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JKIP1_RAT
ID   JKIP1_RAT               Reviewed;         626 AA.
AC   Q3SWS9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Janus kinase and microtubule-interacting protein 1;
DE   AltName: Full=Multiple alpha helices and RNA-linker protein 1;
DE            Short=Marlin-1;
GN   Name=Jakmip1; Synonyms=Marlin1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis, and Thymus;
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   [2]
RP   INTERACTION WITH GABBR1, TOPOLOGY, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA   Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA   Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT   "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL   J. Biol. Chem. 279:13934-13943(2004).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17532644; DOI=10.1016/j.mcn.2007.04.008;
RA   Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S.,
RA   Couve A.;
RT   "Marlin-1 and conventional kinesin link GABAB receptors to the cytoskeleton
RT   and regulate receptor transport.";
RL   Mol. Cell. Neurosci. 35:501-512(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, INTERACTION WITH GABABR1, AND TISSUE SPECIFICITY.
RX   PubMed=17668444; DOI=10.1002/jcb.21456;
RA   Vidal R.L., Ramirez A., Castro M., Concha I.I., Couve A.;
RT   "Marlin-1 is expressed in testis and associates to the cytoskeleton and
RT   GABA(B) receptors.";
RL   J. Cell. Biochem. 103:886-895(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Associates with microtubules and may play a role in the
CC       microtubule-dependent transport of the GABA-B receptor. May play a role
CC       in JAK1 signaling and regulate microtubule cytoskeleton rearrangements.
CC       {ECO:0000269|PubMed:17532644}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with JAK1 and TYK2 (By
CC       similarity). Forms a complex with GABBR1 and KIF5B/kinesin-1.
CC       {ECO:0000250, ECO:0000269|PubMed:14718537,
CC       ECO:0000269|PubMed:17668444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Membrane; Peripheral
CC       membrane protein. Note=Colocalizes with the microtubule network.
CC       Localizes to the cell body and neurites of hippocampal neurons where it
CC       accumulates in granules. Localizes to the tail and to a lower extent to
CC       the head of sperm cells.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain and testis by
CC       spermatogonia, spermatocytes, spermatozoa and Sertoli cells (at protein
CC       level). {ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:17668444}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JAKMIP family. {ECO:0000305}.
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DR   EMBL; BC104677; AAI04678.1; -; mRNA.
DR   EMBL; BC104718; AAI04719.1; -; mRNA.
DR   RefSeq; NP_001029066.1; NM_001033894.1.
DR   AlphaFoldDB; Q3SWS9; -.
DR   SMR; Q3SWS9; -.
DR   STRING; 10116.ENSRNOP00000006771; -.
DR   iPTMnet; Q3SWS9; -.
DR   PhosphoSitePlus; Q3SWS9; -.
DR   jPOST; Q3SWS9; -.
DR   PaxDb; Q3SWS9; -.
DR   PRIDE; Q3SWS9; -.
DR   GeneID; 305434; -.
DR   KEGG; rno:305434; -.
DR   CTD; 152789; -.
DR   RGD; 1562401; Jakmip1.
DR   VEuPathDB; HostDB:ENSRNOG00000004998; -.
DR   eggNOG; ENOG502QS6X; Eukaryota.
DR   HOGENOM; CLU_020294_2_0_1; -.
DR   InParanoid; Q3SWS9; -.
DR   OMA; IEEKHSF; -.
DR   OrthoDB; 727914at2759; -.
DR   PhylomeDB; Q3SWS9; -.
DR   TreeFam; TF331900; -.
DR   PRO; PR:Q3SWS9; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000004998; Expressed in frontal cortex and 15 other tissues.
DR   Genevisible; Q3SWS9; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISO:RGD.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISO:RGD.
DR   GO; GO:0050811; F:GABA receptor binding; ISO:RGD.
DR   GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR   GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISO:RGD.
DR   GO; GO:0050890; P:cognition; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024836; JAKMIP.
DR   InterPro; IPR031994; JAKMIP_C.
DR   PANTHER; PTHR18935; PTHR18935; 1.
DR   Pfam; PF16034; JAKMIP_CC3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..626
FT                   /note="Janus kinase and microtubule-interacting protein 1"
FT                   /id="PRO_0000323010"
FT   REGION          1..365
FT                   /note="Mediates association with microtubules"
FT                   /evidence="ECO:0000250"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          365..626
FT                   /note="Mediates interaction with TYK2 and GABBR1"
FT                   /evidence="ECO:0000250"
FT   REGION          452..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          13..255
FT                   /evidence="ECO:0000255"
FT   COILED          284..413
FT                   /evidence="ECO:0000255"
FT   COILED          490..604
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96N16"
FT   MOD_RES         470
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96N16"
SQ   SEQUENCE   626 AA;  73107 MW;  1EF2D3C42DFA552B CRC64;
     MSKKGRSKGE KPETETDSVQ MANEELRAKL TNIQIEFQQE KSKVGKLRER LQEAKLEREQ
     EQRRHTAYIS ELKAKLHEEK TKELQALREA LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
     RDGAADKVKT ALLADAREEA RRTFDGERQR LQQEILELKA ARKQAEEALS NCMQADKAKA
     ADLRAAYQAH QDEVHRIKRE CERDIRRLMD EIKGKERVIL ALEKELGVQA GQTQRLLLQK
     EALDEQLVQV KEAERHHSSP KRELPPGIGD MAELMGGQDQ HMDERDVRRF QLKIAELNSV
     IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEDLLHSI QRMEEKLKSL
     TRENVEMKEK LSAQASLKRH TSLNDLSLTR DEQEIEFLRL QVLEQQHVID DLSLERERLL
     RSKRHRGKSL KPPKKHVVET FFGFDEESVD SETLSETSYN TDRTDRTPAT PEEDLDETTT
     REEADLRFCQ LTREYQALQR AYALLQEQVG GTLDAEREAR TREQLQADLL RCQAKIEDLE
     KLLVEKGQDA AWVEEKQVLM RTNQDLLEKI YRLEMEENQL KSEMQDAKDQ NELLEFRVLE
     LEVRDSICCK LSNGADILFE PKLKFV
 
 
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