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Q8BI36 (JKAMP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
JNK1/MAPK8-associated membrane protein

Short name=JKAMP
Alternative name(s):
JNK1-associated membrane protein
Short name=JAMP
Medulloblastoma antigen MU-MB-50.4 homolog
Gene names
Name:Jkamp
Synonyms:Jamp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be a regulator of the duration of MAPK8 activity in response to various stress stimuli. Facilitates degradation of misfolded endoplasmic reticulum (ER) luminal proteins through the recruitment of components of the proteasome and endoplasmic reticulum-associated degradation (ERAD) system. Ref.1

Subunit structure

Interacts with RNF5 and MAPK8, but not with MAPK9. Binding to MAPK8 occurs before and after exposure to stress, such as UV irradiation. After exposure to stress, interacts with phosphorylated MAPK8. Competes with DUSP10 for MAPK8 binding. Associates with multiple components of the proteasome and with ERAD regulatory proteins, including AMFR/GP78, CANX, PSMC1, PSMC2, PSMC3/TBP1, PSMC5, PSMC6, PSMD8, SEC61-ALPHA and UFD1L. Ref.1 Ref.4 Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1 Ref.4.

Tissue specificity

Expressed in numerous tissues, including brain, spleen, thymus, liver, kidney and testis. Elevated expression in medulloblastoma. Ref.1

Induction

By ER stress. Ref.4

Post-translational modification

Ubiquitinated by RNF5 via 'Lys-63'-linked ubiquitin linkage in a UBE2N-dependent manner. Ubiquitination decreases association with components of the proteasome and ERAD. Ref.5

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BI36-1)

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: Q8BI36-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAVDIQP → M

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 311311JNK1/MAPK8-associated membrane protein
PRO_0000089904

Regions

Topological domain1 – 5757Lumenal Potential
Transmembrane58 – 7821Helical; Potential
Topological domain79 – 879Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain109 – 14941Lumenal Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 18818Cytoplasmic Potential
Transmembrane189 – 20921Helical; Potential
Topological domain2101Lumenal Potential
Transmembrane211 – 23121Helical; Potential
Topological domain232 – 25019Cytoplasmic Potential
Transmembrane251 – 27121Helical; Potential
Topological domain272 – 2776Lumenal Potential
Transmembrane278 – 29821Helical; Potential
Topological domain299 – 31113Cytoplasmic Potential

Amino acid modifications

Glycosylation221N-linked (GlcNAc...) Ref.1

Natural variations

Alternative sequence1 – 77MAVDIQP → M in isoform 2.
VSP_008813

Experimental info

Mutagenesis241S → A: Loss of glycosylation. Ref.1
Sequence conflict2611H → R in BAC25088. Ref.2
Sequence conflict3031I → M in BAC25088. Ref.2

Sequences

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

Last modified November 7, 2003. Version 2.
Checksum: 7C167E3ABCD8D814

FASTA31135,248
        10         20         30         40         50         60 
MAVDIQPACL GLYCGKTLLF KNGSSEIYGE CGVCPRGQRT NAQKYCQPCT ESPELYDWLY 

        70         80         90        100        110        120 
LGFMAMLPLV LHWFFIEWYS GKKSSSALFQ HITALFECTM AAIITLLVSD PVGVLYIRSC 

       130        140        150        160        170        180 
RVLMLSDWYT MLYNPSPDYV TTVHCTHEAV YPLYTIVFVY YAFCLVLMML LRPLLVKKIA 

       190        200        210        220        230        240 
CGLGKSDRFK SIYAALYFFP ILTVLQAVGG GLLYYAFPYI ILVLSLVTLA VYMSASEIEN 

       250        260        270        280        290        300 
CYDLLVRKKR LIVLFSHWLL HAYGIVSISR VDRLEHDLPL LALVPTPALF YLFTAKFTEP 

       310 
SRILSEGANG H 

« Hide

Isoform 2 [UniParc].

Checksum: 9EC52EF6CAA860EA
Show »

FASTA30534,624

References

« Hide 'large scale' references
[1]"JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein, regulates duration of JNK activity."
Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C., Broday L., Asahara T., Bhoumik A., Ronai Z.
Mol. Cell. Biol. 25:8619-8630(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RNF5 AND MAPK8, MUTAGENESIS OF SER-24, GLYCOSYLATION AT ASN-22.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Hippocampus and Lung.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"JAMP optimizes ERAD to protect cells from unfolded proteins."
Tcherpakov M., Broday L., Delaunay A., Kadoya T., Khurana A., Erdjument-Bromage H., Tempst P., Qiu X.-B., DeMartino G.N., Ronai Z.
Mol. Biol. Cell 19:5019-5028(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AMFR; CANX; PSMC1; PSMC2; PSMC3; PSMC5; PSMC6; PSMC8; RNF5; SEC61-ALPHA AND UFD1L, SUBCELLULAR LOCATION, INDUCTION.
[5]"Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."
Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.
J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF5, UBIQUITINATION.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Czech II.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK013502 mRNA. Translation: BAB28884.1.
AK004555 mRNA. Translation: BAC25088.1.
CR974486 Genomic DNA. Translation: CAX15360.1.
CR974486 Genomic DNA. Translation: CAX15361.1.
BC002238 mRNA. Translation: AAH02238.1.
CCDSCCDS25967.1. [Q8BI36-1]
CCDS56844.1. [Q8BI36-2]
RefSeqNP_001191996.1. NM_001205067.1. [Q8BI36-2]
NP_077167.1. NM_024205.2. [Q8BI36-1]
UniGeneMm.258935.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000112122.

PTM databases

PhosphoSiteQ8BI36.

Proteomic databases

PRIDEQ8BI36.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057257; ENSMUSP00000061370; ENSMUSG00000005078. [Q8BI36-1]
ENSMUST00000117449; ENSMUSP00000113744; ENSMUSG00000005078. [Q8BI36-2]
GeneID104771.
KEGGmmu:104771.
UCSCuc007nvf.2. mouse. [Q8BI36-1]
uc007nvg.2. mouse. [Q8BI36-2]

Organism-specific databases

CTD51528.
MGIMGI:1915057. Jkamp.

Phylogenomic databases

eggNOGNOG262492.
GeneTreeENSGT00390000018097.
HOGENOMHOG000290710.
HOVERGENHBG051016.
InParanoidQ8BI36.
OMAVVLFSHW.
PhylomeDBQ8BI36.
TreeFamTF314201.

Gene expression databases

ArrayExpressQ8BI36.
BgeeQ8BI36.
CleanExMM_1200003C05RIK.
GenevestigatorQ8BI36.

Family and domain databases

InterProIPR008485. DUF766.
[Graphical view]
PANTHERPTHR12740. PTHR12740. 1 hit.
PfamPF05571. DUF766. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio357276.
PROQ8BI36.
SOURCESearch...

Entry information

Entry nameJKAMP_MOUSE
AccessionPrimary (citable) accession number: Q8BI36
Secondary accession number(s): B8JJ79 expand/collapse secondary AC list , B8JJ80, Q99LT2, Q9CUZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: July 9, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot