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Q9ERH6 (MOAP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Modulator of apoptosis 1

Short name=MAP-1
Gene names
Name:Moap1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for death receptor-dependent apoptosis. When associated with RASSF1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation By similarity.

Subunit structure

Homodimer. Under normal circumstances, held in an inactive conformation by an intramolecular interaction. Binding to RASSF1 isoform A(RASSF1A) relieves this inhibitory interaction and allows further binding to BAX. Binds also to BCL2 and BCLX. Recruited to the TNFRSF1A and TNFRSF10A complexes in response to their respective cognate ligand, after internalization By similarity. Interacts with TRIM39 By similarity. Interacts with RASSF6. Ref.4

Tissue specificity

Widely expressed, including in the brain. High expression levels in testis. Ref.5

Domain

The BH3-like domain is required for association with BAX and for mediating apoptosis. The three BH domains (BH1, BH2, and BH3) of BAX are all required for mediating protein-protein interaction By similarity.

Post-translational modification

Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1, this modification is inhibited by TRIM39 By similarity.

Sequence similarities

Belongs to the PNMA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Modulator of apoptosis 1
PRO_0000155207

Regions

Region120 – 1278BH3-like
Region204 – 2074RASSF1-binding By similarity
Compositional bias335 – 3406Poly-Glu

Experimental info

Sequence conflict571R → K in AAH55374. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9ERH6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 8F4630D080495D98

FASTA35239,404
        10         20         30         40         50         60 
MTLRLLEDWC RGMDMNPRKA LLVAGIPPTC GVADIEEALQ AGLAPLGEHR LLGRMFRRDE 

        70         80         90        100        110        120 
NKNVALIGLT VETGSALVPK EIPAKGGVWR VIFKPPDTDS DFLCRLNEFL KGEGMTMGEL 

       130        140        150        160        170        180 
TRVLGNRNDP LGLDPGIMIP EIRAPMLAQA LNEALKPTLQ YLRYKKLSVF SGRDPPGPGE 

       190        200        210        220        230        240 
EEFESWMFHT SQVMKTWQVS DVEKRRRLIE SLRGPAFEII RVLKINNPFI TVAECLKTLE 

       250        260        270        280        290        300 
TIFGIIDNPR ALQVKYLTTY QKTDEKLSAY VLRLEPLLQK LVQKGAIEKE VVNQARLDQV 

       310        320        330        340        350 
IAGAVHKSVR RELGLPEGSP APGLLQLLTL IKDKEAEEEE VLLQAELEGY CT 

« Hide

References

« Hide 'large scale' references
[1]"MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains."
Tan K.O., Tan K.M.L., Chan S.-L., Yee K.S.Y., Bevort M., Ang K.C., Yu V.C.
J. Biol. Chem. 276:2802-2807(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[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].
Strain: C57BL/6J.
Tissue: Testis.
[3]"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].
Strain: C57BL/6NCr.
Tissue: Hematopoietic and Kidney.
[4]"RASSF6 is a novel member of the RASSF family of tumor suppressors."
Allen N.P., Donninger H., Vos M.D., Eckfeld K., Hesson L., Gordon L., Birrer M.J., Latif F., Clark G.J.
Oncogene 26:6203-6211(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASSF6.
[5]"Paraneoplastic antigen-like 5 gene (PNMA5) is preferentially expressed in the association areas in a primate specific manner."
Takaji M., Komatsu Y., Watakabe A., Hashikawa T., Yamamori T.
Cereb. Cortex 19:2865-2879(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF305551 mRNA. Translation: AAG31787.1.
AK019599 mRNA. Translation: BAB31810.1.
BC014715 mRNA. Translation: AAH14715.1.
BC055374 mRNA. Translation: AAH55374.1.
CCDSCCDS26122.1.
RefSeqNP_001136409.1. NM_001142937.2.
NP_071718.1. NM_022323.7.
UniGeneMm.291222.
Mm.489678.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000043336.

PTM databases

PhosphoSiteQ9ERH6.

Proteomic databases

PaxDbQ9ERH6.
PRIDEQ9ERH6.

Protocols and materials databases

DNASU64113.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000173760; ENSMUSP00000133459; ENSMUSG00000096458.
ENSMUST00000178384; ENSMUSP00000137010; ENSMUSG00000096458.
GeneID64113.
KEGGmmu:64113.
UCSCuc011yqo.2. mouse.

Organism-specific databases

CTD64112.
MGIMGI:1915555. Moap1.

Phylogenomic databases

eggNOGNOG145999.
GeneTreeENSGT00530000062986.
HOGENOMHOG000013079.
HOVERGENHBG052488.
InParanoidQ9ERH6.
OMAIPEMWAP.
OrthoDBEOG708VZW.
PhylomeDBQ9ERH6.
TreeFamTF335054.

Gene expression databases

BgeeQ9ERH6.
CleanExMM_MOAP1.
GenevestigatorQ9ERH6.

Family and domain databases

InterProIPR026523. PNMA.
[Graphical view]
PANTHERPTHR23095. PTHR23095. 1 hit.
PfamPF14893. PNMA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio319919.
PROQ9ERH6.
SOURCESearch...

Entry information

Entry nameMOAP1_MOUSE
AccessionPrimary (citable) accession number: Q9ERH6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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