ID   JIP4_MOUSE              Reviewed;        1321 AA.
AC   Q58A65; Q3UH77; Q3UHF0; Q58VQ4; Q5NC70; Q5NC78; Q6A057; Q6PAS3; Q8CJC2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE            Short=JIP-4;
DE            Short=JNK-interacting protein 4;
DE   AltName: Full=JNK-associated leucine-zipper protein;
DE            Short=JLP;
DE   AltName: Full=JNK/SAPK-associated protein 2;
DE            Short=JSAP2;
DE   AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE   AltName: Full=Sperm-associated antigen 9;
GN   Name=Spag9 {ECO:0000312|MGI:MGI:1918084};
GN   Synonyms=Jip4, Jsap2, Kiaa0516, Mapk8ip4;
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 [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH MAX;
RP   MAPK8; MAPK14; MAP3K3; MYC AND MAP2K4, AND SUBCELLULAR LOCATION.
RX   PubMed=12391307; DOI=10.1073/pnas.232310199;
RA   Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT   "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and
RT   transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, INTERACTION WITH KNS2 AND
RP   MAPK8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=15767678; DOI=10.1128/mcb.25.7.2733-2743.2005;
RA   Kelkar N., Standen C.L., Davis R.J.;
RT   "Role of the JIP4 scaffold protein in the regulation of mitogen-activated
RT   protein kinase signaling pathways.";
RL   Mol. Cell. Biol. 25:2733-2743(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Takamatsu N., Tochigi M., Ito M., Odama Y., Xu P., Nakabeppu Y.,
RA   Yoshioka K., Shiba T.;
RT   "JSAP2, a novel member of the JSAP1 JNK scaffold protein family.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Olfactory epithelium;
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   [8]
RP   INTERACTION WITH KNS2, AND INDUCTION.
RX   PubMed=15987681; DOI=10.1074/jbc.m505499200;
RA   Nguyen Q., Lee C.M., Le A., Reddy E.P.;
RT   "JLP associates with kinesin light chain 1 through a novel leucine zipper-
RT   like domain.";
RL   J. Biol. Chem. 280:30185-30191(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   FUNCTION, INTERACTION WITH PIKFYVE, AND SUBCELLULAR LOCATION.
RX   PubMed=19056739; DOI=10.1074/jbc.m806539200;
RA   Ikonomov O.C., Fligger J., Sbrissa D., Dondapati R., Mlak K., Deeb R.,
RA   Shisheva A.;
RT   "Kinesin adapter JLP links PIKfyve to microtubule-based endosome-to-trans-
RT   Golgi network traffic of furin.";
RL   J. Biol. Chem. 284:3750-3761(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217; THR-292 AND
RP   SER-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, 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: The JNK-interacting protein (JIP) group of scaffold proteins
CC       selectively mediates JNK signaling by aggregating specific components
CC       of the MAPK cascade to form a functional JNK signaling module
CC       (PubMed:12391307, PubMed:15767678). Regulates lysosomal positioning by
CC       acting as an adapter protein which links PIP4P1-positive lysosomes to
CC       the dynein-dynactin complex (By similarity). Assists PIKFYVE selective
CC       functionality in microtubule-based endosome-to-TGN trafficking
CC       (PubMed:19056739). {ECO:0000250|UniProtKB:O60271,
CC       ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678,
CC       ECO:0000269|PubMed:19056739}.
CC   -!- SUBUNIT: Homodimer (By similarity). The homodimer interacts with ARF6,
CC       forming a heterotetramer (By similarity). Homooligomer (By similarity).
CC       Interacts with MAX, MAPK8, MAPK14, MAP3K3, MYC, and MAP2K4
CC       (PubMed:12391307). Interacts with KNS2 (PubMed:15987681). Interaction
CC       with KNS2 is important in the formation of ternary complex with MAPK8
CC       (PubMed:15767678). Interacts with PIP4P1 (By similarity). Interacts
CC       with PIKFYVE (PubMed:19056739). {ECO:0000250|UniProtKB:O60271,
CC       ECO:0000269|PubMed:12391307, ECO:0000269|PubMed:15767678,
CC       ECO:0000269|PubMed:15987681, ECO:0000269|PubMed:19056739}.
CC   -!- INTERACTION:
CC       Q58A65; P62331: Arf6; NbExp=10; IntAct=EBI-6530207, EBI-988682;
CC       Q58A65; Q5S007: LRRK2; Xeno; NbExp=2; IntAct=EBI-6530207, EBI-5323863;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12391307,
CC       ECO:0000269|PubMed:15767678, ECO:0000269|PubMed:19056739}. Cytoplasm,
CC       perinuclear region {ECO:0000269|PubMed:12391307,
CC       ECO:0000269|PubMed:19056739}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:O60271}. Note=Perinuclear distribution in
CC       response to stress signals such as UV radiation.
CC       {ECO:0000269|PubMed:12391307}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=JLP(L) {ECO:0000303|PubMed:19056739};
CC         IsoId=Q58A65-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q58A65-2; Sequence=VSP_018228;
CC       Name=3;
CC         IsoId=Q58A65-3; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC                                  VSP_018229;
CC       Name=4;
CC         IsoId=Q58A65-4; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC                                  VSP_018230;
CC       Name=5;
CC         IsoId=Q58A65-5; Sequence=VSP_018227, VSP_018228;
CC       Name=6;
CC         IsoId=Q58A65-6; Sequence=VSP_018225, VSP_018228;
CC   -!- TISSUE SPECIFICITY: [Isoform 6]: Highly expressed in brain, kidney,
CC       liver, heart. {ECO:0000269|PubMed:15767678}.
CC   -!- INDUCTION: Up-regulated during neuronal differentiation.
CC       {ECO:0000269|PubMed:15987681}.
CC   -!- PTM: Phosphorylated by MAPK8 and MAPK14. {ECO:0000269|PubMed:15767678}.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32239.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAI35376.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF327451; AAN61564.1; -; mRNA.
DR   EMBL; AY823270; AAX19462.1; -; mRNA.
DR   EMBL; AB047782; BAD93176.1; -; mRNA.
DR   EMBL; AK172961; BAD32239.1; ALT_INIT; mRNA.
DR   EMBL; AK147431; BAE27907.1; -; mRNA.
DR   EMBL; AK147537; BAE27980.1; -; mRNA.
DR   EMBL; AL662838; CAI35367.1; -; Genomic_DNA.
DR   EMBL; AL662838; CAI35375.1; -; Genomic_DNA.
DR   EMBL; AL662838; CAI35376.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC060100; AAH60100.1; -; mRNA.
DR   EMBL; BC094670; AAH94670.1; -; mRNA.
DR   CCDS; CCDS25248.1; -. [Q58A65-2]
DR   CCDS; CCDS56797.1; -. [Q58A65-3]
DR   RefSeq; NP_001020599.1; NM_001025428.1.
DR   RefSeq; NP_001020600.1; NM_001025429.1. [Q58A65-3]
DR   RefSeq; NP_001020601.1; NM_001025430.1.
DR   RefSeq; NP_001186132.1; NM_001199203.1.
DR   RefSeq; NP_001186133.1; NM_001199204.1.
DR   RefSeq; NP_001186134.1; NM_001199205.1. [Q58A65-4]
DR   RefSeq; NP_081845.2; NM_027569.2. [Q58A65-2]
DR   RefSeq; XP_006534282.1; XM_006534219.2.
DR   AlphaFoldDB; Q58A65; -.
DR   SMR; Q58A65; -.
DR   BioGRID; 214283; 18.
DR   IntAct; Q58A65; 2.
DR   MINT; Q58A65; -.
DR   STRING; 10090.ENSMUSP00000042271; -.
DR   GlyGen; Q58A65; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q58A65; -.
DR   PhosphoSitePlus; Q58A65; -.
DR   SwissPalm; Q58A65; -.
DR   EPD; Q58A65; -.
DR   jPOST; Q58A65; -.
DR   MaxQB; Q58A65; -.
DR   PaxDb; 10090-ENSMUSP00000042271; -.
DR   PeptideAtlas; Q58A65; -.
DR   ProteomicsDB; 268911; -. [Q58A65-1]
DR   ProteomicsDB; 268912; -. [Q58A65-2]
DR   ProteomicsDB; 268913; -. [Q58A65-3]
DR   ProteomicsDB; 268914; -. [Q58A65-4]
DR   ProteomicsDB; 268915; -. [Q58A65-5]
DR   ProteomicsDB; 268916; -. [Q58A65-6]
DR   Pumba; Q58A65; -.
DR   Antibodypedia; 30731; 246 antibodies from 36 providers.
DR   DNASU; 70834; -.
DR   Ensembl; ENSMUST00000041956.14; ENSMUSP00000042271.8; ENSMUSG00000020859.17. [Q58A65-2]
DR   Ensembl; ENSMUST00000075695.13; ENSMUSP00000075115.7; ENSMUSG00000020859.17. [Q58A65-3]
DR   GeneID; 70834; -.
DR   KEGG; mmu:70834; -.
DR   UCSC; uc007kxx.1; mouse. [Q58A65-2]
DR   UCSC; uc007kxy.1; mouse. [Q58A65-1]
DR   UCSC; uc007kxz.1; mouse. [Q58A65-6]
DR   UCSC; uc007kya.1; mouse. [Q58A65-3]
DR   UCSC; uc007kyc.1; mouse. [Q58A65-5]
DR   UCSC; uc007kyd.1; mouse. [Q58A65-4]
DR   AGR; MGI:1918084; -.
DR   CTD; 9043; -.
DR   MGI; MGI:1918084; Spag9.
DR   VEuPathDB; HostDB:ENSMUSG00000020859; -.
DR   eggNOG; KOG2077; Eukaryota.
DR   GeneTree; ENSGT00940000153496; -.
DR   InParanoid; Q58A65; -.
DR   OMA; MEYIERT; -.
DR   OrthoDB; 3685563at2759; -.
DR   PhylomeDB; Q58A65; -.
DR   TreeFam; TF313096; -.
DR   Reactome; R-MMU-525793; Myogenesis.
DR   BioGRID-ORCS; 70834; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Spag9; mouse.
DR   PRO; PR:Q58A65; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q58A65; Protein.
DR   Bgee; ENSMUSG00000020859; Expressed in otolith organ and 232 other cell types or tissues.
DR   ExpressionAtlas; Q58A65; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0008432; F:JUN kinase binding; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:MGI.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR   GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR   GO; GO:1903860; P:negative regulation of dendrite extension; ISO:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.20.58.1770; -; 1.
DR   Gene3D; 1.20.5.1000; arf6 gtpase in complex with a specific effector, jip4; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR039911; JIP3/JIP4.
DR   InterPro; IPR032486; JIP_LZII.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR034743; RH1.
DR   InterPro; IPR034744; RH2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13886:SF2; C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 4; 1.
DR   PANTHER; PTHR13886; JNK/SAPK-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF16471; JIP_LZII; 1.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   Pfam; PF19056; WD40_2; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS51776; RH1; 1.
DR   PROSITE; PS51777; RH2; 1.
DR   Genevisible; Q58A65; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Lysosome;
KW   Membrane; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1321
FT                   /note="C-Jun-amino-terminal kinase-interacting protein 4"
FT                   /id="PRO_0000234077"
FT   DOMAIN          7..95
FT                   /note="RH1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01112"
FT   DOMAIN          500..604
FT                   /note="RH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01113"
FT   REGION          203..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          853..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1239..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          66..166
FT                   /evidence="ECO:0000255"
FT   COILED          408..534
FT                   /evidence="ECO:0000250"
FT   COILED          724..758
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        222..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         185
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         194
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         203
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19131326,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         268
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         272
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         292
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         347
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         348
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         365
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19131326"
FT   MOD_RES         418
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         586
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         588
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         595
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         705
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         728
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         730
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         732
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         733
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   MOD_RES         1264
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O60271"
FT   VAR_SEQ         1..165
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15767678"
FT                   /id="VSP_018225"
FT   VAR_SEQ         1..143
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018226"
FT   VAR_SEQ         144..196
FT                   /note="RLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSGSDQLEATAHSR
FT                   I -> MNPGCMLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALTQNLPRIL
FT                   (in isoform 3, isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018227"
FT   VAR_SEQ         248..261
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT                   5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12391307,
FT                   ECO:0000303|PubMed:15368895, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:15767678, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018228"
FT   VAR_SEQ         405
FT                   /note="G -> GEYSG (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15368895"
FT                   /id="VSP_018229"
FT   VAR_SEQ         1175
FT                   /note="T -> TVILHQGRLLGLRA (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018230"
FT   CONFLICT        241
FT                   /note="R -> C (in Ref. 1; AAN61564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        453
FT                   /note="E -> A (in Ref. 1; AAN61564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="E -> G (in Ref. 5; BAE27980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        705
FT                   /note="S -> T (in Ref. 3; BAD93176)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1114
FT                   /note="L -> P (in Ref. 5; BAE27907)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1321 AA;  146219 MW;  93A6E97A62E0E92C CRC64;
     MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
     LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
     VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
     QLSGSDQLEA TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP
     RSHTSLKVSH SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG
     FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE LDMDKDLSGY
     KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
     LETKNALNVV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEDKNRELE EELRKARAEA
     EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
     NPAMQEKKRS SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
     GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVANG
     QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDIAGLD
     TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN QEELSSQVWI CTSTHSTTKV IIIDAVQPGN
     ILDSFTVCNS HVLCIASVPG ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG
     GITVVGCSTE GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG
     STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV LPNEQDLARE
     EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
     TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
     SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
     LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK
     VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA DKAGSSAQEP
     SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMCGN
     E
//