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Q9NYL9 (TMOD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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:
Tropomodulin-3
Alternative name(s):
Ubiquitous tropomodulin
Short name=U-Tmod
Gene names
Name:TMOD3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton By similarity.

Subunit structure

Binds to the N-terminus of tropomyosin and to actin By similarity.

Subcellular location

Cytoplasmcytoskeleton By similarity.

Tissue specificity

Ubiquitous. Ref.2

Sequence similarities

Belongs to the tropomodulin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentstriated muscle thin filament

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiontropomyosin binding

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Tropomodulin-3
PRO_0000186134

Amino acid modifications

Modified residue251Phosphoserine Ref.7 Ref.10 Ref.12

Experimental info

Sequence conflict271T → S in AAF31670. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NYL9 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8B7F2122C1BE9855

FASTA35239,595
        10         20         30         40         50         60 
MALPFRKDLE KYKDLDEDEL LGNLSETELK QLETVLDDLD PENALLPAGF RQKNQTSKST 

        70         80         90        100        110        120 
TGPFDREHLL SYLEKEALEH KDREDYVPYT GEKKGKIFIP KQKPVQTFTE EKVSLDPELE 

       130        140        150        160        170        180 
EALTSASDTE LCDLAAILGM HNLITNTKFC NIMGSSNGVD QEHFSNVVKG EKILPVFDEP 

       190        200        210        220        230        240 
PNPTNVEESL KRTKENDAHL VEVNLNNIKN IPIPTLKDFA KALETNTHVK CFSLAATRSN 

       250        260        270        280        290        300 
DPVATAFAEM LKVNKTLKSL NVESNFITGV GILALIDALR DNETLAELKI DNQRQQLGTA 

       310        320        330        340        350 
VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRVEGD HQ 

« Hide

References

« Hide 'large scale' references
[1]Conley C.A., Fowler V.M.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequencing, expression analysis, and mapping of three unique human tropomodulin genes and their mouse orthologs."
Cox P.R., Zoghbi H.Y.
Genomics 63:97-107(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"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: Adrenal gland.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-352.
Tissue: Testis.
[6]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 318-328, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237631 mRNA. Translation: AAF45299.1.
AF177171 mRNA. Translation: AAF31670.1.
AK312569 mRNA. Translation: BAG35464.1.
BC020542 mRNA. Translation: AAH20542.1.
AL137543 mRNA. Translation: CAB70801.1.
PIRT46384.
RefSeqNP_055362.1. NM_014547.4.
UniGeneHs.4998.

3D structure databases

ProteinModelPortalQ9NYL9.
SMRQ9NYL9. Positions 182-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118899. 37 interactions.
IntActQ9NYL9. 21 interactions.
MINTMINT-1149880.
STRING9606.ENSP00000308753.

PTM databases

PhosphoSiteQ9NYL9.

Polymorphism databases

DMDM23396884.

2D gel databases

OGPQ9NYL9.

Proteomic databases

PaxDbQ9NYL9.
PeptideAtlasQ9NYL9.
PRIDEQ9NYL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308580; ENSP00000308753; ENSG00000138594.
ENST00000544199; ENSP00000438909; ENSG00000138594.
GeneID29766.
KEGGhsa:29766.
UCSCuc002abn.3. human.

Organism-specific databases

CTD29766.
GeneCardsGC15P052121.
HGNCHGNC:11873. TMOD3.
HPAHPA001849.
MIM605112. gene.
neXtProtNX_Q9NYL9.
PharmGKBPA36574.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329422.
HOGENOMHOG000261624.
HOVERGENHBG056172.
InParanoidQ9NYL9.
KOK10370.
OMAQFCDIVG.
PhylomeDBQ9NYL9.
TreeFamTF315841.

Gene expression databases

ArrayExpressQ9NYL9.
BgeeQ9NYL9.
CleanExHS_TMOD3.
GenevestigatorQ9NYL9.

Family and domain databases

InterProIPR004934. Tropomodulin.
[Graphical view]
PANTHERPTHR10901. PTHR10901. 1 hit.
PfamPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMOD3. human.
GeneWikiTMOD3.
GenomeRNAi29766.
NextBio52268.
PROQ9NYL9.
SOURCESearch...

Entry information

Entry nameTMOD3_HUMAN
AccessionPrimary (citable) accession number: Q9NYL9
Secondary accession number(s): B2R6G7, Q9NT43, Q9NZR0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 106 of the entry and version 1 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

MIM cross-references

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

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM