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P58546 (MTPN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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):
Protein V-1
Gene names
Name:MTPN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 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. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy. Ref.1 Ref.4 Ref.7

Subunit structure

Interacts with RELA By similarity. Interacts with the heterodimer formed by CAPZA1 and CAPZB. Ref.4

Subcellular location

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

Tissue specificity

Ubiquitous. Ref.1

Induction

Up-regulated in heart left ventricle of patients with severe coronary artery disease and history of myocardial ischemia. Up-regulated in heart left ventricle of patients with dilated cardiomyopathy. Ref.1

Miscellaneous

This protein is produced by a bicistronic gene which also produces the MPD6 protein from a non-overlapping reading frame. MPD6 belongs to a group of cryptic antigens without conventional genomic structure. It is encoded by a cryptic open reading frame located in the 3'-untranslated region of MTPN.

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 direct assay Ref.1. Source: UniProtKB

cerebellar granule cell differentiation

Inferred from electronic annotation. Source: Ensembl

neuron differentiation

Non-traceable author statement PubMed 12031792. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cardiac muscle hypertrophy

Inferred from mutant phenotype Ref.1. 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 direct assay Ref.4. Source: UniProtKB

regulation of striated muscle tissue development

Non-traceable author statement PubMed 12031792. Source: UniProtKB

regulation of translation

Non-traceable author statement PubMed 12031792. 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 direct assay Ref.4. Source: UniProtKB

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 Ref.5
Chain2 – 118117Myotrophin
PRO_0000067031

Regions

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

Amino acid modifications

Modified residue21N-acetylcysteine Ref.5
Modified residue41N6-acetyllysine Ref.5
Modified residue111N6-acetyllysine Ref.5
Modified residue241N6-acetyllysine Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P58546 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9097FFDF61D329A2

FASTA11812,895
        10         20         30         40         50         60 
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI LEFLLLKGAD 

        70         80         90        100        110 
INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD GLTAFEATDN QAIKALLQ 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequence and characterization of the gene that encodes human myotrophin/V-1 protein, a mediator of cardiac hypertrophy."
Anderson K.M., Berrebi-Bertrand I., Kirkpatrick R.B., McQueney M.S., Underwood D.C., Rouanet S., Chabot-Fletcher M.
J. Mol. Cell. Cardiol. 31:705-719(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY.
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Lung.
[4]"Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end."
Bhattacharya N., Ghosh S., Sept D., Cooper J.A.
J. Biol. Chem. 281:31021-31030(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN AN ACTIN CAPPING COMPLEX, INTERACTION WITH WITH CAPZA1 AND CAPZB.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2; LYS-4; LYS-11 AND LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition."
Takeda S., Minakata S., Koike R., Kawahata I., Narita A., Kitazawa M., Ota M., Yamakuni T., Maeda Y., Nitanai Y.
PLoS Biol. 8:E1000416-E1000416(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CAPZA1 AND CAPZB, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC015987 Genomic DNA. No translation available.
BC028093 mRNA. Translation: AAH28093.1.
CCDSCCDS5842.1.
RefSeqNP_665807.1. NM_145808.3.
UniGeneHs.602015.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AAAX-ray2.20C1-118[»]
ProteinModelPortalP58546.
SMRP58546. Positions 2-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126455. 15 interactions.
DIPDIP-50234N.
IntActP58546. 3 interactions.

PTM databases

PhosphoSiteP58546.

Polymorphism databases

DMDM20138912.

2D gel databases

OGPP58546.

Proteomic databases

MaxQBP58546.
PaxDbP58546.
PeptideAtlasP58546.
PRIDEP58546.

Protocols and materials databases

DNASU136319.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000393085; ENSP00000376800; ENSG00000105887.
GeneID136319.
KEGGhsa:136319.
UCSCuc003vte.4. human.

Organism-specific databases

CTD136319.
GeneCardsGC07M135613.
HGNCHGNC:15667. MTPN.
HPAHPA019735.
MIM606484. gene.
neXtProtNX_P58546.
PharmGKBPA31271.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000276399.
HOVERGENHBG019067.
InParanoidP58546.
OMAYEGHVTC.
OrthoDBEOG7SBNQP.
PhylomeDBP58546.
TreeFamTF327387.

Gene expression databases

ArrayExpressP58546.
BgeeP58546.
CleanExHS_MTPN.
GenevestigatorP58546.

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. human.
EvolutionaryTraceP58546.
GeneWikiMTPN.
GenomeRNAi136319.
NextBio83582.
PROP58546.
SOURCESearch...

Entry information

Entry nameMTPN_HUMAN
AccessionPrimary (citable) accession number: P58546
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 115 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM