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JIP1 protein

 JIP1_RAT                Reviewed;         708 AA.
Q9R237; B0VXR5; O88979; Q9R1H8; Q9WVI5; Q9WVI6;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
05-DEC-2001, sequence version 2.
12-SEP-2018, entry version 153.
RecName: Full=C-Jun-amino-terminal kinase-interacting protein 1;
Short=JIP-1;
Short=JNK-interacting protein 1;
AltName: Full=Islet-brain-1;
Short=IB-1;
AltName: Full=JIP-1-related protein;
Short=JRP;
AltName: Full=JNK MAP kinase scaffold protein 1;
AltName: Full=Mitogen-activated protein kinase 8-interacting protein 1;
Name=Mapk8ip1; Synonyms=Ib1, Jip1, Mapk8ip;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=9442013; DOI=10.1074/jbc.273.4.1843;
Bonny C., Nicod P., Waeber G.;
"IB1, a JIP-1-related nuclear protein present in insulin-secreting
cells.";
J. Biol. Chem. 273:1843-1846(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=Fischer; TISSUE=Fibroblast;
Chen Y., Talmage D.;
"JIP-1 related protein (JRP).";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=10098834; DOI=10.1046/j.1471-4159.1999.721335.x;
Kim I.-J., Lee K.-W., Park B.Y., Lee J.-K., Park J., Choi I.Y.,
Eom S.-J., Chang T.-S., Kim M.J., Yeom Y.I., Chang S.K., Lee Y.-D.,
Choi E.-J., Han P.-L.;
"Molecular cloning of multiple splicing variants of JIP-1
preferentially expressed in brain.";
J. Neurochem. 72:1335-1343(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
MAPK10.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=21076496; DOI=10.1139/y10-088;
Xu B., Zhou Y., Karmin O., Choy P.C., Pierce G.N., Siow Y.L.;
"Regulation of stress-associated scaffold proteins JIP1 and JIP3 on
the c-Jun NH2-terminal kinase in ischemia-reperfusion.";
Can. J. Physiol. Pharmacol. 88:1084-1092(2010).
[5]
INTERACTION WITH SH3RF2.
PubMed=22128169; DOI=10.1074/jbc.M111.269431;
Wilhelm M., Kukekov N.V., Schmit T.L., Biagas K.V., Sproul A.A.,
Gire S., Maes M.E., Xu Z., Greene L.A.;
"Sh3rf2/POSHER protein promotes cell survival by RING-mediated
proteasomal degradation of the c-Jun N-terminal kinase scaffold POSH
(Plenty of SH3s) protein.";
J. Biol. Chem. 287:2247-2256(2012).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-28, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[7]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 487-546, SH3 DOMAIN, AND
SUBUNIT.
PubMed=16456539; DOI=10.1038/sj.emboj.7600982;
Kristensen O., Guenat S., Dar I., Allaman-Pillet N., Abderrahmani A.,
Ferdaoussi M., Roduit R., Maurer F., Beckmann J.S., Kastrup J.S.,
Gajhede M., Bonny C.;
"A unique set of SH3-SH3 interactions controls IB1 homodimerization.";
EMBO J. 25:785-797(2006).
-!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
proteins selectively mediates JNK signaling by aggregating
specific components of the MAPK cascade to form a functional JNK
signaling module. Required for JNK activation in response to
excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-
regulated activity by retaining JNK in the cytoplasm and thus
inhibiting the JNK phosphorylation of c-Jun. May also participate
in ApoER2-specific reelin signaling. Directly, or indirectly,
regulates GLUT2 gene expression and beta-cell function. Appears to
have a role in cell signaling in mature and developing nerve
terminals. May function as a regulator of vesicle transport,
through interactions with the JNK-signaling components and motor
proteins. Functions as an anti-apoptotic protein and whose level
seems to influence the beta-cell death or survival response. Acts
as a scaffold protein that coordinates with SH3RF1 in organizing
different components of the JNK pathway, including RAC1 or RAC2,
MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or
MAPK9/JNK2 into a functional multiprotein complex to ensure the
effective activation of the JNK signaling pathway. Regulates the
activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells.
{ECO:0000250|UniProtKB:Q9WVI9, ECO:0000269|PubMed:21076496}.
-!- SUBUNIT: Forms homo- or heterooligomeric complexes
(PubMed:16456539). Binds specific components of the JNK signaling
pathway namely MAPK8/JNK1, MAPK9/JNK2, MAPK10/JNK3, MAP2K7/MKK7,
MAP3K11/MLK3 and DLK1. Also binds the proline-rich domain-
containing splice variant of apolipoprotein E receptor 2 (ApoER2).
Interacts, via the PID domain, with ARHGEF28 (By similarity).
Binds the cytoplasmic tails of LRP1 and LRP2 (Megalin). Binds the
TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-
assembled MAPK8IP1 scaffolding complexes are then transported as a
cargo of kinesin, to the required subcellular location. Interacts
with the cytoplasmic domain of APP (By similarity). Interacts with
DCLK2, VRK2 and MAP3K7/TAK1. Found in a complex with SH3RF1, RAC1,
MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1. Found in a complex with
SH3RF1, RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and MAPK9/JNK2
(By similarity). Interacts with SH3RF2 (PubMed:22128169).
{ECO:0000250|UniProtKB:Q9UQF2, ECO:0000250|UniProtKB:Q9WVI9,
ECO:0000269|PubMed:16456539, ECO:0000269|PubMed:21076496,
ECO:0000269|PubMed:22128169}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
perinuclear region {ECO:0000250}. Nucleus. Endoplasmic reticulum
membrane {ECO:0000250}. Mitochondrion membrane {ECO:0000250}.
Note=Accumulates in cell surface projections. Under certain stress
conditions, translocates to the perinuclear region of neurons. In
insulin-secreting cells, detected in both the cytoplasm and
nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=JIP-1a, JIP-1b;
IsoId=Q9R237-1; Sequence=Displayed;
Name=2; Synonyms=JIP-1c, 2A;
IsoId=Q9R237-2; Sequence=VSP_002767;
Name=3; Synonyms=JIP-1d;
IsoId=Q9R237-3; Sequence=VSP_002768, VSP_002769;
-!- TISSUE SPECIFICITY: Highly expressed in brain and pancreatic beta-
cells. Weaker expression found in kidney.
-!- DOMAIN: The SH3 domain mediates homodimerization.
-!- PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on
Thr-103 is also necessary for the dissociation and activation of
MAP3K12. Phosphorylated by VRK2. Hyperphosphorylated during
mitosis following activation of stress-activated and MAP kinases
(By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. Two preliminary events are required to prime
for ubiquitination; phosphorylation and an increased in
intracellular calcium concentration. Then, the calcium influx
initiates ubiquitination and degradation by the ubiquitin-
proteasome pathway (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the JIP scaffold family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD22543.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAD38351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF108959; AAD22543.1; ALT_INIT; mRNA.
EMBL; AF092450; AAC62110.1; -; mRNA.
EMBL; AF109772; AAD38350.1; -; mRNA.
EMBL; AF109773; AAD38351.1; ALT_INIT; mRNA.
EMBL; AF109774; AAD38352.1; -; mRNA.
EMBL; DQ377223; ABD24062.1; -; mRNA.
RefSeq; NP_446229.1; NM_053777.1. [Q9R237-2]
UniGene; Rn.44266; -.
PDB; 2FPD; X-ray; 2.05 A; A/B/C/D=487-546.
PDB; 2FPE; X-ray; 1.75 A; A/B/C/D/E/F/G/H=487-546.
PDB; 2FPF; X-ray; 3.00 A; A/B/C/D=482-552.
PDBsum; 2FPD; -.
PDBsum; 2FPE; -.
PDBsum; 2FPF; -.
ProteinModelPortal; Q9R237; -.
SMR; Q9R237; -.
IntAct; Q9R237; 6.
MINT; Q9R237; -.
STRING; 10116.ENSRNOP00000065176; -.
iPTMnet; Q9R237; -.
PhosphoSitePlus; Q9R237; -.
PaxDb; Q9R237; -.
PRIDE; Q9R237; -.
Ensembl; ENSRNOT00000079746; ENSRNOP00000074684; ENSRNOG00000058478. [Q9R237-2]
GeneID; 116457; -.
KEGG; rno:116457; -.
UCSC; RGD:70937; rat. [Q9R237-1]
CTD; 9479; -.
RGD; 70937; Mapk8ip1.
eggNOG; KOG3775; Eukaryota.
eggNOG; ENOG410ZFRJ; LUCA.
GeneTree; ENSGT00390000003908; -.
HOGENOM; HOG000231470; -.
HOVERGEN; HBG018568; -.
InParanoid; Q9R237; -.
KO; K04434; -.
OMA; KQCYSGY; -.
PhylomeDB; Q9R237; -.
TreeFam; TF325073; -.
EvolutionaryTrace; Q9R237; -.
PRO; PR:Q9R237; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000058478; Expressed in 10 organ(s), highest expression level in brain.
GO; GO:0044295; C:axonal growth cone; IDA:MGI.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0044294; C:dendritic growth cone; IDA:MGI.
GO; GO:0044302; C:dentate gyrus mossy fiber; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008432; F:JUN kinase binding; IPI:RGD.
GO; GO:0019894; F:kinesin binding; ISS:UniProtKB.
GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:RGD.
GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; IPI:RGD.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
GO; GO:0007258; P:JUN phosphorylation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0046329; P:negative regulation of JNK cascade; IMP:RGD.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:UniProtKB.
GO; GO:2000564; P:regulation of CD8-positive, alpha-beta T cell proliferation; ISS:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0016192; P:vesicle-mediated transport; IEA:Ensembl.
CDD; cd11943; SH3_JIP1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035638; JIP1_SH3.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00640; PID; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00462; PTB; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 2.
PROSITE; PS01179; PID; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Membrane; Mitochondrion; Nucleus;
Phosphoprotein; Reference proteome; Repeat; SH3 domain;
Ubl conjugation.
CHAIN 1 708 C-Jun-amino-terminal kinase-interacting
protein 1.
/FTId=PRO_0000220630.
DOMAIN 485 546 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 558 697 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 126 282 JNK-binding domain (JBD).
REGION 154 173 Minimal inhibitory domain (MID).
REGION 280 468 Interaction with MAP3K7. {ECO:0000250}.
REGION 468 657 Interaction with VRK2. {ECO:0000250}.
MOTIF 350 357 D-box 1.
MOTIF 361 369 D-box 2.
COMPBIAS 41 47 Asp/Glu-rich (acidic).
COMPBIAS 107 115 Asp/Glu-rich (acidic).
COMPBIAS 356 360 Poly-Pro.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 28 28 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 39 39 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 103 103 Phosphothreonine; by MAPK8, MAPK9 and
MAPK10. {ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 178 178 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 192 192 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 202 202 Phosphothreonine; by MAPK8, MAPK9 and
MAPK10. {ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 366 366 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 406 406 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 408 408 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 445 445 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 469 469 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
MOD_RES 470 470 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UQF2}.
VAR_SEQ 1 33 MAERESGLSGGAASPPAASPFLGLHIASPPNFR -> MQLV
LKMDSSPDNDSWLEDQWERW (in isoform 2).
{ECO:0000303|PubMed:10098834}.
/FTId=VSP_002767.
VAR_SEQ 69 93 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_002768.
VAR_SEQ 708 708 E -> EPMAQVQLQVDLEIKRAAAEQKLISEEDLNGAA
(in isoform 3). {ECO:0000303|Ref.2}.
/FTId=VSP_002769.
CONFLICT 38 38 I -> V (in Ref. 2; AAC62110).
{ECO:0000305}.
CONFLICT 149 149 S -> C (in Ref. 1; AAD22543).
{ECO:0000305}.
CONFLICT 384 384 E -> D (in Ref. 4; ABD24062).
{ECO:0000305}.
STRAND 490 492 {ECO:0000244|PDB:2FPE}.
STRAND 511 517 {ECO:0000244|PDB:2FPE}.
STRAND 521 527 {ECO:0000244|PDB:2FPE}.
TURN 528 530 {ECO:0000244|PDB:2FPE}.
STRAND 533 537 {ECO:0000244|PDB:2FPE}.
HELIX 538 540 {ECO:0000244|PDB:2FPE}.
STRAND 541 543 {ECO:0000244|PDB:2FPE}.
SEQUENCE 708 AA; 77318 MW; 4923FD55F1C511F4 CRC64;
MAERESGLSG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ
CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA SDTPGAEDDE EDDDELAAQR
PGVGPSKAES GQEPASRSQG QGQGPGTGSG DTYRPKRPTT LNLFPQVPRS QDTLNNNSLG
KKHSWQDRVS RSSSPLKTGE QTPPHEHICL SDELPPQGSP VPTQDRGTST DSPCRRTAAT
QMAPPSGPPA TAPGGRGHSH RDRIHYQADV RLEATEEIYL TPVQRPPDPA EPTSTFLPPT
ESRMSVSSDP DPAAYSVTAG RPHPSISEED EGFDCLSSPE QAEPPGGGWR GSLGEPPPPP
RASLSSDTSA LSYDSVKYTL VVDEHAQLEL VSLRPCFGDY SDESDSATVY DNCASASSPY
ESAIGEEYEE APQPRPPTCL SEDSTPDEPD VHFSKKFLNV FMSGRSRSSS AESFGLFSCV
INGEEHEQTH RAIFRFVPRH EDELELEVDD PLLVELQAED YWYEAYNMRT GARGVFPAYY
AIEVTKEPEH MAALAKNSDW IDQFRVKFLG SVQVPYHKGN DVLCAAMQKI ATTRRLTVHF
NPPSSCVLEI SVRGVKIGVK ADEAQEAKGN KCSHFFQLKN ISFCGYHPKN NKYFGFITKH
PADHRFACHV FVSEDSTKAL AESVGRAFQQ FYKQFVEYTC PTEDIYLE


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