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Q58A65 (JIP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Spag9
Synonyms:Jip4, Jsap2, Kiaa0516, Mapk8ip4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1321 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.1 Ref.2

Subunit structure

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. Ref.1 Ref.2 Ref.8

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Note: Perinuclear distribution in response to stress signals such as UV radiation. Ref.1 Ref.2

Tissue specificity

Isoform 6 is highly expressed in brain, kidney, liver, heart. Ref.2

Induction

Up-regulated during neuronal differentiation. Ref.8

Post-translational modification

Phosphorylated by MAPK8 and MAPK14. Ref.2

Sequence similarities

Belongs to the JIP scaffold family.

Sequence caution

The sequence BAD32239.1 differs from that shown. Reason: Erroneous initiation.

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

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Inferred from direct assay Ref.1. Source: MGI

activation of MAPK activity

Inferred from direct assay Ref.2. Source: MGI

negative regulation of protein homodimerization activity

Inferred from direct assay Ref.1. Source: MGI

positive regulation of MAPK cascade

Inferred from genetic interaction PubMed 20004020. Source: MGI

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 19244314. Source: MGI

protein homooligomerization

Inferred from direct assay Ref.2. Source: MGI

retrograde transport, endosome to Golgi

Inferred from electronic annotation. Source: Ensembl

striated muscle cell differentiation

Inferred from genetic interaction PubMed 20160094. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: MGI

cytosol

Traceable author statement. Source: Reactome

perinuclear region of cytoplasm

Inferred from direct assay PubMed 19056739. Source: MGI

   Molecular_functionJUN kinase binding

Inferred from direct assay Ref.1Ref.2. Source: MGI

kinesin binding

Inferred from direct assay Ref.2. Source: MGI

mitogen-activated protein kinase p38 binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Arf6P6233110EBI-6530207,EBI-988682
LRRK2Q5S0072EBI-6530207,EBI-5323863From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q58A65-1)

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 2 (identifier: Q58A65-2)

The sequence of this isoform differs from the canonical sequence as follows:
     248-261: Missing.
Isoform 3 (identifier: Q58A65-3)

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.
Isoform 4 (identifier: Q58A65-4)

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.
Isoform 5 (identifier: Q58A65-5)

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.
Isoform 6 (identifier: Q58A65-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13211321C-Jun-amino-terminal kinase-interacting protein 4
PRO_0000234077

Regions

Coiled coil66 – 166101 Potential
Coiled coil408 – 534127 By similarity
Coiled coil724 – 75835 Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1091Phosphoserine By similarity
Modified residue1831Phosphoserine By similarity
Modified residue1851Phosphoserine By similarity
Modified residue1941Phosphoserine By similarity
Modified residue2031Phosphoserine By similarity
Modified residue2171Phosphothreonine Ref.10
Modified residue2511Phosphoserine By similarity
Modified residue2651Phosphoserine By similarity
Modified residue2681Phosphoserine By similarity
Modified residue2721Phosphoserine By similarity
Modified residue3111Phosphoserine By similarity
Modified residue3291Phosphoserine By similarity
Modified residue3321Phosphoserine By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3481Phosphothreonine By similarity
Modified residue3651Phosphothreonine Ref.10
Modified residue4181Phosphothreonine By similarity
Modified residue5861Phosphothreonine By similarity
Modified residue7301Phosphoserine By similarity
Modified residue7331Phosphoserine Ref.9

Natural variations

Alternative sequence1 – 165165Missing in isoform 6.
VSP_018225
Alternative sequence1 – 143143Missing in isoform 3 and isoform 4.
VSP_018226
Alternative sequence144 – 19653RLEER…AHSRI → MNPGCMLLFVFGFVGGAVVI NSAILVSLSVLLLVHFSIST GVPALTQNLPRIL in isoform 3, isoform 4 and isoform 5.
VSP_018227
Alternative sequence248 – 26114Missing in isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.
VSP_018228
Alternative sequence4051G → GEYSG in isoform 3.
VSP_018229
Alternative sequence11751T → TVILHQGRLLGLRA in isoform 4.
VSP_018230

Experimental info

Sequence conflict2411R → C in AAN61564. Ref.1
Sequence conflict4531E → A in AAN61564. Ref.1
Sequence conflict4681E → G in BAE27980. Ref.5
Sequence conflict7051S → T in BAD93176. Ref.3
Sequence conflict11141L → P in BAE27907. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: 93A6E97A62E0E92C

FASTA1,321146,219
        10         20         30         40         50         60 
MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN 

        70         80         90        100        110        120 
LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR 

       130        140        150        160        170        180 
VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH 

       190        200        210        220        230        240 
QLSGSDQLEA TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP 

       250        260        270        280        290        300 
RSHTSLKVSH SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG 

       310        320        330        340        350        360 
FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE LDMDKDLSGY 

       370        380        390        400        410        420 
KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL 

       430        440        450        460        470        480 
LETKNALNVV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEDKNRELE EELRKARAEA 

       490        500        510        520        530        540 
EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE 

       550        560        570        580        590        600 
NPAMQEKKRS SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP 

       610        620        630        640        650        660 
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVANG 

       670        680        690        700        710        720 
QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDIAGLD 

       730        740        750        760        770        780 
TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN QEELSSQVWI CTSTHSTTKV IIIDAVQPGN 

       790        800        810        820        830        840 
ILDSFTVCNS HVLCIASVPG ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG 

       850        860        870        880        890        900 
GITVVGCSTE GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG 

       910        920        930        940        950        960 
STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV LPNEQDLARE 

       970        980        990       1000       1010       1020 
EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG 

      1030       1040       1050       1060       1070       1080 
TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK 

      1090       1100       1110       1120       1130       1140 
SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK 

      1150       1160       1170       1180       1190       1200 
LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK 

      1210       1220       1230       1240       1250       1260 
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA DKAGSSAQEP 

      1270       1280       1290       1300       1310       1320 
SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMCGN 


E 

« Hide

Isoform 2 [UniParc].

Checksum: 8C99195A5AFFC7BF
Show »

FASTA1,307144,704
Isoform 3 [UniParc].

Checksum: 34B7E6B2D81B7DF9
Show »

FASTA1,168127,680
Isoform 4 [UniParc].

Checksum: 730D991D29C5A74B
Show »

FASTA1,177128,672
Isoform 5 [UniParc].

Checksum: F186D445467EE5B6
Show »

FASTA1,307143,835
Isoform 6 [UniParc].

Checksum: 16184E1CE2BF26A1
Show »

FASTA1,142125,350

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001020599.1. NM_001025428.1.
NP_001020600.1. NM_001025429.1.
NP_001020601.1. NM_001025430.1.
NP_001186132.1. NM_001199203.1.
NP_001186133.1. NM_001199204.1.
NP_001186134.1. NM_001199205.1.
NP_081845.2. NM_027569.2.
XP_006534282.1. XM_006534219.1.
UniGeneMm.260737.

3D structure databases

ProteinModelPortalQ58A65.
SMRQ58A65. Positions 406-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214283. 5 interactions.
IntActQ58A65. 3 interactions.
MINTMINT-1351345.
STRING10090.ENSMUSP00000099458.

PTM databases

PhosphoSiteQ58A65.

Proteomic databases

PaxDbQ58A65.
PRIDEQ58A65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041956; ENSMUSP00000042271; ENSMUSG00000020859. [Q58A65-2]
ENSMUST00000075695; ENSMUSP00000075115; ENSMUSG00000020859. [Q58A65-3]
ENSMUST00000103168; ENSMUSP00000099457; ENSMUSG00000020859.
GeneID70834.
KEGGmmu:70834.
UCSCuc007kxx.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

CTD9043.
MGIMGI:1918084. Spag9.
RougeSearch...

Phylogenomic databases

eggNOGNOG270333.
GeneTreeENSGT00670000097546.
HOVERGENHBG024110.
InParanoidQ58A65.
OMAGSDQLES.
OrthoDBEOG7GXP9P.
PhylomeDBQ58A65.
TreeFamTF313096.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressQ58A65.
BgeeQ58A65.
CleanExMM_SPAG9.
GenevestigatorQ58A65.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR019143. JNK/Rab-associated_protein-1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF09744. Jnk-SapK_ap_N. 1 hit.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSPAG9. mouse.
NextBio332372.
PROQ58A65.
SOURCESearch...

Entry information

Entry nameJIP4_MOUSE
AccessionPrimary (citable) accession number: Q58A65
Secondary accession number(s): Q3UH77 expand/collapse secondary AC list , Q3UHF0, Q58VQ4, Q5NC70, Q5NC78, Q6A057, Q6PAS3, Q8CJC2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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