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ADCK2_MOUSE
ID   ADCK2_MOUSE             Reviewed;         617 AA.
AC   Q6NSR3; Q3TTS5; Q8BHC6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Uncharacterized aarF domain-containing protein kinase 2;
DE            EC=2.7.11.-;
GN   Name=Adck2;
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=Head, and Skin;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
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: The function of this protein is not yet clear. It is not
CC       known if it has protein kinase activity and what type of substrate it
CC       would phosphorylate (Ser, Thr or Tyr).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC       kinase family. {ECO:0000305}.
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DR   EMBL; AK028557; BAC26008.1; -; mRNA.
DR   EMBL; AK028568; BAC26013.1; -; mRNA.
DR   EMBL; AK161225; BAE36249.1; -; mRNA.
DR   EMBL; BC069944; AAH69944.1; -; mRNA.
DR   CCDS; CCDS20024.1; -.
DR   RefSeq; NP_849204.1; NM_178873.3.
DR   AlphaFoldDB; Q6NSR3; -.
DR   STRING; 10090.ENSMUSP00000123563; -.
DR   iPTMnet; Q6NSR3; -.
DR   PhosphoSitePlus; Q6NSR3; -.
DR   MaxQB; Q6NSR3; -.
DR   PaxDb; Q6NSR3; -.
DR   PRIDE; Q6NSR3; -.
DR   ProteomicsDB; 285617; -.
DR   DNASU; 57869; -.
DR   GeneID; 57869; -.
DR   KEGG; mmu:57869; -.
DR   UCSC; uc009bmb.1; mouse.
DR   CTD; 90956; -.
DR   MGI; MGI:1889336; Adck2.
DR   eggNOG; KOG1236; Eukaryota.
DR   InParanoid; Q6NSR3; -.
DR   OrthoDB; 1299789at2759; -.
DR   TreeFam; TF315018; -.
DR   BioGRID-ORCS; 57869; 3 hits in 75 CRISPR screens.
DR   ChiTaRS; Adck2; mouse.
DR   PRO; PR:Q6NSR3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6NSR3; protein.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd13971; ADCK2-like; 1.
DR   InterPro; IPR004147; ABC1_dom.
DR   InterPro; IPR044095; ADCK2_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   Pfam; PF03109; ABC1; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..617
FT                   /note="Uncharacterized aarF domain-containing protein
FT                   kinase 2"
FT                   /id="PRO_0000271793"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          200..609
FT                   /note="Protein kinase"
FT   ACT_SITE        436
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         206..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         302
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        342
FT                   /note="E -> K (in Ref. 1; BAE36249)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        528
FT                   /note="R -> K (in Ref. 1; BAC26008/BAC26013/BAE36249)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   617 AA;  68677 MW;  3230111C7DB65CEC CRC64;
     MVTPWRLSVR VCLSHLRCFE FRKELGHSRP LGCSRNARLC WFLLGTLPKL ISAHGSVGEG
     APGSLCQRKT HWSDLAENGL VEKVAQEGPL ARVLLCLRLG LRAGVLLAKF FPLLFLYPLT
     YLAPGLSTLW LHLLFKATET SGPTYIKLGQ WASTRRDLFS EAFCTQFSKL HVQVTPHPWA
     RTEYLLQQAF GEDWGSLLFF ETREPVGSGC VAQVYKAFAS ISLLEEDRIW RLGELSAPGT
     RAVVMQREPF MKDRKPSENL ADEAFLEKLL LPKADLGGSE VGVSQAPWHL PKSDHLIPVA
     VKVLHPGLLS QVSMDLLLMK IGSKALGLLP GVKWLSLPEI VEEFEKLMVQ QTDLRYEAQN
     LEHFQHNFQD MASVKFPTPL RPLITRDILV ETYEESVPVS SYQQAGIPTD LKRKIAQLGI
     NMLLKMIFVD NFVHGDLHPG NILVQGADGV SPSLEMQQQQ VNVCDTLVAT IAPALCPLRL
     VLLDAGIVAK LQASDLRNFR AVFQAVVMGQ GHRVAELMLH HAQANECRDV ERFKAEMATL
     VTQARKNIVT LEKLHVSSLL SSVFKLLMTH KVKLESNFAS IVVAIMVLEG LGRSLDPTLD
     ILEAAKPFLF KGPASFL
 
 
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