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Q9UPT6 (JIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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 3

Short name=JIP-3
Short name=JNK-interacting protein 3
Alternative name(s):
JNK MAP kinase scaffold protein 3
Mitogen-activated protein kinase 8-interacting protein 3
Gene names
Name:MAPK8IP3
Synonyms:JIP3, KIAA1066
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1336 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. May function as a regulator of vesicle transport, through interations with the JNK-signaling components and motor proteins By similarity. Ref.7 UniProtKB Q9ESN9

Subunit structure

Forms homo- or heterooligomeric complexes. The central region of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but not MAPK8IP1. Binds specific components of the JNK signaling pathway namely MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3 to the N-terminal region, MAP2K4/MKK4 and MAP2K7/MKK7 to the central region and MAP3K11 to the C-terminal region. Binds the TPR motif-containing C-terminal of kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding complexes are then transported as a cargo of kinesin, to the required subcellular location By similarity. Interacts with ROCK1 and this interaction is enhanced by ultraviolet-B (UVB) radiation. Ref.7 Ref.9 UniProtKB Q9ESN9

Subcellular location

Cytoplasm By similarity UniProtKB Q9ESN9.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Phosphorylation by ROCK1 is crucial for the recruitment of JNK. Ref.8 Ref.9

Sequence similarities

Belongs to the JIP scaffold family.

Sequence caution

The sequence AAK61290.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAA83018.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB15727.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAB72318.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processvesicle-mediated transport

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentGolgi membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionMAP-kinase scaffold activity

Inferred from sequence or structural similarity. Source: UniProtKB

kinesin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UPT6-1)

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: Q9UPT6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     249-250: CP → VL
     251-1336: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13361336C-Jun-amino-terminal kinase-interacting protein 3
PRO_0000220633

Regions

Coiled coil58 – 177120 Potential
Coiled coil440 – 554115 Potential

Amino acid modifications

Modified residue2651Phosphothreonine; by MAPK By similarity
Modified residue2671Phosphoserine By similarity
Modified residue2751Phosphothreonine; by MAPK By similarity
Modified residue2861Phosphothreonine; by MAPK By similarity
Modified residue3141Phosphoserine; by ROCK1 Ref.9
Modified residue3641Phosphoserine; by ROCK1 Ref.9
Modified residue3651Phosphoserine; by ROCK1 Ref.9
Modified residue5851Phosphoserine Ref.8
Modified residue6761Phosphoserine By similarity

Natural variations

Alternative sequence249 – 2502CP → VL in isoform 2.
VSP_024430
Alternative sequence251 – 13361086Missing in isoform 2.
VSP_024431
Natural variant7531T → A.
Corresponds to variant rs2294619 [ dbSNP | Ensembl ].
VAR_049667

Sequences

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

Last modified April 17, 2007. Version 3.
Checksum: 84166F5725D74B25

FASTA1,336147,457
        10         20         30         40         50         60 
MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV 

        70         80         90        100        110        120 
NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RRQAEEKFIE FEDALEQEKK 

       130        140        150        160        170        180 
ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE 

       190        200        210        220        230        240 
RSKMQQVGGN SQTESSLPGR RKERPTSLNV FPLADGTVRA QIGGKLVPAG DHWHLSDLGQ 

       250        260        270        280        290        300 
LQSSSSYQCP QDEMSESGQS SAAATPSTTG TKSNTPTSSV PSAAVTPLNE SLQPLGDYGV 

       310        320        330        340        350        360 
GSKNSKRARE KRDSRNMEVQ VTQEMRNVSI GMGSSDEWSD VQDIIDSTPE LDMCPETRLD 

       370        380        390        400        410        420 
RTGSSPTQGI VNKAFGINTD SLYHELSTAG SEVIGDVDEG ADLLGEFSVR DDFFGMGKEV 

       430        440        450        460        470        480 
GNLLLENSQL LETKNALNVV KNDLIAKVDQ LSGEQEVLRG ELEAAKQAKV KLENRIKELE 

       490        500        510        520        530        540 
EELKRVKSEA IIARREPKEE AEDVSSYLCT ESDKIPMAQR RRFTRVEMAR VLMERNQYKE 

       550        560        570        580        590        600 
RLMELQEAVR WTEMIRASRE HPSVQEKKKS TIWQFFSRLF SSSSSPPPAK RPYPSVNIHY 

       610        620        630        640        650        660 
KSPTTAGFSQ RRNHAMCPIS AGSRPLEFFP DDDCTSSARR EQKREQYRQV REHVRNDDGR 

       670        680        690        700        710        720 
LQACGWSLPA KYKQLSPNGG QEDTRMKNVP VPVYCRPLVE KDPTMKLWCA AGVNLSGWRP 

       730        740        750        760        770        780 
NEDDAGNGVK PAPGRDPLTC DREGDGEPKS AHTSPEKKKA KELPEMDATS SRVWILTSTL 

       790        800        810        820        830        840 
TTSKVVIIDA NQPGTVVDQF TVCNAHVLCI SSIPAASDSD YPPGEMFLDS DVNPEDPGAD 

       850        860        870        880        890        900 
GVLAGITLVG CATRCNVPRS NCSSRGDTPV LDKGQGEVAT IANGKVNPSQ STEEATEATE 

       910        920        930        940        950        960 
VPDPGPSEPE TATLRPGPLT EHVFTDPAPT PSSGPQPGSE NGPEPDSSST RPEPEPSGDP 

       970        980        990       1000       1010       1020 
TGAGSSAAPT MWLGAQNGWL YVHSAVANWK KCLHSIKLKD SVLSLVHVKG RVLVALADGT 

      1030       1040       1050       1060       1070       1080 
LAIFHRGEDG QWDLSNYHLM DLGHPHHSIR CMAVVYDRVW CGYKNKVHVI QPKTMQIEKS 

      1090       1100       1110       1120       1130       1140 
FDAHPRRESQ VRQLAWIGDG VWVSIRLDST LRLYHAHTHQ HLQDVDIEPY VSKMLGTGKL 

      1150       1160       1170       1180       1190       1200 
GFSFVRITAL LVAGSRLWVG TGNGVVISIP LTETVVLHRG QLLGLRANKT SPTSGEGARP 

      1210       1220       1230       1240       1250       1260 
GGIIHVYGDD SSDRAASSFI PYCSMAQAQL CFHGHRDAVK FFVSVPGNVL ATLNGSVLDS 

      1270       1280       1290       1300       1310       1320 
PAEGPGPAAP ASEVEGQKLR NVLVLSGGEG YIDFRIGDGE DDETEEGAGD MSQVKPVLSK 

      1330 
AERSHIIVWQ VSYTPE 

« Hide

Isoform 2 [UniParc].

Checksum: E7C2A9B0793A810E
Show »

FASTA25029,052

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed: 10470851] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 324; 414 AND 753.
[3]"Characterization of long cDNA clones from human adult spleen."
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
DNA Res. 7:357-366(2000) [PubMed: 11214971] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[4]"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16."
Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.
Hum. Mol. Genet. 10:339-352(2001) [PubMed: 11157797] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[7]"Phosphorylation-dependent scaffolding role of JSAP1/JIP3 in the ASK1-JNK signaling pathway. A new mode of regulation of the MAP kinase cascade."
Matsuura H., Nishitoh H., Takeda K., Matsuzawa A., Amagasa T., Ito M., Yoshioka K., Ichijo H.
J. Biol. Chem. 277:40703-40709(2002) [PubMed: 12189133] [Abstract]
Cited for: INTERACTION WITH MAP2K4/MEK4, MAP2K7/MKK7, MAPK10/JNK3 AND MAP3K5/ASK1, FUNCTION.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-585, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"Identification of ROCK1 as an upstream activator of the JIP-3 to JNK signaling axis in response to UVB damage."
Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J., Shi Y., Liao J.K., Lee S.W.
Sci. Signal. 1:RA14-RA14(2008) [PubMed: 19036714] [Abstract]
Cited for: INTERACTION WITH ROCK1, PHOSPHORYLATION AT SER-314; SER-364 AND SER-365.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028989 mRNA. Translation: BAA83018.2. Different initiation.
AK024437 mRNA. Translation: BAB15727.1. Different initiation.
AE006639 Genomic DNA. Translation: AAK61290.1. Sequence problems.
AL031718 Genomic DNA. Translation: CAB72318.1. Sequence problems.
AL031710, AC012180, AL031717 Genomic DNA. Translation: CAM26364.1.
AL031717, AC012180, AL031710 Genomic DNA. Translation: CAM26394.1.
BC137123 mRNA. Translation: AAI37124.1.
BC137124 mRNA. Translation: AAI37125.1.
BC150266 mRNA. Translation: AAI50267.1.
IPIIPI00219817.
IPI00398504.
RefSeqNP_001035529.1. NM_001040439.1.
NP_055948.2. NM_015133.3.
UniGeneHs.207763.

3D structure databases

ProteinModelPortalQ9UPT6.
SMRQ9UPT6. Positions 416-475.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9UPT6. 3 interactions.
MINTMINT-1404510.
STRINGQ9UPT6.

PTM databases

PhosphoSiteQ9UPT6.

Polymorphism databases

DMDM145559484.

Proteomic databases

PRIDEQ9UPT6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250894; ENSP00000250894; ENSG00000138834.
GeneID23162.
KEGGhsa:23162.
UCSCuc002cmi.1. human.
uc002cmk.1. human.

Organism-specific databases

CTD23162.
GeneCardsGC16P001696.
H-InvDBHIX0012690.
HGNCHGNC:6884. MAPK8IP3.
HPACAB005580.
MIM605431. gene.
neXtProtNX_Q9UPT6.
PharmGKBPA30628.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG11458.
GeneTreeENSGT00600000084097.
HOVERGENHBG024110.
OMAWLYVHSA.
OrthoDBEOG4B2SWD.
PhylomeDBQ9UPT6.

Gene expression databases

ArrayExpressQ9UPT6.
BgeeQ9UPT6.
CleanExHS_MAPK8IP3.
GenevestigatorQ9UPT6.
GermOnlineENSG00000138834. Homo sapiens.

Family and domain databases

InterProIPR019143. JNK/Rab-associated_protein-1_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR011046. WD40_repeat-like_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK04436.
PfamPF09744. Jnk-SapK_ap_N. 1 hit.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
ProtoNetSearch...

Other

NextBio44539.
SOURCESearch...

Entry information

Entry nameJIP3_HUMAN
AccessionPrimary (citable) accession number: Q9UPT6
Secondary accession number(s): A2A2B3 expand/collapse secondary AC list , A7E2B3, Q96RY4, Q9H4I4, Q9H7P1, Q9NUG0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: April 17, 2007
Last modified: December 14, 2011
This is version 82 of the entry and version 3 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

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families