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P62774 (MTPN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Myotrophin
Alternative name(s):
Granule cell differentiation protein
Protein V-1
Gene names
Name:Mtpn
Synonyms:Gcdp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length118 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy By similarity. Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer. Ref.5

Subunit structure

Interacts with RELA By similarity. Interacts with the heterodimer formed by CAPZA1 and CAPZB.

Subcellular location

Cytoplasm Probable. Nucleus By similarity. Cytoplasmperinuclear region By similarity.

Sequence similarities

Belongs to the myotrophin family.

Contains 3 ANK repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainANK repeat
Repeat
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcatecholamine metabolic process

Inferred from electronic annotation. Source: Ensembl

cell growth

Inferred from electronic annotation. Source: Ensembl

cerebellar granule cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cardiac muscle hypertrophy

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of macromolecule biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of barbed-end actin filament capping

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal muscle tissue regeneration

Inferred from electronic annotation. Source: Ensembl

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentF-actin capping protein complex

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 118117Myotrophin
PRO_0000067032

Regions

Repeat2 – 3029ANK 1
Repeat34 – 6633ANK 2
Repeat67 – 9933ANK 3

Amino acid modifications

Modified residue21N-acetylcysteine Ref.4
Modified residue41N6-acetyllysine Ref.4
Modified residue111N6-acetyllysine By similarity
Modified residue241N6-acetyllysine By similarity

Experimental info

Sequence conflict261E → K in BAB22235. Ref.2

Secondary structure

........................... 118
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62774 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9097FFDF61DB8BA2

FASTA11812,861
        10         20         30         40         50         60 
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD 

        70         80         90        100        110 
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTALEATDN QAIKALLQ 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of cDNA clones encoding the mouse protein V-1."
Pennica D., Shaw K.J., Luoh S., Wood W.I.
Gene 158:305-306(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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 and DBA/2.
Tissue: Bone marrow, Kidney, Spinal ganglion and Stomach.
[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/6.
Tissue: Brain.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2 AND LYS-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[5]"Structural basis for capping protein sequestration by myotrophin (V-1)."
Zwolak A., Fujiwara I., Hammer J.A. III, Tjandra N.
J. Biol. Chem. 285:25767-25781(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH CAPZA1 AND CAPZB, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U20290 mRNA. Translation: AAA86719.1.
AK002620 mRNA. Translation: BAB22235.1.
AK028027 mRNA. Translation: BAC25707.1.
AK049398 mRNA. Translation: BAC33734.1.
AK083888 mRNA. Translation: BAC39050.1.
AK132029 mRNA. Translation: BAE20953.1.
AK145755 mRNA. Translation: BAE26630.1.
AK146305 mRNA. Translation: BAE27061.1.
AK146473 mRNA. Translation: BAE27198.1.
AK150750 mRNA. Translation: BAE29820.1.
AK151106 mRNA. Translation: BAE30116.1.
AK151147 mRNA. Translation: BAE30153.1.
AK151485 mRNA. Translation: BAE30438.1.
AK151564 mRNA. Translation: BAE30506.1.
AK151640 mRNA. Translation: BAE30570.1.
AK151687 mRNA. Translation: BAE30611.1.
AK152272 mRNA. Translation: BAE31088.1.
BC043084 mRNA. Translation: AAH43084.1.
BC054811 mRNA. Translation: AAH54811.1.
CCDSCCDS20002.1.
RefSeqNP_032124.1. NM_008098.4.
UniGeneMm.182746.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KXPNMR-C1-118[»]
ProteinModelPortalP62774.
SMRP62774. Positions 1-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62774. 3 interactions.
MINTMINT-4102563.

PTM databases

PhosphoSiteP62774.

Proteomic databases

MaxQBP62774.
PaxDbP62774.
PRIDEP62774.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031866; ENSMUSP00000031866; ENSMUSG00000029840.
GeneID14489.
KEGGmmu:14489.
UCSCuc009bit.2. mouse.

Organism-specific databases

CTD136319.
MGIMGI:99445. Mtpn.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00430000031071.
HOGENOMHOG000276399.
HOVERGENHBG019067.
InParanoidP62774.
OMAYEGHVTC.
OrthoDBEOG7SBNQP.
PhylomeDBP62774.
TreeFamTF327387.

Gene expression databases

BgeeP62774.
CleanExMM_MTPN.
GenevestigatorP62774.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMTPN. mouse.
NextBio286160.
PROP62774.
SOURCESearch...

Entry information

Entry nameMTPN_MOUSE
AccessionPrimary (citable) accession number: P62774
Secondary accession number(s): P80144, Q543M6, Q9DCN8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 83 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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