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O60271 - JIP4_HUMAN

UniProt

O60271 - JIP4_HUMAN

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Protein

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

Gene

SPAG9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Isoform 5 may play a role in spermatozoa-egg-interaction.2 Publications

GO - Molecular functioni

  1. JUN kinase binding Source: GO_Central
  2. kinesin binding Source: GO_Central
  3. MAP-kinase scaffold activity Source: GO_Central
  4. receptor signaling complex scaffold activity Source: GO_Central

GO - Biological processi

  1. activation of JUN kinase activity Source: GO_Central
  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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:14524. SPAG9.

Subcellular locationi

Cytoplasm. Cytoplasm › perinuclear region
Note: Perinuclear distribution in response to stress signals such as UV radiation.
Isoform 5 : Cytoplasmic vesicle › secretory vesicle › acrosome
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: UniProtKB
  5. integral component of membrane Source: ProtInc
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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

BgeeiO60271.
ExpressionAtlasiO60271. baseline and differential.
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.
EXOC4Q96A653EBI-1023301,EBI-355383

Protein-protein interaction databases

BioGridi114505. 29 interactions.
IntActiO60271. 10 interactions.
MINTiMINT-1136008.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W83X-ray1.93C/D406-476[»]
ProteinModelPortaliO60271.
SMRiO60271. Positions 406-466.
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.
GeneTreeiENSGT00670000097546.
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

        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 QLSGSDQLES TAHSRIRKER 
       210        220        230        240        250
PISLGIFPLP AGDGLLTPDA QKGGETPGSE QWKFQELSQP RSHTSLKVSN 
       260        270        280        290        300
SPEPQKAVEQ EDELSDVSQG GSKATTPAST ANSDVATIPT DTPLKEENEG 
       310        320        330        340        350
FVKVTDAPNK SEISKHIEVQ VAQETRNVST GSAENEEKSE VQAIIESTPE 
       360        370        380        390        400
LDMDKDLSGY KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG 
       410        420        430        440        450
ADLLGMGREV ENLILENTQL LETKNALNIV KNDLIAKVDE LTCEKDVLQG 
       460        470        480        490        500
ELEAVKQAKL KLEEKNRELE EELRKARAEA EDARQKAKDD DDSDIPTAQR 
       510        520        530        540        550
KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE NPAMQEKKRS 
       560        570        580        590        600
SIWQFFSRLF SSSSNTTKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP 
       610        620        630        640        650
GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL 
       660        670        680        690        700
PQKYKQVTNG QGENKMKNLP VPVYLRPLDE KDTSMKLWCA VGVNLSGGKT 
       710        720        730        740        750
RDGGSVVGAS VFYKDVAGLD TEGSKQRSAS QSSLDKLDQE LKEQQKELKN 
       760        770        780        790        800
QEELSSLVWI CTSTHSATKV LIIDAVQPGN ILDSFTVCNS HVLCIASVPG 
       810        820        830        840        850
ARETDYPAGE DLSESGQVDK ASLCGSMTSN SSAETDSLLG GITVVGCSAE 
       860        870        880        890        900
GVTGAATSPS TNGASPVMDK PPEMEAENSE VDENVPTAEE ATEATEGNAG 
       910        920        930        940        950
SAEDTVDISQ TGVYTEHVFT DPLGVQIPED LSPVYQSSND SDAYKDQISV 
       960        970        980        990       1000
LPNEQDLVRE 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 VPGNRPGSVI RVYGDENSDK 
      1210       1220       1230       1240       1250
VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSSGTDLTG 
      1260       1270       1280       1290       1300
DKAGPSAQEP GSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE 
      1310       1320 
PSVTKAERSH LIVWQVMYGN E
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.Probable cloning artifact.Curated
The sequence AAH59946.1 differs from that shown.Probable cloning artifact.Curated
The sequence AAI06049.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAO66462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA25442.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB14812.1 differs from that shown.Unlikely isoform. Aberrant splicing.Curated
The sequence CAA62987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W83X-ray1.93C/D406-476[»]
ProteinModelPortaliO60271.
SMRiO60271. Positions 406-466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114505. 29 interactions.
IntActiO60271. 10 interactions.
MINTiMINT-1136008.

PTM databases

PhosphoSiteiO60271.

Proteomic databases

MaxQBiO60271.
PaxDbiO60271.
PRIDEiO60271.

Protocols and materials databases

DNASUi9043.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi9043.
GeneCardsiGC17M049039.
HGNCiHGNC:14524. SPAG9.
HPAiHPA040446.
MIMi605430. gene.
neXtProtiNX_O60271.
PharmGKBiPA37890.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG270333.
GeneTreeiENSGT00670000097546.
HOGENOMiHOG000290716.
HOVERGENiHBG024110.
InParanoidiO60271.
OMAiGSDQLES.
OrthoDBiEOG7GXP9P.
PhylomeDBiO60271.
TreeFamiTF313096.

Enzyme and pathway databases

ReactomeiREACT_21402. CDO in myogenesis.
SignaLinkiO60271.

Miscellaneous databases

ChiTaRSiSPAG9. human.
EvolutionaryTraceiO60271.
GeneWikiiSPAG9.
GenomeRNAii9043.
NextBioi33871.
PMAP-CutDBO60271.
PROiO60271.
SOURCEiSearch...

Gene expression databases

BgeeiO60271.
ExpressionAtlasiO60271. baseline and differential.
GenevestigatoriO60271.

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.
ProtoNetiSearch...

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).
    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.
+Additional computationally mapped references.

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: February 4, 2015
This is version 124 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.