JKIP1_MOUSE
ID JKIP1_MOUSE Reviewed; 626 AA.
AC Q8BVL9; B2RS01;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Janus kinase and microtubule-interacting protein 1;
DE AltName: Full=GABA-B receptor-binding protein;
DE AltName: Full=Multiple alpha-helices and RNA-linker protein 1;
DE Short=Marlin-1;
GN Name=Jakmip1; Synonyms=Gababrbp, Marlin1;
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=Intestine;
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 TISSUE=Brain;
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 [3]
RP INTERACTION WITH GABBR1.
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 [4]
RP FUNCTION, AND INTERACTION WITH KIF5B.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
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: 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:17532644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Colocalizes with the microtubule network. Localizes to the cell
CC body and neurites of hippocampal neurons where it accumulates in
CC granules. Localizes to the tail and to a lower extent to the head of
CC sperm cells (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JAKMIP family. {ECO:0000305}.
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DR EMBL; AK077298; BAC36736.1; -; mRNA.
DR EMBL; BC138646; AAI38647.1; -; mRNA.
DR EMBL; BC138649; AAI38650.1; -; mRNA.
DR CCDS; CCDS19246.1; -.
DR RefSeq; NP_848481.2; NM_178394.4.
DR RefSeq; XP_017176628.1; XM_017321139.1.
DR AlphaFoldDB; Q8BVL9; -.
DR SMR; Q8BVL9; -.
DR BioGRID; 217944; 6.
DR IntAct; Q8BVL9; 1.
DR STRING; 10090.ENSMUSP00000038504; -.
DR iPTMnet; Q8BVL9; -.
DR PhosphoSitePlus; Q8BVL9; -.
DR EPD; Q8BVL9; -.
DR jPOST; Q8BVL9; -.
DR MaxQB; Q8BVL9; -.
DR PaxDb; Q8BVL9; -.
DR PRIDE; Q8BVL9; -.
DR ProteomicsDB; 269121; -.
DR Antibodypedia; 22639; 175 antibodies from 28 providers.
DR Ensembl; ENSMUST00000043794; ENSMUSP00000038504; ENSMUSG00000063646.
DR GeneID; 76071; -.
DR KEGG; mmu:76071; -.
DR UCSC; uc008xfh.1; mouse.
DR CTD; 152789; -.
DR MGI; MGI:1923321; Jakmip1.
DR VEuPathDB; HostDB:ENSMUSG00000063646; -.
DR eggNOG; ENOG502QS6X; Eukaryota.
DR GeneTree; ENSGT00940000153713; -.
DR HOGENOM; CLU_020294_2_0_1; -.
DR InParanoid; Q8BVL9; -.
DR OrthoDB; 143470at2759; -.
DR TreeFam; TF331900; -.
DR BioGRID-ORCS; 76071; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Jakmip1; mouse.
DR PRO; PR:Q8BVL9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BVL9; protein.
DR Bgee; ENSMUSG00000063646; Expressed in olfactory epithelium and 160 other tissues.
DR ExpressionAtlas; Q8BVL9; baseline and differential.
DR Genevisible; Q8BVL9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0050811; F:GABA receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0021756; P:striatum development; IC:GOC-OWL.
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_0000323009"
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:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96N16"
FT CONFLICT 207
FT /note="R -> G (in Ref. 1; BAC36736)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 73139 MW; EDE98EDF83AF486A CRC64;
MSKKGRSKGD KPEAETDSVQ MANEELRAKL TNIQIEFQQE KSKVGKLRER LQEAKLEREQ
EQRRHTAYIS ELKAKLHEEK TKELQALREA LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
RDGAADKVKT ALLADAREEA RRTFDGERQR LQQEILELKA ARKQAEEALS NCMQADKAKA
ADLRAAYQAH QDEVHRIKRE CERDIRRLMD EIKGKERVIL ALEKELGVQT GQTQRLLLQK
EALDEQLVQV KEAERHHSSP KRELPPGIGD MAELMGGQDQ HMDERDVRRF QLKIAELNSV
IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEELLHSI 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 PKLKFM
