C-Jun-amino-terminal kinase-interacting protein 1

Preferred order of sections

Names and origin

Protein names

Recommended name:
C-Jun-amino-terminal kinase-interacting protein 1
Short name=JIP-1
Short name=JNK-interacting protein 1

Alternative name(s):
Islet-brain-1
Short name=IB-1
JNK MAP kinase scaffold protein 1
Mitogen-activated protein kinase 8-interacting protein 1

Gene names

Name:	Mapk8ip1
Synonyms:	Ib1, Jip1, Mapk8ip, Prkm8ip

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.1 Ref.10
Subunit structure	Forms homo- or heterooligomeric complexes. Binds specific components of the JNK signaling pathway namely MAPK8, MAPK9, MAPK10, MAP2K7, MAP3K10, MAP3K11 and DLK1. Also binds the proline-rich domain-containing splice variant of apolipoprotein E receptor 2 (ApoER2) 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, via the PID domain, with ARHGEF28. Interacts with MAP3K7 and VRK2 By similarity. Interacts with DCLK2. Ref.6 Ref.8 Ref.9 Ref.11
Subcellular location	Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Nucleus By similarity. Endoplasmic reticulum membrane By similarity. Mitochondrion membrane By similarity. 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 By similarity. Ref.6 Ref.7
Tissue specificity	Expressed predominantly in the brain and insulin-secreting cells. In the brain, high expression found in the cerebral cortex and hippocampus. Localizes in the synaptic regions of the olfactory bulb, retina, cerebral and cerebellar cortex and hippocampus. Also expressed in a restricted number of axons, including mossy fibers from the hippocampal dentate gyrus, soma, dendrites and axons of cerebellar Purkinje cells. Also expressed in kidney, testis and prostate. Low levels in heart, ovary and small intestine. Isoform JIP-1b is more predominant in the brain than isoform JIP-1a. Isoform Jip1-a is expressed both in the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform JIP-1e are brain specific. Ref.7
Developmental stage	Low levels at prenatal stage E15, increased levels during the first postnatal days, with a plateau at postnatal day 15.
Induction	Upon neuron differentiation.
Domain	The SH3 domain mediates homodimerization By similarity.
Post-translational modification	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. 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.
Sequence similarities	Belongs to the JIP scaffold family. Contains 1 PID domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JUN phosphorylation Inferred from direct assay Ref.1. Source: MGI negative regulation of JNK cascade Inferred from electronic annotation. Source: Compara negative regulation of JUN kinase activity Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from direct assay Ref.2. Source: MGI regulation of JNK cascade Inferred from mutant phenotype Ref.10. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from direct assay Ref.1. Source: MGI vesicle-mediated transport Inferred from direct assay PubMed 16301330. Source: MGI
Cellular_component	axonal growth cone Inferred from sequence orthology Ref.7. Source: MGI cell body Inferred from direct assay Ref.7. Source: MGI cytosol Inferred from direct assay Ref.7. Source: MGI dendritic growth cone Inferred from sequence orthology Ref.7. Source: MGI dentate gyrus mossy fiber Inferred from direct assay Ref.7. Source: MGI endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay Ref.7. Source: UniProtKB mitochondrial membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from direct assay Ref.7. Source: MGI
Molecular_function	MAP-kinase scaffold activity Non-traceable author statement Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	2	EBI-288461,EBI-77613	From a different organism.
App	P12023	3	EBI-74515,EBI-78814
App	P12023-2	2	EBI-288461,EBI-286828
Lrp1	Q91ZX7	2	EBI-74515,EBI-300955
Lrp2	A2ARV4	2	EBI-74515,EBI-300875
Map3k7	Q62073	4	EBI-288464,EBI-1775345
MAPK8	P45983	2	EBI-288461,EBI-286483	From a different organism.
VRK2	Q86Y07-2	2	EBI-288464,EBI-1207636	From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform JIP-1b (identifier: Q9WVI9-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform JIP-1a (identifier: Q9WVI9-2) Also known as: 1; The sequence of this isoform differs from the canonical sequence as follows: 558-604: Missing.

Isoform JIP-1c (identifier: Q9WVI9-3) Also known as: 2a; The sequence of this isoform differs from the canonical sequence as follows: 1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW

Isoform JIP-1d (identifier: Q9WVI9-4) Also known as: 2B; The sequence of this isoform differs from the canonical sequence as follows: 1-33: MAERESGLGGGAASPPAASPFLGLHIASPPNFR → MQLVLKMDSSPDNDSWLEDQWEHW 69-93: Missing.

Isoform JIP-1e (identifier: Q9WVI9-5) Also known as: 3; The sequence of this isoform differs from the canonical sequence as follows: 1-90: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 707

707

C-Jun-amino-terminal kinase-interacting protein 1

PRO_0000220629

Regions

Domain

484 – 545

62

SH3

Domain

557 – 696

140

PID

Region

127 – 281

155

JNK-binding domain (JBD)

Region

153 – 172

20

Minimal inhibitory domain (MID)

Region

279 – 467

189

Interaction with MAP3K7 By similarity

Region

467 – 656

190

Interaction with VRK2 By similarity

Motif

349 – 356

8

D-box 1

Motif

360 – 368

9

D-box 2

Compositional bias

41 – 47

7

Asp/Glu-rich (acidic)

Compositional bias

107 – 116

10

Asp/Glu-rich (acidic)

Compositional bias

355 – 359

5

Poly-Pro

Amino acid modifications

Modified residue

39

1

Phosphoserine By similarity

Modified residue

103

1

Phosphothreonine; by MAPK8, MAPK9 and MAPK10 By similarity

Modified residue

148

1

Phosphoserine By similarity

Modified residue

177

1

Phosphoserine By similarity

Modified residue

183

1

Phosphoserine By similarity

Modified residue

189

1

Phosphoserine By similarity

Modified residue

191

1

Phosphoserine By similarity

Modified residue

192

1

Phosphoserine By similarity

Modified residue

201

1

Phosphothreonine; by MAPK8, MAPK9 and MAPK10 By similarity

Modified residue

210

1

Phosphoserine By similarity

Modified residue

307

1

Phosphoserine By similarity

Modified residue

324

1

Phosphoserine By similarity

Modified residue

326

1

Phosphoserine By similarity

Modified residue

336

1

Phosphoserine By similarity

Modified residue

351

1

Phosphoserine By similarity

Modified residue

362

1

Phosphoserine By similarity

Modified residue

365

1

Phosphoserine By similarity

Modified residue

403

1

Phosphoserine By similarity

Modified residue

405

1

Phosphoserine By similarity

Modified residue

407

1

Phosphothreonine By similarity

Modified residue

440

1

Phosphoserine By similarity

Modified residue

443

1

Phosphoserine By similarity

Modified residue

444

1

Phosphothreonine By similarity

Modified residue

465

1

Phosphoserine By similarity

Modified residue

467

1

Phosphoserine By similarity

Modified residue

468

1

Phosphoserine By similarity

Modified residue

469

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 90

90

Missing in isoform JIP-1e.

VSP_002764

Alternative sequence

1 – 33

33

MAERE…PPNFR → MQLVLKMDSSPDNDSWLEDQ WEHW in isoform JIP-1c and isoform JIP-1d.

VSP_002763

Alternative sequence

69 – 93

25

Missing in isoform JIP-1d.

VSP_002765

Alternative sequence

558 – 604

47

Missing in isoform JIP-1a.

VSP_002766

Natural variant

10

1

G → R in strain: ILS. Ref.4

Experimental info

Sequence conflict

144 – 145

2

PG → A in AAD38346. Ref.2

Sequence conflict

144 – 145

2

PG → A in AAD38347. Ref.2

Sequence conflict

144 – 145

2

PG → A in AAD38348. Ref.2

Sequence conflict

593

1

R → RP in AAD38346. Ref.2

Sequence conflict

593

1

R → RP in AAD38347. Ref.2

Sequence conflict

593

1

R → RP in AAD38348. Ref.2

Sequences

Sequence		Length	Mass (Da)
Isoform JIP-1b [UniParc]. Last modified December 5, 2001. Version 2. Checksum: 274013B12D91049D Show »	FASTA	707	77,282
10 20 30 40 50 60 MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ 70 80 90 100 110 120 CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ 130 140 150 160 170 180 RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK 190 200 210 220 230 240 KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ 250 260 270 280 290 300 MAPPSGPPAT APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE 310 320 330 340 350 360 SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG SLGEPPPPPR 370 380 390 400 410 420 ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS DESDSATVYD NCASASSPYE 430 440 450 460 470 480 SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI 490 500 510 520 530 540 NGEEHEQTHR AIFRFVPRHE DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA 550 560 570 580 590 600 IEVTKEPEHM AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN 610 620 630 640 650 660 PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN KYFGFITKHP 670 680 690 700 ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP TEDIYLE « Hide
Isoform JIP-1a (1) [UniParc]. Checksum: A303DB4A3C9A9775 Show »	FASTA	660	71,927
10 20 30 40 50 60 MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ 70 80 90 100 110 120 CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ 130 140 150 160 170 180 RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK 190 200 210 220 230 240 KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ 250 260 270 280 290 300 MAPPSGPPAT APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE 310 320 330 340 350 360 SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG SLGEPPPPPR 370 380 390 400 410 420 ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS DESDSATVYD NCASASSPYE 430 440 450 460 470 480 SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI 490 500 510 520 530 540 NGEEHEQTHR AIFRFVPRHE DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA 550 560 570 580 590 600 IEVTKEPEHM AALAKNSCVL EISVRGVKIG VKADDALEAK GNKCSHFFQL KNISFCGYHP 610 620 630 640 650 660 KNNKYFGFIT KHPADHRFAC HVFVSEDSTK ALAESVGRAF QQFYKQFVEY TCPTEDIYLE « Hide
Isoform JIP-1c (2a) [UniParc]. Checksum: 7451CE05C930E9F7 Show »	FASTA	698	77,009
10 20 30 40 50 60 MQLVLKMDSS PDNDSWLEDQ WEHWLTHDIS LEEFEDEDLS EITDECGISL QCKDTLSLRP 70 80 90 100 110 120 PRAGLLSAGS SGSAGSRLQA EMLQMDLIDA AGDTPGAEDD EEEEDDELAA QRPGVGPPKA 130 140 150 160 170 180 ESNQDPAPRS QGQGPGTGSG DTYRPKRPTT LNLFPQVPRS QDTLNNNSLG KKHSWQDRVS 190 200 210 220 230 240 RSSSPLKTGE QTPPHEHICL SDELPPQGSP VPTQDRGTST DSPCRRSAAT QMAPPSGPPA 250 260 270 280 290 300 TAPGGRGHSH RDRIHYQADV RLEATEEIYL TPVQRPPDPA EPTSTFMPPT ESRMSVSSDP 310 320 330 340 350 360 DPAAYSVTAG RPHPSISEED EGFDCLSSPE RAEPPGGGWR GSLGEPPPPP RASLSSDTSA 370 380 390 400 410 420 LSYDSVKYTL VVDEHAQLEL VSLRPCFGDY SDESDSATVY DNCASASSPY ESAIGEEYEE 430 440 450 460 470 480 APQPRPPTCL SEDSTPDEPD VHFSKKFLNV FMSGRSRSSS AESFGLFSCV INGEEHEQTH 490 500 510 520 530 540 RAIFRFVPRH EDELELEVDD PLLVELQAED YWYEAYNMRT GARGVFPAYY AIEVTKEPEH 550 560 570 580 590 600 MAALAKNSDW IDQFRVKFLG SVQVPYHKGN DVLCAAMQKI ATTRRLTVHF NPPSSCVLEI 610 620 630 640 650 660 SVRGVKIGVK ADDALEAKGN KCSHFFQLKN ISFCGYHPKN NKYFGFITKH PADHRFACHV 670 680 690 FVSEDSTKAL AESVGRAFQQ FYKQFVEYTC PTEDIYLE « Hide
Isoform JIP-1d (2B) [UniParc]. Checksum: CCB2C92E28D27E23 Show »	FASTA	673	74,585
10 20 30 40 50 60 MQLVLKMDSS PDNDSWLEDQ WEHWLTHDIS LEEFEDEDLS EITDECGISL QCKDTLSLRM 70 80 90 100 110 120 DLIDAAGDTP GAEDDEEEED DELAAQRPGV GPPKAESNQD PAPRSQGQGP GTGSGDTYRP 130 140 150 160 170 180 KRPTTLNLFP QVPRSQDTLN NNSLGKKHSW QDRVSRSSSP LKTGEQTPPH EHICLSDELP 190 200 210 220 230 240 PQGSPVPTQD RGTSTDSPCR RSAATQMAPP SGPPATAPGG RGHSHRDRIH YQADVRLEAT 250 260 270 280 290 300 EEIYLTPVQR PPDPAEPTST FMPPTESRMS VSSDPDPAAY SVTAGRPHPS ISEEDEGFDC 310 320 330 340 350 360 LSSPERAEPP GGGWRGSLGE PPPPPRASLS SDTSALSYDS VKYTLVVDEH AQLELVSLRP 370 380 390 400 410 420 CFGDYSDESD SATVYDNCAS ASSPYESAIG EEYEEAPQPR PPTCLSEDST PDEPDVHFSK 430 440 450 460 470 480 KFLNVFMSGR SRSSSAESFG LFSCVINGEE HEQTHRAIFR FVPRHEDELE LEVDDPLLVE 490 500 510 520 530 540 LQAEDYWYEA YNMRTGARGV FPAYYAIEVT KEPEHMAALA KNSDWIDQFR VKFLGSVQVP 550 560 570 580 590 600 YHKGNDVLCA AMQKIATTRR LTVHFNPPSS CVLEISVRGV KIGVKADDAL EAKGNKCSHF 610 620 630 640 650 660 FQLKNISFCG YHPKNNKYFG FITKHPADHR FACHVFVSED STKALAESVG RAFQQFYKQF 670 VEYTCPTEDI YLE « Hide
Isoform JIP-1e (3) [UniParc]. Checksum: A22DC803C3DB62DF Show »	FASTA	617	68,005
10 20 30 40 50 60 MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD 70 80 90 100 110 120 TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS 130 140 150 160 170 180 DELPPQGSPV PTQDRGTSTD SPCRRSAATQ MAPPSGPPAT APGGRGHSHR DRIHYQADVR 190 200 210 220 230 240 LEATEEIYLT PVQRPPDPAE PTSTFMPPTE SRMSVSSDPD PAAYSVTAGR PHPSISEEDE 250 260 270 280 290 300 GFDCLSSPER AEPPGGGWRG SLGEPPPPPR ASLSSDTSAL SYDSVKYTLV VDEHAQLELV 310 320 330 340 350 360 SLRPCFGDYS DESDSATVYD NCASASSPYE SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV 370 380 390 400 410 420 HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI NGEEHEQTHR AIFRFVPRHE DELELEVDDP 430 440 450 460 470 480 LLVELQAEDY WYEAYNMRTG ARGVFPAYYA IEVTKEPEHM AALAKNSDWI DQFRVKFLGS 490 500 510 520 530 540 VQVPYHKGND VLCAAMQKIA TTRRLTVHFN PPSSCVLEIS VRGVKIGVKA DDALEAKGNK 550 560 570 580 590 600 CSHFFQLKNI SFCGYHPKNN KYFGFITKHP ADHRFACHVF VSEDSTKALA ESVGRAFQQF 610 YKQFVEYTCP TEDIYLE « Hide

References

[1]	"A cytoplasmic inhibitor of the JNK signal transduction pathway." Dickens M., Rogers J.S., Cavanagh J., Raitano A., Xia Z., Halpern J.R., Greenberg M.E., Sawyers C.L., Davis R.J. Science 277:693-696(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1A), POSSIBLE FUNCTION. Tissue: Brain.
[2]	"Molecular cloning of multiple splicing variants of JIP-1 preferentially expressed in brain." 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. J. Neurochem. 72:1335-1343(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JIP-1B; JIP-1C; JIP-1D AND JIP-1E). Strain: BALB/c. Tissue: Brain.
[3]	"The JIP group of mitogen-activated protein kinase scaffold proteins." Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J. Mol. Cell. Biol. 19:7245-7254(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), CHARACTERIZATION. Tissue: Brain.
[4]	"High-throughput sequence identification of gene coding variants within alcohol-related QTLs." Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M. Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), VARIANT ARG-10. Strain: ILS and ISS.
[5]	"Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade." Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T. J. Biol. Chem. 277:20070-20078(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B). Tissue: Brain.
[6]	"Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons." Meyer D., Liu A., Margolis B. J. Biol. Chem. 274:35113-35118(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGEF28, SUBCELLULAR LOCATION.
[7]	"Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain." Pellet J.-B., Haefliger J.-A., Staple J.K., Widmann C., Welker E., Hirling H., Bonny C., Nicod P., Catsicas S., Waeber G., Riederer B.M. Eur. J. Neurosci. 12:621-632(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[8]	"Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction." Gotthardt M., Trommsdorff M., Nevitt M.F., Shelton J., Richardson J.A., Stockinger W., Nimpf J., Herz J. J. Biol. Chem. 275:25616-25624(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LRPS.
[9]	"Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules." Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J., Rapoport T.A., Margolis B. J. Cell Biol. 152:959-970(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KLC1. Tissue: Brain.
[10]	"Requirement of the JIP1 scaffold protein for stress-induced JNK activation." Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F., Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A., Rakic P., Davis R.J. Genes Dev. 15:2421-2432(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Common and divergent roles for members of the mouse DCX superfamily." Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T., Brody Y., Orr I., Barkai N., Eichele G., Reiner O. Cell Cycle 5:976-983(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCLK2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF003115 mRNA. Translation: AAB66317.1.
AF109768 mRNA. Translation: AAD38346.1.
AF109769 mRNA. Translation: AAD38347.1.
AF109770 mRNA. Translation: AAD38348.1.
AF109771 mRNA. Translation: AAD38349.1.
AF054611 mRNA. Translation: AAD22580.1.
AF332075 mRNA. Translation: AAK56103.1.
AF332076 mRNA. Translation: AAK56104.1.

IPI

IPI00230316.
IPI00230317.
IPI00230318.
IPI00321873.
IPI00465532.

PIR

T03038.

RefSeq

NP_035292.2. NM_011162.5.

UniGene

Mm.2720.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UKH	X-ray	2.35	B	153-163	[»]
1UKI	X-ray	2.70	B	153-163	[»]
3O17	X-ray	3.00	F/G	154-163	[»]
3O2M	X-ray	2.70	F/G	154-163	[»]
3V3V	X-ray	2.70	B	153-163	[»]

ProteinModelPortal

Q9WVI9.

SMR

Q9WVI9. Positions 486-545.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9WVI9. 15 interactions.

MINT

MINT-126863.

STRING

10090.ENSMUSP00000050773.

PTM databases

PhosphoSite

Q9WVI9.

Proteomic databases

PaxDb

Q9WVI9.

PRIDE

Q9WVI9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223.
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223.

GeneID

19099.

KEGG

mmu:19099.

UCSC

uc008kxw.2. mouse.

Organism-specific databases

CTD

9479.

MGI

MGI:1309464. Mapk8ip1.

Phylogenomic databases

eggNOG

NOG266073.

GeneTree

ENSGT00390000003908.

HOVERGEN

HBG018568.

InParanoid

Q9WVI9.

KO

K04434.

OMA

SPCRRSA.

OrthoDB

EOG4BP1BD.

Gene expression databases

ArrayExpress

Q9WVI9.

Bgee

Q9WVI9.

Genevestigator

Q9WVI9.

GermOnline

ENSMUSG00000027223. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR006020. PTyr_interaction_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00640. PID. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS01179. PID. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

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Other

EvolutionaryTrace

Q9WVI9.

NextBio

295662.

SOURCE

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Entry information

Entry name

JIP1_MOUSE

Accession

Primary (citable) accession number: Q9WVI9
Secondary accession number(s): O35145

Q9WVI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	December 5, 2001
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents