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Q58A65

- JIP4_MOUSE

UniProt

Q58A65 - JIP4_MOUSE

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Protein

C-Jun-amino-terminal kinase-interacting protein 4

Gene

Spag9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. JUN kinase binding Source: MGI
  2. kinesin binding Source: MGI
  3. mitogen-activated protein kinase p38 binding Source: MGI

GO - Biological processi

  1. activation of JUN kinase activity Source: MGI
  2. activation of MAPK activity Source: MGI
  3. negative regulation of protein homodimerization activity Source: MGI
  4. positive regulation of cell migration Source: Ensembl
  5. positive regulation of MAPK cascade Source: MGI
  6. positive regulation of neuron differentiation Source: MGI
  7. protein homooligomerization Source: MGI
  8. retrograde transport, endosome to Golgi Source: Ensembl
  9. striated muscle cell differentiation Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
C-Jun-amino-terminal kinase-interacting protein 4
Short name:
JIP-4
Short name:
JNK-interacting protein 4
Alternative name(s):
JNK-associated leucine-zipper protein
Short name:
JLP
JNK/SAPK-associated protein 2
Short name:
JSAP2
Mitogen-activated protein kinase 8-interacting protein 4
Sperm-associated antigen 9
Gene namesi
Name:Spag9
Synonyms:Jip4, Jsap2, Kiaa0516, Mapk8ip4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1918084. Spag9.

Subcellular locationi

Cytoplasm. Cytoplasmperinuclear region
Note: Perinuclear distribution in response to stress signals such as UV radiation.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. perinuclear region of cytoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13211321C-Jun-amino-terminal kinase-interacting protein 4PRO_0000234077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei109 – 1091PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity
Modified residuei194 – 1941PhosphoserineBy similarity
Modified residuei203 – 2031PhosphoserineBy similarity
Modified residuei217 – 2171Phosphothreonine1 Publication
Modified residuei251 – 2511PhosphoserineBy similarity
Modified residuei265 – 2651PhosphoserineBy similarity
Modified residuei268 – 2681PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineBy similarity
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei329 – 3291PhosphoserineBy similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei348 – 3481PhosphothreonineBy similarity
Modified residuei365 – 3651Phosphothreonine1 Publication
Modified residuei418 – 4181PhosphothreonineBy similarity
Modified residuei586 – 5861PhosphothreonineBy similarity
Modified residuei730 – 7301PhosphoserineBy similarity
Modified residuei733 – 7331Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by MAPK8 and MAPK14.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ58A65.
PaxDbiQ58A65.
PRIDEiQ58A65.

PTM databases

PhosphoSiteiQ58A65.

Expressioni

Tissue specificityi

Isoform 6 is highly expressed in brain, kidney, liver, heart.1 Publication

Inductioni

Up-regulated during neuronal differentiation.1 Publication

Gene expression databases

BgeeiQ58A65.
CleanExiMM_SPAG9.
ExpressionAtlasiQ58A65. baseline and differential.
GenevestigatoriQ58A65.

Interactioni

Subunit structurei

Homodimer. The homodimer interacts with ARF6, forming a heterotetramer By similarity. Homooligomer. Interacts with MAX, MAPK8, MAPK14, MAPK10, MAPK14, MAP3K3, MYC, KNS2, and MAP2K4. Interaction with KNS2 is important in the formation of ternary complex with MAPK8.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arf6P6233110EBI-6530207,EBI-988682
LRRK2Q5S0072EBI-6530207,EBI-5323863From a different organism.

Protein-protein interaction databases

BioGridi214283. 5 interactions.
IntActiQ58A65. 3 interactions.
MINTiMINT-1351345.
STRINGi10090.ENSMUSP00000099458.

Structurei

3D structure databases

ProteinModelPortaliQ58A65.
SMRiQ58A65. Positions 406-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili66 – 166101Sequence AnalysisAdd
BLAST
Coiled coili408 – 534127By similarityAdd
BLAST
Coiled coili724 – 75835Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the JIP scaffold family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG270333.
GeneTreeiENSGT00670000097546.
HOVERGENiHBG024110.
InParanoidiQ58A65.
OMAiGSDQLES.
OrthoDBiEOG7GXP9P.
PhylomeDBiQ58A65.
TreeFamiTF313096.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR019143. JNK/Rab-associated_protein-1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF09744. Jnk-SapK_ap_N. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q58A65-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL
60 70 80 90 100
MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE
110 120 130 140 150
EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA
160 170 180 190 200
ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLEA TAHSRIRKER
210 220 230 240 250
PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP RSHTSLKVSH
260 270 280 290 300
SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG
310 320 330 340 350
FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE
360 370 380 390 400
LDMDKDLSGY KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG
410 420 430 440 450
ADLLGMGREV ENLILENTQL LETKNALNVV KNDLIAKVDE LTCEKDVLQG
460 470 480 490 500
ELEAVKQAKL KLEDKNRELE EELRKARAEA EDARQKAKDD DDSDIPTAQR
510 520 530 540 550
KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE NPAMQEKKRS
560 570 580 590 600
SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
610 620 630 640 650
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL
660 670 680 690 700
PQKYKQVANG QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT
710 720 730 740 750
RDGGSVVGAS VFYKDIAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN
760 770 780 790 800
QEELSSQVWI CTSTHSTTKV IIIDAVQPGN ILDSFTVCNS HVLCIASVPG
810 820 830 840 850
ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG GITVVGCSTE
860 870 880 890 900
GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG
910 920 930 940 950
STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV
960 970 980 990 1000
LPNEQDLARE EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK
1010 1020 1030 1040 1050
DSILSIVHVK GIVLVALADG TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI
1060 1070 1080 1090 1100
RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK SFDAHPRKES QVRQLAWVGD
1110 1120 1130 1140 1150
GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK LGFSFVRITA
1160 1170 1180 1190 1200
LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK
1210 1220 1230 1240 1250
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA
1260 1270 1280 1290 1300
DKAGSSAQEP SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE
1310 1320
PSVTKAERSH LIVWQVMCGN E
Length:1,321
Mass (Da):146,219
Last modified:May 2, 2006 - v2
Checksum:i93A6E97A62E0E92C
GO
Isoform 2 (identifier: Q58A65-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-261: Missing.

Show »
Length:1,307
Mass (Da):144,704
Checksum:i8C99195A5AFFC7BF
GO
Isoform 3 (identifier: Q58A65-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.
     144-196: RLEEREAELK...QLEATAHSRI → MNPGCMLLFV...ALTQNLPRIL
     248-261: Missing.
     405-405: G → GEYSG

Note: No experimental confirmation available.

Show »
Length:1,168
Mass (Da):127,680
Checksum:i34B7E6B2D81B7DF9
GO
Isoform 4 (identifier: Q58A65-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.
     144-196: RLEEREAELK...QLEATAHSRI → MNPGCMLLFV...ALTQNLPRIL
     248-261: Missing.
     1175-1175: T → TVILHQGRLLGLRA

Note: No experimental confirmation available.

Show »
Length:1,177
Mass (Da):128,672
Checksum:i730D991D29C5A74B
GO
Isoform 5 (identifier: Q58A65-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     144-196: RLEEREAELK...QLEATAHSRI → MNPGCMLLFV...ALTQNLPRIL
     248-261: Missing.

Note: No experimental confirmation available.

Show »
Length:1,307
Mass (Da):143,835
Checksum:iF186D445467EE5B6
GO
Isoform 6 (identifier: Q58A65-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-165: Missing.
     248-261: Missing.

Show »
Length:1,142
Mass (Da):125,350
Checksum:i16184E1CE2BF26A1
GO

Sequence cautioni

The sequence BAD32239.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAI35376.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti241 – 2411R → C in AAN61564. (PubMed:12391307)Curated
Sequence conflicti453 – 4531E → A in AAN61564. (PubMed:12391307)Curated
Sequence conflicti468 – 4681E → G in BAE27980. (PubMed:16141072)Curated
Sequence conflicti705 – 7051S → T in BAD93176. 1 PublicationCurated
Sequence conflicti1114 – 11141L → P in BAE27907. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 165165Missing in isoform 6. 1 PublicationVSP_018225Add
BLAST
Alternative sequencei1 – 143143Missing in isoform 3 and isoform 4. 2 PublicationsVSP_018226Add
BLAST
Alternative sequencei144 – 19653RLEER…AHSRI → MNPGCMLLFVFGFVGGAVVI NSAILVSLSVLLLVHFSIST GVPALTQNLPRIL in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_018227Add
BLAST
Alternative sequencei248 – 26114Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6. 5 PublicationsVSP_018228Add
BLAST
Alternative sequencei405 – 4051G → GEYSG in isoform 3. 1 PublicationVSP_018229
Alternative sequencei1175 – 11751T → TVILHQGRLLGLRA in isoform 4. 1 PublicationVSP_018230

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF327451 mRNA. Translation: AAN61564.1.
AY823270 mRNA. Translation: AAX19462.1.
AB047782 mRNA. Translation: BAD93176.1.
AK172961 mRNA. Translation: BAD32239.1. Different initiation.
AK147431 mRNA. Translation: BAE27907.1.
AK147537 mRNA. Translation: BAE27980.1.
AL662838 Genomic DNA. Translation: CAI35367.1.
AL662838 Genomic DNA. Translation: CAI35375.1.
AL662838 Genomic DNA. Translation: CAI35376.1. Sequence problems.
BC060100 mRNA. Translation: AAH60100.1.
BC094670 mRNA. Translation: AAH94670.1.
CCDSiCCDS25248.1. [Q58A65-2]
CCDS56797.1. [Q58A65-3]
RefSeqiNP_001020599.1. NM_001025428.1.
NP_001020600.1. NM_001025429.1. [Q58A65-3]
NP_001020601.1. NM_001025430.1.
NP_001186132.1. NM_001199203.1.
NP_001186133.1. NM_001199204.1.
NP_001186134.1. NM_001199205.1. [Q58A65-4]
NP_081845.2. NM_027569.2. [Q58A65-2]
XP_006534282.1. XM_006534219.1. [Q58A65-6]
UniGeneiMm.260737.

Genome annotation databases

EnsembliENSMUST00000041956; ENSMUSP00000042271; ENSMUSG00000020859. [Q58A65-2]
ENSMUST00000075695; ENSMUSP00000075115; ENSMUSG00000020859. [Q58A65-3]
ENSMUST00000103168; ENSMUSP00000099457; ENSMUSG00000020859.
GeneIDi70834.
KEGGimmu:70834.
UCSCiuc007kxx.1. mouse. [Q58A65-2]
uc007kxy.1. mouse. [Q58A65-1]
uc007kxz.1. mouse. [Q58A65-6]
uc007kya.1. mouse. [Q58A65-3]
uc007kyc.1. mouse. [Q58A65-5]
uc007kyd.1. mouse. [Q58A65-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF327451 mRNA. Translation: AAN61564.1 .
AY823270 mRNA. Translation: AAX19462.1 .
AB047782 mRNA. Translation: BAD93176.1 .
AK172961 mRNA. Translation: BAD32239.1 . Different initiation.
AK147431 mRNA. Translation: BAE27907.1 .
AK147537 mRNA. Translation: BAE27980.1 .
AL662838 Genomic DNA. Translation: CAI35367.1 .
AL662838 Genomic DNA. Translation: CAI35375.1 .
AL662838 Genomic DNA. Translation: CAI35376.1 . Sequence problems.
BC060100 mRNA. Translation: AAH60100.1 .
BC094670 mRNA. Translation: AAH94670.1 .
CCDSi CCDS25248.1. [Q58A65-2 ]
CCDS56797.1. [Q58A65-3 ]
RefSeqi NP_001020599.1. NM_001025428.1.
NP_001020600.1. NM_001025429.1. [Q58A65-3 ]
NP_001020601.1. NM_001025430.1.
NP_001186132.1. NM_001199203.1.
NP_001186133.1. NM_001199204.1.
NP_001186134.1. NM_001199205.1. [Q58A65-4 ]
NP_081845.2. NM_027569.2. [Q58A65-2 ]
XP_006534282.1. XM_006534219.1. [Q58A65-6 ]
UniGenei Mm.260737.

3D structure databases

ProteinModelPortali Q58A65.
SMRi Q58A65. Positions 406-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 214283. 5 interactions.
IntActi Q58A65. 3 interactions.
MINTi MINT-1351345.
STRINGi 10090.ENSMUSP00000099458.

PTM databases

PhosphoSitei Q58A65.

Proteomic databases

MaxQBi Q58A65.
PaxDbi Q58A65.
PRIDEi Q58A65.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041956 ; ENSMUSP00000042271 ; ENSMUSG00000020859 . [Q58A65-2 ]
ENSMUST00000075695 ; ENSMUSP00000075115 ; ENSMUSG00000020859 . [Q58A65-3 ]
ENSMUST00000103168 ; ENSMUSP00000099457 ; ENSMUSG00000020859 .
GeneIDi 70834.
KEGGi mmu:70834.
UCSCi uc007kxx.1. mouse. [Q58A65-2 ]
uc007kxy.1. mouse. [Q58A65-1 ]
uc007kxz.1. mouse. [Q58A65-6 ]
uc007kya.1. mouse. [Q58A65-3 ]
uc007kyc.1. mouse. [Q58A65-5 ]
uc007kyd.1. mouse. [Q58A65-4 ]

Organism-specific databases

CTDi 9043.
MGIi MGI:1918084. Spag9.
Rougei Search...

Phylogenomic databases

eggNOGi NOG270333.
GeneTreei ENSGT00670000097546.
HOVERGENi HBG024110.
InParanoidi Q58A65.
OMAi GSDQLES.
OrthoDBi EOG7GXP9P.
PhylomeDBi Q58A65.
TreeFami TF313096.

Miscellaneous databases

ChiTaRSi SPAG9. mouse.
NextBioi 332372.
PROi Q58A65.
SOURCEi Search...

Gene expression databases

Bgeei Q58A65.
CleanExi MM_SPAG9.
ExpressionAtlasi Q58A65. baseline and differential.
Genevestigatori Q58A65.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR019143. JNK/Rab-associated_protein-1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF09744. Jnk-SapK_ap_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
    Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.
    Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH MAX; MAPK8; MAPK14; MAP3K3; MYC AND MAP2K4, SUBCELLULAR LOCATION.
  2. "Role of the JIP4 scaffold protein in the regulation of mitogen-activated protein kinase signaling pathways."
    Kelkar N., Standen C.L., Davis R.J.
    Mol. Cell. Biol. 25:2733-2743(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, INTERACTION WITH KNS2 AND MAPK8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Strain: C57BL/6J.
    Tissue: Testis.
  3. "JSAP2, a novel member of the JSAP1 JNK scaffold protein family."
    Takamatsu N., Tochigi M., Ito M., Odama Y., Xu P., Nakabeppu Y., Yoshioka K., Shiba T.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Strain: C57BL/6J.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: C57BL/6J.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Strain: C57BL/6.
    Tissue: Brain and Olfactory epithelium.
  8. "JLP associates with kinesin light chain 1 through a novel leucine zipper-like domain."
    Nguyen Q., Lee C.M., Le A., Reddy E.P.
    J. Biol. Chem. 280:30185-30191(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KNS2, INDUCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiJIP4_MOUSE
AccessioniPrimary (citable) accession number: Q58A65
Secondary accession number(s): Q3UH77
, Q3UHF0, Q58VQ4, Q5NC70, Q5NC78, Q6A057, Q6PAS3, Q8CJC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: October 29, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3