Hmdb loader
Identification
HMDB Protein ID HMDBP07747
Secondary Accession Numbers
  • 13456
Name C-Jun-amino-terminal kinase-interacting protein 1
Synonyms
  1. IB-1
  2. Islet-brain 1
  3. JIP-1
  4. JNK MAP kinase scaffold protein 1
  5. JNK-interacting protein 1
  6. Mitogen-activated protein kinase 8-interacting protein 1
Gene Name MAPK8IP1
Protein Type Unknown
Biological Properties
General Function Involved in kinesin binding
Specific 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. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK- regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Nucleus
  2. Cytoplasm
  3. Cytoplasm
  4. perinuclear region
Gene Properties
Chromosome Location Chromosome:1
Locus 11p11.2
SNPs MAPK8IP1
Gene Sequence
>2136 bp
ATGGCGGAGCGAGAAAGCGGCGGCCTGGGAGGGGGGGCCGCGTCCCCGCCCGCCGCCTCC
CCGTTCCTGGGGCTGCACATCGCTTCGCCTCCCAATTTCAGGCTCACCCATGACATCAGC
CTGGAGGAGTTTGAGGATGAAGACCTCTCGGAGATCACTGATGAGTGTGGCATCAGCTTA
CAGTGCAAAGACACCCTGTCCTTACGGCCCCCGCGCGCCGGGCTGCTCTCTGCGGGCGGC
GGCGGCGCGGGGAGCCGGTTGCAGGCCGAGATGCTGCAGATGGACCTGATCGACGCGACG
GGGGACACTCCCGGGGCCGAGGACGACGAGGAGGACGACGACGAGGAGCGCGCGGCCCGG
CGGCCGGGAGCGGGGCCGCCCAAGGCCGAGTCCGGCCAGGAGCCGGCGTCCCGCGGCCAG
GGCCAGAGCCAAGGCCAGAGCCAGGGCCCGGGCAGCGGGGACACGTACCGGCCCAAGCGG
CCCACCACGCTCAACCTCTTTCCGCAGGTGCCGCGGTCTCAGGACACACTGAATAATAAT
TCTCTGGGCAAAAAGCACAGTTGGCAGGATCGGGTGTCTCGATCATCCTCACCCCTGAAG
ACAGGGGAGCAGACACCACCGCATGAACACATCTGCCTGAGCGATGAGCTGCCCCCCCAG
AGCGGCCCCGCCCCCACCACAGATCGAGGCACCTCCACCGACAGCCCTTGCCGCCGCAGC
ACAGCCACCCAGATGGCACCTCCGGGTGGTCCCCCTGCTGCCCCGCCTGGGGGTCGGGGC
CACTCGCATCGAGACCGAATCCACTACCAGGCCGATGTGCGACTAGAGGCCACTGAGGAG
ATCTACCTGACCCCAGTGCAGAGGCCCCCAGACGCTGCAGAGCCCACCTCCGCCTTCCTG
CCGCCCACTGAGAGCCGGATGTCAGTCAGCTCCGATCCAGACCCTGCCGCCTACCCCTCC
ACGGCAGGGCGGCCGCACCCCTCCATCAGTGAAGAGGAAGAGGGCTTCGACTGCCTGTCG
TCCCCAGAGCGGGCTGAGCCCCCAGGCGGAGGGTGGCGGGGGAGCCTGGGGGAGCCGCCG
CCACCTCCACGGGCCTCTCTGAGCTCGGACACCAGCGCCCTGTCCTATGACTCTGTCAAG
TACACGCTGGTGGTAGATGAGCATGCACAGCTGGAGCTGGTGAGCCTGCGGCCGTGCTTC
GGAGACTACAGTGACGAGAGTGACTCTGCCACCGTCTATGACAACTGTGCCTCCGTCTCC
TCGCCCTATGAGTCGGCCATCGGAGAGGAATATGAGGAGGCCCCGCGGCCCCAGCCCCCT
GCCTGCCTCTCCGAGGACTCCACGCCTGATGAACCCGACGTCCATTTCTCCAAGAAATTC
CTGAACGTCTTCATGAGTGGCCGCTCCCGCTCCTCCAGTGCTGAGTCCTTCGGGCTGTTC
TCCTGCATCATCAACGGGGAGGAGCAGGAGCAGACCCACCGGGCCATATTCAGGTTTGTG
CCTCGACACGAAGACGAACTTGAGCTGGAAGTGGATGACCCTCTGCTAGTGGAGCTCCAG
GCTGAAGACTACTGGTACGAGGCCTACAACATGCGCACTGGTGCCCGGGGTGTCTTTCCT
GCCTATTACGCCATCGAGGTCACCAAGGAGCCCGAGCACATGGCAGCCCTGGCCAAAAAC
AGTGACTGGGTGGACCAGTTCCGGGTGAAGTTCCTGGGCTCAGTCCAGGTTCCCTATCAC
AAGGGCAATGACGTCCTCTGTGCTGCTATGCAAAAGATTGCCACCACCCGCCGGCTCACC
GTGCACTTTAACCCGCCCTCCAGCTGTGTCCTGGAGATCAGCGTGCGGGGTGTGAAGATA
GGCGTCAAGGCCGATGACTCCCAGGAGGCCAAGGGGAATAAATGTAGCCACTTTTTCCAG
TTAAAAAACATCTCTTTCTGCGGATATCATCCAAAGAACAACAAGTACTTTGGGTTCATC
ACCAAGCACCCCGCCGACCACCGGTTTGCCTGCCACGTCTTTGTGTCTGAAGACTCCACC
AAAGCCCTGGCAGAGTCCGTGGGGAGAGCATTCCAGCAGTTCTACAAGCAGTTTGTGGAG
TACACCTGCCCCACAGAAGATATCTACCTGGAGTAG
Protein Properties
Number of Residues 711
Molecular Weight 77523.6
Theoretical pI 4.61
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>C-Jun-amino-terminal kinase-interacting protein 1
MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISL
QCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAAR
RPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNN
SLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRS
TATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFL
PPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPP
PPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVS
SPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLF
SCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFP
AYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLT
VHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFI
TKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9UQF2
UniProtKB/Swiss-Prot Entry Name JIP1_HUMAN
PDB IDs Not Available
GenBank Gene ID AF074091
GeneCard ID MAPK8IP1
GenAtlas ID MAPK8IP1
HGNC ID HGNC:6882
References
General References
  1. Mooser V, Maillard A, Bonny C, Steinmann M, Shaw P, Yarnall DP, Burns DK, Schorderet DF, Nicod P, Waeber G: Genomic organization, fine-mapping, and expression of the human islet-brain 1 (IB1)/c-Jun-amino-terminal kinase interacting protein-1 (JIP-1) gene. Genomics. 1999 Jan 15;55(2):202-8. [PubMed:9933567 ]
  2. Meyer D, Liu A, Margolis B: Interaction of c-Jun amino-terminal kinase interacting protein-1 with p190 rhoGEF and its localization in differentiated neurons. J Biol Chem. 1999 Dec 3;274(49):35113-8. [PubMed:10574993 ]
  3. Verhey KJ, Meyer D, Deehan R, Blenis J, Schnapp BJ, Rapoport TA, Margolis B: Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules. J Cell Biol. 2001 Mar 5;152(5):959-70. [PubMed:11238452 ]
  4. Ikeda A, Hasegawa K, Masaki M, Moriguchi T, Nishida E, Kozutsumi Y, Oka S, Kawasaki T: Mixed lineage kinase LZK forms a functional signaling complex with JIP-1, a scaffold protein of the c-Jun NH(2)-terminal kinase pathway. J Biochem. 2001 Dec;130(6):773-81. [PubMed:11726277 ]
  5. Taru H, Iijima K, Hase M, Kirino Y, Yagi Y, Suzuki T: Interaction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J Biol Chem. 2002 May 31;277(22):20070-8. Epub 2002 Mar 22. [PubMed:11912189 ]
  6. Nihalani D, Wong HN, Holzman LB: Recruitment of JNK to JIP1 and JNK-dependent JIP1 phosphorylation regulates JNK module dynamics and activation. J Biol Chem. 2003 Aug 1;278(31):28694-702. Epub 2003 May 19. [PubMed:12756254 ]
  7. Bonny C, Oberson A, Negri S, Sauser C, Schorderet DF: Cell-permeable peptide inhibitors of JNK: novel blockers of beta-cell death. Diabetes. 2001 Jan;50(1):77-82. [PubMed:11147798 ]
  8. Allaman-Pillet N, Storling J, Oberson A, Roduit R, Negri S, Sauser C, Nicod P, Beckmann JS, Schorderet DF, Mandrup-Poulsen T, Bonny C: Calcium- and proteasome-dependent degradation of the JNK scaffold protein islet-brain 1. J Biol Chem. 2003 Dec 5;278(49):48720-6. Epub 2003 Sep 24. [PubMed:14507925 ]
  9. Borsello T, Clarke PG, Hirt L, Vercelli A, Repici M, Schorderet DF, Bogousslavsky J, Bonny C: A peptide inhibitor of c-Jun N-terminal kinase protects against excitotoxicity and cerebral ischemia. Nat Med. 2003 Sep;9(9):1180-6. Epub 2003 Aug 24. [PubMed:12937412 ]
  10. Waeber G, Delplanque J, Bonny C, Mooser V, Steinmann M, Widmann C, Maillard A, Miklossy J, Dina C, Hani EH, Vionnet N, Nicod P, Boutin P, Froguel P: The gene MAPK8IP1, encoding islet-brain-1, is a candidate for type 2 diabetes. Nat Genet. 2000 Mar;24(3):291-5. [PubMed:10700186 ]