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O60271 (JIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
Cancer/testis antigen 89
Short name=CT89
Human lung cancer oncogene 6 protein
Short name=HLC-6
JNK-associated leucine-zipper protein
Short name=JLP
Mitogen-activated protein kinase 8-interacting protein 4
Proliferation-inducing protein 6
Protein highly expressed in testis
Short name=PHET
Sperm surface protein
Sperm-associated antigen 9
Sperm-specific protein
Sunday driver 1
Gene names
Name:SPAG9
Synonyms:HSS, KIAA0516, MAPK8IP4, SYD1
ORF Names:HLC6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Isoform 5 may play a role in spermatozoa-egg-interaction. Ref.11 Ref.12

Subunit structure

Homodimer. The homodimer interacts with ARF6, forming a heterotetramer. Homooligomer. Interacts with MAX, MAPK8, MAPK9, MAPK10, MAPK14, MAP3K3, MYC, KNS2 and MAP2K4. Interaction with KNS2 is important in the formation of ternary complex with MAPK8. Interacts with NFKB1. Ref.11 Ref.12 Ref.23

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Note: Perinuclear distribution in response to stress signals such as UV radiation. Ref.9 Ref.12

Isoform 5: Cytoplasmic vesiclesecretory vesicleacrosome. Note: Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix. Ref.9 Ref.12

Tissue specificity

Isoform 5 is expressed only in testis on the round spermatids of stage I, II and II. Isoform 5 is absent in spermatogonia and spermatocyte. Isoform 3 is expressed in testis. Isoform 4 is expressed in testis and in acute myeloid leukemia (AML) patients. Ref.2 Ref.8 Ref.9

Induction

Isoform 3 is increased in systemic sclerosis fibroblasts. Ref.9

Post-translational modification

Phosphorylated by MAPK8 and MAPK14 By similarity.

Sequence similarities

Belongs to the JIP scaffold family.

Sequence caution

The sequence AAH07524.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAH59946.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAI06049.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

The sequence AAO66462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAA25442.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB14812.1 differs from that shown. Reason: Unlikely isoform. Aberrant splicing.

The sequence CAA62987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoplasmic vesicle
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

muscle cell differentiation

Traceable author statement. Source: Reactome

negative regulation of protein homodimerization activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from mutant phenotype PubMed 18826971. Source: UniProtKB

positive regulation of muscle cell differentiation

Traceable author statement. Source: Reactome

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

retrograde transport, endosome to Golgi

Inferred from direct assay PubMed 19056739. Source: MGI

spermatogenesis

Traceable author statement Ref.8. Source: ProtInc

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of membrane

Traceable author statement Ref.8. Source: ProtInc

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARF1P840773EBI-1023301,EBI-447171
ARF6P623308EBI-1023301,EBI-638181
Arf6P623312EBI-1023301,EBI-988682From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60271-1)

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: O60271-2)

The sequence of this isoform differs from the canonical sequence as follows:
     248-261: Missing.
     555-555: F → FVPTR
Isoform 3 (identifier: O60271-3)

The sequence of this isoform differs from the canonical sequence as follows:
     938-945: SNDSDAYK → RYNNGSST
     946-1321: Missing.
Note: Due to intron retention.
Isoform 4 (identifier: O60271-4)

The sequence of this isoform differs from the canonical sequence as follows:
     248-261: Missing.
Isoform 5 (identifier: O60271-5)

The sequence of this isoform differs from the canonical sequence as follows:
     248-261: Missing.
     938-945: SNDSDAYK → RYNNGSST
     946-1321: Missing.
Isoform 6 (identifier: O60271-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: MELEDGVVYQ...QLESTAHSRI → MSPGCMLLFV...ALTQNLPRIL
     248-261: Missing.
     1175-1175: T → TVILHQGRLLGLRA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13211321C-Jun-amino-terminal kinase-interacting protein 4
PRO_0000234076

Regions

Coiled coil66 – 166101 Potential
Coiled coil408 – 534127 Ref.23
Coiled coil724 – 75835 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17 Ref.22
Modified residue1091Phosphoserine Ref.14
Modified residue1831Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue1851Phosphoserine Ref.16 Ref.21
Modified residue1941Phosphoserine Ref.19
Modified residue2031Phosphoserine Ref.13 Ref.18 Ref.19
Modified residue2171Phosphothreonine Ref.13 Ref.16 Ref.18 Ref.19
Modified residue2511Phosphoserine Ref.19
Modified residue2651Phosphoserine Ref.14 Ref.19
Modified residue2681Phosphoserine Ref.19
Modified residue2721Phosphoserine Ref.14 Ref.19
Modified residue3111Phosphoserine Ref.16
Modified residue3291Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue3321Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue3471Phosphoserine Ref.19
Modified residue3481Phosphothreonine Ref.19
Modified residue3651Phosphothreonine By similarity
Modified residue4181Phosphothreonine Ref.14 Ref.16 Ref.19
Modified residue5861Phosphothreonine Ref.16
Modified residue7301Phosphoserine Ref.19
Modified residue7331Phosphoserine Ref.16 Ref.18 Ref.19

Natural variations

Alternative sequence1 – 196196MELED…AHSRI → MSPGCMLLFVFGFVGGAVVI NSAILVSLSVLLLVHFSIST GVPALTQNLPRIL in isoform 6.
VSP_042253
Alternative sequence248 – 26114Missing in isoform 2, isoform 4, isoform 5 and isoform 6.
VSP_018214
Alternative sequence5551F → FVPTR in isoform 2.
VSP_018220
Alternative sequence938 – 9458SNDSDAYK → RYNNGSST in isoform 3 and isoform 5.
VSP_018221
Alternative sequence946 – 1321376Missing in isoform 3 and isoform 5.
VSP_018222
Alternative sequence11751T → TVILHQGRLLGLRA in isoform 6.
VSP_042254
Natural variant13201N → S.
Corresponds to variant rs9896965 [ dbSNP | Ensembl ].
VAR_059364

Experimental info

Sequence conflict4511E → G in AAO66462. Ref.9
Sequence conflict6801E → K in CAA62987. Ref.8
Sequence conflict6801E → K in AAO66462. Ref.9
Isoform 6:
Sequence conflict91F → S in BAG58134. Ref.5

Secondary structure

... 1321
Helix Strand Turn

Details...

Sequences

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

Last modified May 2, 2006. Version 4.
Checksum: 5CAE349FBDF91B40

FASTA1,321146,205
        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 
QLSGSDQLES TAHSRIRKER PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP 

       250        260        270        280        290        300 
RSHTSLKVSN SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG 

       310        320        330        340        350        360 
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE LDMDKDLSGY 

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

       430        440        450        460        470        480 
LETKNALNIV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEEKNRELE EELRKARAEA 

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

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

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

       670        680        690        700        710        720 
QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDVAGLD 

       730        740        750        760        770        780 
TEGSKQRSAS QSSLDKLDQE LKEQQKELKN QEELSSLVWI CTSTHSATKV LIIDAVQPGN 

       790        800        810        820        830        840 
ILDSFTVCNS HVLCIASVPG ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG 

       850        860        870        880        890        900 
GITVVGCSAE GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG 

       910        920        930        940        950        960 
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV LPNEQDLVRE 

       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 VPGNRPGSVI RVYGDENSDK 

      1210       1220       1230       1240       1250       1260 
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG DKAGPSAQEP 

      1270       1280       1290       1300       1310       1320 
GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMYGN 


E 

« Hide

Isoform 2 [UniParc].

Checksum: D60A544D70BD1F97
Show »

FASTA1,311145,135
Isoform 3 [UniParc].

Checksum: EB17642AA2BF0BB4
Show »

FASTA945104,736
Isoform 4 [UniParc].

Checksum: 55B30E422A8ABD0E
Show »

FASTA1,307144,682
Isoform 5 [UniParc].

Checksum: 1A427D7B60367814
Show »

FASTA931103,212
Isoform 6 [UniParc].

Checksum: 8CD074A547DCC690
Show »

FASTA1,177128,607

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).
Tissue: Liver.
[2]"Humoral detection of leukaemia-associated antigens in presentation acute myeloid leukaemia."
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., Wells J.W., Banham A.H., Mufti G.J.
Biochem. Biophys. Res. Commun. 335:1293-1304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
[3]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
Tissue: Brain and Testis.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-478 (ISOFORMS 2/4/5).
Tissue: Eye and Kidney.
[8]"Cloning of a novel human testis mRNA specifically expressed in testicular haploid germ cells, having unique palindromic sequences and encoding a leucine zipper dimerization motif."
Shankar S., Mohapatra B., Suri A.
Biochem. Biophys. Res. Commun. 243:561-565(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-1321 (ISOFORM 5), TISSUE SPECIFICITY.
Tissue: Testis.
[9]"A novel protein highly expressed in testis is overexpressed in systemic sclerosis fibroblasts and targeted by autoantibodies."
Yasuoka H., Ihn H., Medsger T.A. Jr., Hirakata M., Kawakami Y., Ikeda Y., Kuwana M.
J. Immunol. 171:6883-6890(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-1321 (ISOFORM 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
Tissue: Testis.
[10]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway."
Bouwmeester T., Bauch A., Ruffner H., Angrand P.-O., Bergamini G., Croughton K., Cruciat C., Eberhard D., Gagneur J., Ghidelli S., Hopf C., Huhse B., Mangano R., Michon A.-M., Schirle M., Schlegl J., Schwab M., Stein M.A. expand/collapse author list , Bauer A., Casari G., Drewes G., Gavin A.-C., Jackson D.B., Joberty G., Neubauer G., Rick J., Kuster B., Superti-Furga G.
Nat. Cell Biol. 6:97-105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NFKB1.
[12]"Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein."
Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.
Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAPK9; MAPK10 AND MAPK8, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-265; SER-272 AND THR-418, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; THR-217; SER-311; SER-329; SER-332; THR-418; THR-586 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; THR-217 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-194; SER-203; THR-217; SER-251; SER-265; SER-268; SER-272; SER-329; SER-332; SER-347; THR-348; THR-418; SER-730 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-185; SER-329 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The structural basis of Arf effector specificity: the crystal structure of ARF6 in a complex with JIP4."
Isabet T., Montagnac G., Regazzoni K., Raynal B., El Khadali F., England P., Franco M., Chavrier P., Houdusse A., Menetrey J.
EMBO J. 28:2835-2845(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 406-476 IN COMPLEX WITH ARF6, COILED COIL, SUBUNIT, INTERACTION WITH ARF6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF327452 mRNA. Translation: AAN61565.1.
AY850123 mRNA. Translation: AAX47276.1.
AB011088 mRNA. Translation: BAA25442.3. Different initiation.
AK024068 mRNA. Translation: BAB14812.1. Sequence problems.
AK295098 mRNA. Translation: BAG58134.1.
AK302789 mRNA. Translation: BAG63993.1.
AC005920 Genomic DNA. No translation available.
AC005839 Genomic DNA. No translation available.
BC007524 mRNA. Translation: AAH07524.1. Sequence problems.
BC059946 mRNA. Translation: AAH59946.1. Sequence problems.
BC106048 mRNA. Translation: AAI06049.1. Sequence problems.
BC146755 mRNA. Translation: AAI46756.1.
BC153878 mRNA. Translation: AAI53879.1.
X91879 mRNA. Translation: CAA62987.1. Different initiation.
AY219897 mRNA. Translation: AAO66462.1. Different initiation.
AY219898 mRNA. Translation: AAO66463.1.
PIRJC5958.
RefSeqNP_001123999.1. NM_001130527.2.
NP_001124000.1. NM_001130528.2.
NP_001238900.1. NM_001251971.1.
NP_003962.3. NM_003971.5.
UniGeneHs.463439.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W83X-ray1.93C/D406-476[»]
ProteinModelPortalO60271.
SMRO60271. Positions 406-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114505. 27 interactions.
IntActO60271. 9 interactions.
MINTMINT-1136008.

PTM databases

PhosphoSiteO60271.

Proteomic databases

PaxDbO60271.
PRIDEO60271.

Protocols and materials databases

DNASU9043.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262013; ENSP00000262013; ENSG00000008294. [O60271-1]
ENST00000357122; ENSP00000349636; ENSG00000008294. [O60271-4]
ENST00000505279; ENSP00000426900; ENSG00000008294. [O60271-2]
ENST00000510283; ENSP00000423165; ENSG00000008294. [O60271-9]
GeneID9043.
KEGGhsa:9043.
UCSCuc002ita.3. human. [O60271-9]
uc002itb.3. human. [O60271-4]
uc002itc.3. human. [O60271-1]
uc002itd.3. human. [O60271-2]
uc002ite.3. human. [O60271-3]
uc002itf.3. human. [O60271-5]

Organism-specific databases

CTD9043.
GeneCardsGC17M049039.
HGNCHGNC:14524. SPAG9.
HPAHPA040446.
MIM605430. gene.
neXtProtNX_O60271.
PharmGKBPA37890.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270333.
HOGENOMHOG000290716.
HOVERGENHBG024110.
InParanoidO60271.
OMAGSDQLES.
OrthoDBEOG7GXP9P.
PhylomeDBO60271.
TreeFamTF313096.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkO60271.

Gene expression databases

ArrayExpressO60271.
BgeeO60271.
GenevestigatorO60271.

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. human.
EvolutionaryTraceO60271.
GeneWikiSPAG9.
GenomeRNAi9043.
NextBio33871.
PMAP-CutDBO60271.
PROO60271.
SOURCESearch...

Entry information

Entry nameJIP4_HUMAN
AccessionPrimary (citable) accession number: O60271
Secondary accession number(s): A6H8U5 expand/collapse secondary AC list , A8MSX0, B4DHH2, O60905, Q3KQU8, Q3MKM7, Q86WC7, Q86WC8, Q8IZX7, Q96II0, Q9H811
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 115 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM