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O60271

- JIP4_HUMAN

UniProt

O60271 - JIP4_HUMAN

Protein

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

Gene

SPAG9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 4 (02 May 2006)
      Previous versions | rss
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    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. Isoform 5 may play a role in spermatozoa-egg-interaction.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. activation of JUN kinase activity Source: Ensembl
    2. muscle cell differentiation Source: Reactome
    3. negative regulation of protein homodimerization activity Source: Ensembl
    4. positive regulation of cell migration Source: UniProtKB
    5. positive regulation of muscle cell differentiation Source: Reactome
    6. positive regulation of neuron differentiation Source: Ensembl
    7. protein homooligomerization Source: Ensembl
    8. retrograde transport, endosome to Golgi Source: MGI
    9. spermatogenesis Source: ProtInc
    10. striated muscle cell differentiation Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_21402. CDO in myogenesis.
    SignaLinkiO60271.

    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):
    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 namesi
    Name:SPAG9
    Synonyms:HSS, KIAA0516, MAPK8IP4, SYD1
    ORF Names:HLC6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14524. SPAG9.

    Subcellular locationi

    Cytoplasm. Cytoplasmperinuclear region
    Note: Perinuclear distribution in response to stress signals such as UV radiation.
    Isoform 5 : Cytoplasmic vesiclesecretory vesicleacrosome
    Note: Associated with the plasma membrane of the acrosomal compartment and also localizes in the acrosome matrix.

    GO - Cellular componenti

    1. acrosomal vesicle Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of membrane Source: ProtInc
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37890.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13211321C-Jun-amino-terminal kinase-interacting protein 4PRO_0000234076Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Modified residuei109 – 1091Phosphoserine1 Publication
    Modified residuei183 – 1831Phosphoserine3 Publications
    Modified residuei185 – 1851Phosphoserine2 Publications
    Modified residuei194 – 1941Phosphoserine1 Publication
    Modified residuei203 – 2031Phosphoserine3 Publications
    Modified residuei217 – 2171Phosphothreonine4 Publications
    Modified residuei251 – 2511Phosphoserine1 Publication
    Modified residuei265 – 2651Phosphoserine2 Publications
    Modified residuei268 – 2681Phosphoserine1 Publication
    Modified residuei272 – 2721Phosphoserine2 Publications
    Modified residuei311 – 3111Phosphoserine1 Publication
    Modified residuei329 – 3291Phosphoserine3 Publications
    Modified residuei332 – 3321Phosphoserine3 Publications
    Modified residuei347 – 3471Phosphoserine1 Publication
    Modified residuei348 – 3481Phosphothreonine1 Publication
    Modified residuei365 – 3651PhosphothreonineBy similarity
    Modified residuei418 – 4181Phosphothreonine3 Publications
    Modified residuei586 – 5861Phosphothreonine1 Publication
    Modified residuei730 – 7301Phosphoserine1 Publication
    Modified residuei733 – 7331Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by MAPK8 and MAPK14.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO60271.
    PaxDbiO60271.
    PRIDEiO60271.

    PTM databases

    PhosphoSiteiO60271.

    Miscellaneous databases

    PMAP-CutDBO60271.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Inductioni

    Isoform 3 is increased in systemic sclerosis fibroblasts.1 Publication

    Gene expression databases

    ArrayExpressiO60271.
    BgeeiO60271.
    GenevestigatoriO60271.

    Organism-specific databases

    HPAiHPA040446.

    Interactioni

    Subunit structurei

    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 NFKB1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARF1P840773EBI-1023301,EBI-447171
    ARF6P623308EBI-1023301,EBI-638181
    Arf6P623312EBI-1023301,EBI-988682From a different organism.

    Protein-protein interaction databases

    BioGridi114505. 27 interactions.
    IntActiO60271. 9 interactions.
    MINTiMINT-1136008.

    Structurei

    Secondary structure

    1
    1321
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi406 – 46560

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W83X-ray1.93C/D406-476[»]
    ProteinModelPortaliO60271.
    SMRiO60271. Positions 406-466, 1001-1026.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO60271.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili66 – 166101Sequence AnalysisAdd
    BLAST
    Coiled coili408 – 5341271 PublicationAdd
    BLAST
    Coiled coili724 – 75835Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the JIP scaffold family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG270333.
    HOGENOMiHOG000290716.
    HOVERGENiHBG024110.
    InParanoidiO60271.
    OMAiGSDQLES.
    OrthoDBiEOG7GXP9P.
    PhylomeDBiO60271.
    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: O60271-1) [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

    MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL     50
    MPLVVAVLEN LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE 100
    EKFIEFEDSQ EQEKKDLQTR VESLESQTRQ LELKAKNYAD QISRLEEREA 150
    ELKKEYNALH QRHTEMIHNY MEHLERTKLH QLSGSDQLES TAHSRIRKER 200
    PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKVSN 250
    SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG 300
    FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE 350
    LDMDKDLSGY KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG 400
    ADLLGMGREV ENLILENTQL LETKNALNIV KNDLIAKVDE LTCEKDVLQG 450
    ELEAVKQAKL KLEEKNRELE EELRKARAEA EDARQKAKDD DDSDIPTAQR 500
    KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE NPAMQEKKRS 550
    SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP 600
    GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL 650
    PQKYKQVTNG QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT 700
    RDGGSVVGAS VFYKDVAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKELKN 750
    QEELSSLVWI CTSTHSATKV LIIDAVQPGN ILDSFTVCNS HVLCIASVPG 800
    ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG GITVVGCSAE 850
    GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG 900
    SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV 950
    LPNEQDLVRE EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK 1000
    DSILSIVHVK GIVLVALADG TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI 1050
    RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK SFDAHPRKES QVRQLAWVGD 1100
    GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK LGFSFVRITA 1150
    LMVSCNRLWV GTGNGVIISI PLTETNKTSG VPGNRPGSVI RVYGDENSDK 1200
    VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG 1250
    DKAGPSAQEP GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE 1300
    PSVTKAERSH LIVWQVMYGN E 1321
    Length:1,321
    Mass (Da):146,205
    Last modified:May 2, 2006 - v4
    Checksum:i5CAE349FBDF91B40
    GO
    Isoform 2 (identifier: O60271-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         248-261: Missing.
         555-555: F → FVPTR

    Show »
    Length:1,311
    Mass (Da):145,135
    Checksum:iD60A544D70BD1F97
    GO
    Isoform 3 (identifier: O60271-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         938-945: SNDSDAYK → RYNNGSST
         946-1321: Missing.

    Note: Due to intron retention.

    Show »
    Length:945
    Mass (Da):104,736
    Checksum:iEB17642AA2BF0BB4
    GO
    Isoform 4 (identifier: O60271-4) [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):144,682
    Checksum:i55B30E422A8ABD0E
    GO
    Isoform 5 (identifier: O60271-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         248-261: Missing.
         938-945: SNDSDAYK → RYNNGSST
         946-1321: Missing.

    Show »
    Length:931
    Mass (Da):103,212
    Checksum:i1A427D7B60367814
    GO
    Isoform 6 (identifier: O60271-9) [UniParc]FASTAAdd to Basket

    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.Curated

    Show »
    Length:1,177
    Mass (Da):128,607
    Checksum:i8CD074A547DCC690
    GO

    Sequence cautioni

    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 BAB14812.1 differs from that shown. Reason: Unlikely isoform. Aberrant splicing.
    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 CAA62987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti451 – 4511E → G in AAO66462. (PubMed:14662895)Curated
    Sequence conflicti680 – 6801E → K in CAA62987. (PubMed:9480848)Curated
    Sequence conflicti680 – 6801E → K in AAO66462. (PubMed:14662895)Curated
    Isoform 6 (identifier: O60271-9)
    Sequence conflicti9 – 91F → S in BAG58134. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1320 – 13201N → S.
    Corresponds to variant rs9896965 [ dbSNP | Ensembl ].
    VAR_059364

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 196196MELED…AHSRI → MSPGCMLLFVFGFVGGAVVI NSAILVSLSVLLLVHFSIST GVPALTQNLPRIL in isoform 6. 2 PublicationsVSP_042253Add
    BLAST
    Alternative sequencei248 – 26114Missing in isoform 2, isoform 4, isoform 5 and isoform 6. 5 PublicationsVSP_018214Add
    BLAST
    Alternative sequencei555 – 5551F → FVPTR in isoform 2. 1 PublicationVSP_018220
    Alternative sequencei938 – 9458SNDSDAYK → RYNNGSST in isoform 3 and isoform 5. 2 PublicationsVSP_018221
    Alternative sequencei946 – 1321376Missing in isoform 3 and isoform 5. 2 PublicationsVSP_018222Add
    BLAST
    Alternative sequencei1175 – 11751T → TVILHQGRLLGLRA in isoform 6. 2 PublicationsVSP_042254

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11577.1. [O60271-4]
    CCDS45740.1. [O60271-1]
    CCDS58577.1. [O60271-9]
    CCDS58578.1. [O60271-2]
    PIRiJC5958.
    RefSeqiNP_001123999.1. NM_001130527.2. [O60271-2]
    NP_001124000.1. NM_001130528.2. [O60271-1]
    NP_001238900.1. NM_001251971.1. [O60271-9]
    NP_003962.3. NM_003971.5. [O60271-4]
    UniGeneiHs.463439.

    Genome annotation databases

    EnsembliENST00000262013; ENSP00000262013; ENSG00000008294. [O60271-1]
    ENST00000357122; ENSP00000349636; ENSG00000008294. [O60271-4]
    ENST00000505279; ENSP00000426900; ENSG00000008294. [O60271-2]
    ENST00000510283; ENSP00000423165; ENSG00000008294. [O60271-9]
    GeneIDi9043.
    KEGGihsa:9043.
    UCSCiuc002ita.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]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11577.1. [O60271-4 ]
    CCDS45740.1. [O60271-1 ]
    CCDS58577.1. [O60271-9 ]
    CCDS58578.1. [O60271-2 ]
    PIRi JC5958.
    RefSeqi NP_001123999.1. NM_001130527.2. [O60271-2 ]
    NP_001124000.1. NM_001130528.2. [O60271-1 ]
    NP_001238900.1. NM_001251971.1. [O60271-9 ]
    NP_003962.3. NM_003971.5. [O60271-4 ]
    UniGenei Hs.463439.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W83 X-ray 1.93 C/D 406-476 [» ]
    ProteinModelPortali O60271.
    SMRi O60271. Positions 406-466, 1001-1026.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114505. 27 interactions.
    IntActi O60271. 9 interactions.
    MINTi MINT-1136008.

    PTM databases

    PhosphoSitei O60271.

    Proteomic databases

    MaxQBi O60271.
    PaxDbi O60271.
    PRIDEi O60271.

    Protocols and materials databases

    DNASUi 9043.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262013 ; ENSP00000262013 ; ENSG00000008294 . [O60271-1 ]
    ENST00000357122 ; ENSP00000349636 ; ENSG00000008294 . [O60271-4 ]
    ENST00000505279 ; ENSP00000426900 ; ENSG00000008294 . [O60271-2 ]
    ENST00000510283 ; ENSP00000423165 ; ENSG00000008294 . [O60271-9 ]
    GeneIDi 9043.
    KEGGi hsa:9043.
    UCSCi uc002ita.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

    CTDi 9043.
    GeneCardsi GC17M049039.
    HGNCi HGNC:14524. SPAG9.
    HPAi HPA040446.
    MIMi 605430. gene.
    neXtProti NX_O60271.
    PharmGKBi PA37890.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270333.
    HOGENOMi HOG000290716.
    HOVERGENi HBG024110.
    InParanoidi O60271.
    OMAi GSDQLES.
    OrthoDBi EOG7GXP9P.
    PhylomeDBi O60271.
    TreeFami TF313096.

    Enzyme and pathway databases

    Reactomei REACT_21402. CDO in myogenesis.
    SignaLinki O60271.

    Miscellaneous databases

    ChiTaRSi SPAG9. human.
    EvolutionaryTracei O60271.
    GeneWikii SPAG9.
    GenomeRNAii 9043.
    NextBioi 33871.
    PMAP-CutDB O60271.
    PROi O60271.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60271.
    Bgeei O60271.
    Genevestigatori O60271.

    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

    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.
      , 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.
      , 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiJIP4_HUMAN
    AccessioniPrimary (citable) accession number: O60271
    Secondary accession number(s): A6H8U5
    , A8MSX0, B4DHH2, O60905, Q3KQU8, Q3MKM7, Q86WC7, Q86WC8, Q8IZX7, Q96II0, Q9H811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 120 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3