Reviewed, UniProtKB/Swiss-Prot Q9WVI9 (JIP1_MOUSE)

Names and origin

Protein names

Recommended name:
    C-jun-amino-terminal kinase-interacting protein 1
      Short name=JNK-interacting protein 1
      Short name=JIP-1
Alternative name(s):
    JNK MAP kinase scaffold protein 1
    Islet-brain-1
      Short name=IB-1
    Mitogen-activated protein kinase 8-interacting protein 1

Gene names

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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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 interations 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 RGNEF. Ref.6 Ref.8 Ref.9
Subcellular location	Cytoplasm By similarity. Cytoplasm › perinuclear region By similarity. Nucleus 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.
Post-translational modification	Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on Thr-103 is also necessary for the dissociation and activation of MAP3K12. 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 Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat SH3 domain
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	JUN phosphorylation Ref.1 Inferred from direct assay. Source: MGI anti-apoptosis Ref.2 Inferred from direct assay. Source: MGI regulation of transcription, DNA-dependent Ref.1 Inferred from direct assay. Source: MGI vesicle-mediated transport Inferred from direct assay. Source: MGI
Cellular component	membrane Ref.7 Inferred from direct assay. Source: UniProtKB neuron projection Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	MAP-kinase scaffold activity Ref.10 Non-traceable author statement. Source: UniProtKB kinesin binding Ref.9 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	1	EBI-288461,EBI-77613	From a different organism.
App	P12023	2	EBI-288461,EBI-78814
App	P12023	2	EBI-74515,EBI-78814
App	P12023-2	1	EBI-288461,EBI-286828
Appl	P14599	1	EBI-74515,EBI-74135	From a different organism.
bsk	P92208	1	EBI-74515,EBI-74487	From a different organism.
Lrp1	Q91ZX7	1	EBI-74515,EBI-300955
Map3k7	Q62073	1	EBI-288464,EBI-1775345
MAPK8	P45983	1	EBI-288461,EBI-286483	From a different organism.
VRK2	Q86Y07-1	1	EBI-288464,EBI-1207633	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)
	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	103	1	Phosphothreonine; by MAPK8, MAPK9 and MAPK10 By similarity
	Modified residue	201	1	Phosphothreonine; by MAPK8, MAPK9 and MAPK10 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	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
	Isoform JIP-1a (1). Checksum: A303DB4A3C9A9775	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
	Isoform JIP-1c (2a). Checksum: 7451CE05C930E9F7	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
	Isoform JIP-1d (2B). Checksum: CCB2C92E28D27E23	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
	Isoform JIP-1e (3). Checksum: A22DC803C3DB62DF	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

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: 9235893] [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: 10098834] [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: 10490659] [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: 11471062] [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: 11912189] [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: 10574993] [Abstract] Cited for: INTERACTION WITH RGNEF, 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: 10712642] [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: 10827173] [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: 11238452] [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: 11562351] [Abstract] Cited for: FUNCTION.
+	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.

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	[»]

SMR

Q9WVI9. Positions 485-544, 561-696.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9WVI9. 20 interactions.

STRING

Q9WVI9.

PTM databases

PhosphoSite

Q9WVI9.

Proteomic databases

PRIDE

Q9WVI9.

Genome annotation databases

Ensembl

ENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223; Mus musculus. [Genome view]
ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223; Mus musculus. [Genome view]

GeneID

19099.

KEGG

mmu:19099.

UCSC

uc008kxv.1. mouse.
uc008kxw.1. mouse.
uc008kxx.1. mouse.

Organism-specific databases

CTD

19099.

MGI

MGI:1309464. Mapk8ip1.

Phylogenomic databases

HOVERGEN

Q9WVI9.

InParanoid

Q9WVI9.

OMA

GRGHSHR.

OrthoDB

EOG9GQSQT.

PhylomeDB

Q9WVI9.

Gene expression databases

ArrayExpress

Q9WVI9.

Bgee

Q9WVI9.

Genevestigator

Q9WVI9.

GermOnline

ENSMUSG00000027223. Mus musculus.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.30.29.30. PH_type. 1 hit.

Pfam

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

SMART

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

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

295662.

SOURCE

Search...

Entry information

Entry name

JIP1_MOUSE

Accession

Primary (citable) accession number: Q9WVI9
Secondary accession number(s): O35145 , Q925J8, Q9R1H9, Q9R1Z1, Q9WVI7, Q9WVI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	December 5, 2001
Last modified:	January 19, 2010
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)