DR   Antibodypedia; 2098; 115 antibodies from 29 providers.
DR   DNASU; 244859; -.
DR   Ensembl; ENSMUST00000034792; ENSMUSP00000034792; ENSMUSG00000032257.
DR   GeneID; 244859; -.
DR   KEGG; mmu:244859; -.
DR   UCSC; uc009pjb.1; mouse.
DR   CTD; 255239; -.
DR   MGI; MGI:3045301; Ankk1.
DR   VEuPathDB; HostDB:ENSMUSG00000032257; -.
DR   eggNOG; KOG0192; Eukaryota.
DR   GeneTree; ENSGT00940000162060; -.
DR   HOGENOM; CLU_015188_1_0_1; -.
DR   InParanoid; Q8BZ25; -.
DR   OMA; SIYGVCR; -.
DR   OrthoDB; 1112022at2759; -.
DR   PhylomeDB; Q8BZ25; -.
DR   TreeFam; TF106506; -.
DR   BioGRID-ORCS; 244859; 0 hits in 76 CRISPR screens.
DR   PRO; PR:Q8BZ25; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8BZ25; protein.
DR   Bgee; ENSMUSG00000032257; Expressed in striatum and 8 other tissues.
DR   ExpressionAtlas; Q8BZ25; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0010564; P:regulation of cell cycle process; IDA:MGI.
DR   Gene3D; 1.25.40.20; -; 4.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 4.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 11.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 11.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..745
FT                   /note="Ankyrin repeat and protein kinase domain-containing
FT                   protein 1"
FT                   /id="PRO_0000085621"
FT   DOMAIN          34..301
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          369..398
FT                   /note="ANK 1"
FT   REPEAT          402..431
FT                   /note="ANK 2"
FT   REPEAT          435..464
FT                   /note="ANK 3"
FT   REPEAT          468..497
FT                   /note="ANK 4"
FT   REPEAT          501..530
FT                   /note="ANK 5"
FT   REPEAT          534..563
FT                   /note="ANK 6"
FT   REPEAT          567..596
FT                   /note="ANK 7"
FT   REPEAT          600..629
FT                   /note="ANK 8"
FT   REPEAT          633..662
FT                   /note="ANK 9"
FT   REPEAT          666..695
FT                   /note="ANK 10"
FT   REPEAT          699..728
FT                   /note="ANK 11"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         40..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   745 AA;  82480 MW;  DDD391ECD19EB84D CRC64;
     MVPHRARRLL NPMAVGPLAQ QLGSLTVFTR DDFEEEWHLV ASGGFSKVFQ ARHKRWRTQY
     AIKCSPCLQK ETTSSEVTCL FEEAVKMEKI KFQHIVSIYG VCKQPLGIVM EFMASGSLEK
     TLPTHSLCWP LKLRIIHETS LAMNFLHSIK PPLLHLDLKP GNILLDNNMH VKISDFGLSK
     WMEQSTQKQY IERSALRGTL SYIPPEMFLE NNKAPGPEYD VYSFAIVIWE ILTQKKPYAG
     LNMMTIIIRV AAGMRPSLQD VSDEWPEEVH QMVNLMKRCW DQDPKKRPCF LNVAVETDML
     LSLFQSPMTD PGCEALTQKV SCKPSLSQPH KVSKEVNQEI ADSVSSDSLK WILQLSDSKS
     LVASDVYENR VTPLHFLVAG GSLEQVRLLL SHDVDVDCQT ASGYTPLLIA TQDQQPDLCA
     LLLAHGADTN LADEDGWAPL HFAAQNGDDH TARLLLDHGA LVNAREHEGW TPLHLAAQNN
     FENVARLLVS RQADLSPHEA EGKTPLHVAA YFGHIGLVKL LSGQGAELDA QQRNLRTPLH
     LAVERGKVRA IQHLLKCGAL PDALDHSGYS PLHIAAARGK DLIFKMLLRY GASLELRTQQ
     GWTPLHLATY KGHLEIIHQL AKSHVDLDAL GSMQWTPLHL AAFQGEEGVM LALLQCGANP
     NAAEQSGWTP LHLAVHKGTF LGITHLLEYG ADIHACNKVG WTPAHLAALK GNTAILKVLV
     KAAAQVDVKG GVSCTPLQLA IHSPK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024