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DEN2A_MOUSE
ID   DEN2A_MOUSE             Reviewed;        1000 AA.
AC   Q8C4S8; Q3TJU2; Q3TUG3; Q3UXA3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=DENN domain-containing protein 2A;
GN   Name=Dennd2a;
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=Cerebellum, and Head;
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   PROTEIN SEQUENCE OF 210-217, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC       RAB9A and RAB9B. Promotes the exchange of GDP to GTP, converting
CC       inactive GDP-bound Rab proteins into their active GTP-bound form. May
CC       play a role in late endosomes back to trans-Golgi network/TGN transport
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Note=Associated with actin filaments. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22660.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK081176; BAC38157.1; -; mRNA.
DR   EMBL; AK135781; BAE22660.1; ALT_INIT; mRNA.
DR   EMBL; AK160784; BAE36008.1; -; mRNA.
DR   EMBL; AK167298; BAE39403.1; -; mRNA.
DR   CCDS; CCDS20023.1; -.
DR   RefSeq; NP_766065.1; NM_172477.4.
DR   AlphaFoldDB; Q8C4S8; -.
DR   SMR; Q8C4S8; -.
DR   BioGRID; 229109; 2.
DR   STRING; 10090.ENSMUSP00000045367; -.
DR   iPTMnet; Q8C4S8; -.
DR   PhosphoSitePlus; Q8C4S8; -.
DR   jPOST; Q8C4S8; -.
DR   MaxQB; Q8C4S8; -.
DR   PaxDb; Q8C4S8; -.
DR   PRIDE; Q8C4S8; -.
DR   ProteomicsDB; 279369; -.
DR   Antibodypedia; 32452; 39 antibodies from 13 providers.
DR   DNASU; 209773; -.
DR   Ensembl; ENSMUST00000036877; ENSMUSP00000045367; ENSMUSG00000038456.
DR   GeneID; 209773; -.
DR   KEGG; mmu:209773; -.
DR   UCSC; uc009blx.1; mouse.
DR   CTD; 27147; -.
DR   MGI; MGI:2444961; Dennd2a.
DR   VEuPathDB; HostDB:ENSMUSG00000038456; -.
DR   eggNOG; KOG3569; Eukaryota.
DR   GeneTree; ENSGT00950000182931; -.
DR   HOGENOM; CLU_008960_1_1_1; -.
DR   InParanoid; Q8C4S8; -.
DR   OMA; KPIFFRQ; -.
DR   OrthoDB; 138384at2759; -.
DR   PhylomeDB; Q8C4S8; -.
DR   TreeFam; TF320336; -.
DR   Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   BioGRID-ORCS; 209773; 7 hits in 71 CRISPR screens.
DR   ChiTaRS; Dennd2a; mouse.
DR   PRO; PR:Q8C4S8; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8C4S8; protein.
DR   Bgee; ENSMUSG00000038456; Expressed in floor plate of midbrain and 188 other tissues.
DR   ExpressionAtlas; Q8C4S8; baseline and differential.
DR   Genevisible; Q8C4S8; MM.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..1000
FT                   /note="DENN domain-containing protein 2A"
FT                   /id="PRO_0000242683"
FT   DOMAIN          559..708
FT                   /note="uDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          730..863
FT                   /note="cDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          865..960
FT                   /note="dDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          427..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        262..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..306
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         544
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        67
FT                   /note="K -> E (in Ref. 1; BAE36008)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="Q -> L (in Ref. 1; BAE39403)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        523
FT                   /note="K -> E (in Ref. 1; BAE39403)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        612
FT                   /note="A -> V (in Ref. 1; BAE22660)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        620
FT                   /note="E -> G (in Ref. 1; BAE39403)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        698
FT                   /note="A -> P (in Ref. 1; BAE22660)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1000 AA;  113094 MW;  8866696B3B25303B CRC64;
     MLEARVDMLS SNMIISGPAA DLGAKEASRP WKKQLNSVPN SGPSARARAQ PQPLSIKDKI
     SKWEGKKEPP ASDPARQTDG QEDHLPSCKV ERRGSELTRT KNGMRLETER LQNDSRARTV
     CQDTEQLPGP RPIDGQPELS QHRGRELKPS DLRFQSDHLS VLRQVKRLEK ALKDGSAGLD
     PQMPGTCYSP HCLPDKTEED LPSLESHEKG GVLAAGRRAH HLEVREPGPE ISEDWKGQES
     VYRGSRWYPP KPFINPVPKP RRTFKHAGEG DKDVSPGISF KKEKRNLPPL PSLPPPPPPL
     PSSPPPTSVN RRLWTGRQRP SADHRKSYEF EDLLQSSSEN SRVDWYAQTK LGLTRTLSEE
     NVYEDILDPP MKENPYEDVE LHGRCLGKKC VLTFPASPTS SIPDTSTKQS LSKSAFFRQN
     SERRNLKLLD TRKLSRDGAG SPLRTSPPST PSSPDDTFFN LGDLQNGRKK KKIPRLVLRI
     NAIYEARRGK KRVKRLSQST ESNSGKVTDE NSESDSDTEE KLKAHSQRLV NVKSRLKQAP
     RYSSLDRDLI EYQERQLFEY FVVVSLHKKQ AGAAYVPELT QQFPLKLEKS FKFMREAEDQ
     LKAIPQFCFP DAKDWAPVQE FTSETFSFVL TGEDGSRRFG YCRRLLPGGK GKRLPEVYCI
     VSRLGCFSLF SKILDEVEKR RGISPALVQP LMRSVMEAPF PALGKTIIVK NFLPGSGTEV
     IELCRPLDSR LEHVDFESLF SSLSVRHLVS VFASLLLERR VIFIADKLST LSKCCHAMVA
     LIYPFSWQHT YIPVLPPAMI DIVCSPTPFL IGLLSSSLPL LRELPLEEVL VVDLINDRFL
     RQMEDEDSIL PRKLQVALEH ILEQRNDLAC DQDGGPLDCV HGPESSSLSE VVSEAFVRFF
     VEIVGHYPLF LTSGEERSLQ REAFRKAVSS KSLRRFLEVF METQTFRGFI QERELRRQDA
     KGLFEVRAQE YLETLPSGEH SGVNKFLKGL GNKMKFLHKK
 
 
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