Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P58546

- MTPN_HUMAN

UniProt

P58546 - MTPN_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Myotrophin

Gene

MTPN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

GO - Biological processi

  1. catecholamine metabolic process Source: Ensembl
  2. cell growth Source: UniProtKB
  3. cerebellar granule cell differentiation Source: Ensembl
  4. neuron differentiation Source: UniProtKB
  5. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  6. positive regulation of cell growth Source: UniProtKB
  7. positive regulation of macromolecule biosynthetic process Source: UniProtKB
  8. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  9. positive regulation of protein metabolic process Source: UniProtKB
  10. regulation of barbed-end actin filament capping Source: UniProtKB
  11. regulation of striated muscle tissue development Source: UniProtKB
  12. regulation of translation Source: UniProtKB
  13. skeletal muscle tissue regeneration Source: Ensembl
  14. striated muscle cell differentiation Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myotrophin
Alternative name(s):
Protein V-1
Gene namesi
Name:MTPN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:15667. MTPN.

Subcellular locationi

Cytoplasm Curated. Nucleus By similarity. Cytoplasmperinuclear region By similarity

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. F-actin capping protein complex Source: UniProtKB
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 118117MyotrophinPRO_0000067031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylcysteine1 Publication
Modified residuei4 – 41N6-acetyllysine1 Publication
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei24 – 241N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP58546.
PaxDbiP58546.
PeptideAtlasiP58546.
PRIDEiP58546.

2D gel databases

OGPiP58546.

PTM databases

PhosphoSiteiP58546.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

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.1 Publication

Gene expression databases

BgeeiP58546.
CleanExiHS_MTPN.
ExpressionAtlasiP58546. baseline.
GenevestigatoriP58546.

Organism-specific databases

HPAiHPA019735.

Interactioni

Subunit structurei

Interacts with RELA (By similarity). Interacts with the heterodimer formed by CAPZA1 and CAPZB.By similarity2 Publications

Protein-protein interaction databases

BioGridi126455. 15 interactions.
DIPiDIP-50234N.
IntActiP58546. 3 interactions.

Structurei

Secondary structure

1
118
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi15 – 239Combined sources
Helixi38 – 447Combined sources
Helixi48 – 558Combined sources
Turni56 – 583Combined sources
Helixi71 – 788Combined sources
Helixi81 – 899Combined sources
Helixi104 – 1074Combined sources
Helixi111 – 1177Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AAAX-ray2.20C1-118[»]
ProteinModelPortaliP58546.
SMRiP58546. Positions 2-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58546.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati2 – 3029ANK 1Add
BLAST
Repeati34 – 6633ANK 2Add
BLAST
Repeati67 – 9933ANK 3Add
BLAST

Sequence similaritiesi

Belongs to the myotrophin family.Curated
Contains 3 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000276399.
HOVERGENiHBG019067.
InParanoidiP58546.
OMAiYEGHVTC.
OrthoDBiEOG7SBNQP.
PhylomeDBiP58546.
TreeFamiTF327387.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P58546-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCDKEFMWAL KNGDLDEVKD YVAKGEDVNR TLEGGRKPLH YAADCGQLEI
60 70 80 90 100
LEFLLLKGAD INAPDKHHIT PLLSAVYEGH VSCVKLLLSK GADKTVKGPD
110
GLTAFEATDN QAIKALLQ
Length:118
Mass (Da):12,895
Last modified:January 23, 2007 - v2
Checksum:i9097FFDF61D329A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC015987 Genomic DNA. No translation available.
BC028093 mRNA. Translation: AAH28093.1.
CCDSiCCDS5842.1.
RefSeqiNP_665807.1. NM_145808.3.
UniGeneiHs.602015.

Genome annotation databases

EnsembliENST00000393085; ENSP00000376800; ENSG00000105887.
GeneIDi136319.
KEGGihsa:136319.
UCSCiuc003vte.4. human.

Polymorphism databases

DMDMi20138912.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC015987 Genomic DNA. No translation available.
BC028093 mRNA. Translation: AAH28093.1 .
CCDSi CCDS5842.1.
RefSeqi NP_665807.1. NM_145808.3.
UniGenei Hs.602015.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AAA X-ray 2.20 C 1-118 [» ]
ProteinModelPortali P58546.
SMRi P58546. Positions 2-118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126455. 15 interactions.
DIPi DIP-50234N.
IntActi P58546. 3 interactions.

PTM databases

PhosphoSitei P58546.

Polymorphism databases

DMDMi 20138912.

2D gel databases

OGPi P58546.

Proteomic databases

MaxQBi P58546.
PaxDbi P58546.
PeptideAtlasi P58546.
PRIDEi P58546.

Protocols and materials databases

DNASUi 136319.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393085 ; ENSP00000376800 ; ENSG00000105887 .
GeneIDi 136319.
KEGGi hsa:136319.
UCSCi uc003vte.4. human.

Organism-specific databases

CTDi 136319.
GeneCardsi GC07M135613.
HGNCi HGNC:15667. MTPN.
HPAi HPA019735.
MIMi 606484. gene.
neXtProti NX_P58546.
PharmGKBi PA31271.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000276399.
HOVERGENi HBG019067.
InParanoidi P58546.
OMAi YEGHVTC.
OrthoDBi EOG7SBNQP.
PhylomeDBi P58546.
TreeFami TF327387.

Miscellaneous databases

ChiTaRSi MTPN. human.
EvolutionaryTracei P58546.
GeneWikii MTPN.
GenomeRNAii 136319.
NextBioi 83582.
PROi P58546.
SOURCEi Search...

Gene expression databases

Bgeei P58546.
CleanExi HS_MTPN.
ExpressionAtlasi P58546. baseline.
Genevestigatori P58546.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view ]
Pfami PF12796. Ank_2. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 2 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiMTPN_HUMAN
AccessioniPrimary (citable) accession number: P58546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3