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Protein

Tropomodulin-3

Gene

Tmod3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • microtubule minus-end binding Source: MGI
  • tropomyosin binding Source: MGI

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • erythrocyte development Source: MGI
  • negative regulation of cellular component movement Source: MGI
  • pointed-end actin filament capping Source: MGI
  • positive regulation of mitotic cell cycle phase transition Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomodulin-3
Alternative name(s):
Ubiquitous tropomodulin
Short name:
U-Tmod
Gene namesi
Name:Tmod3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1355315. Tmod3.

Subcellular locationi

GO - Cellular componenti

  • filamentous actin Source: MGI
  • lamellipodium Source: MGI
  • ruffle Source: MGI
  • striated muscle thin filament Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Tropomodulin-3PRO_0000186135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JHJ0.
MaxQBiQ9JHJ0.
PaxDbiQ9JHJ0.
PRIDEiQ9JHJ0.

PTM databases

iPTMnetiQ9JHJ0.
PhosphoSiteiQ9JHJ0.

Miscellaneous databases

PMAP-CutDBQ9JHJ0.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ9JHJ0.
CleanExiMM_TMOD3.
GenevisibleiQ9JHJ0. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • microtubule minus-end binding Source: MGI
  • tropomyosin binding Source: MGI

Protein-protein interaction databases

BioGridi206138. 91 interactions.
IntActiQ9JHJ0. 91 interactions.
MINTiMINT-1852170.
STRINGi10090.ENSMUSP00000072087.

Structurei

3D structure databases

ProteinModelPortaliQ9JHJ0.
SMRiQ9JHJ0. Positions 61-101, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tropomodulin family.Curated

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9JHJ0.
KOiK10370.
OMAiNTHVKNF.
OrthoDBiEOG7D59Q1.
PhylomeDBiQ9JHJ0.
TreeFamiTF315841.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030133. TMOD3.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF18. PTHR10901:SF18. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHJ0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPFRKDLG DYKDLDEDEL LGKLSESELK QLETVLDDLD PENALLPAGF
60 70 80 90 100
RQKNQTSKSA TGPFDRERLL SYLEKQALEH KDRDDYVPYT GEKKGKIFIP
110 120 130 140 150
KQKPAQTLTE ETISLDPELE EALTSASDTE LCDLAAILGM HNLIADTPFC
160 170 180 190 200
DVLGSSNGVN QERFPNVVKG EKILPVFDEP PNPTNVEESL KRIRENDARL
210 220 230 240 250
VEVNLNNIKN IPIPTLKDFA KTLEANTHVK HFSLAATRSN DPVAVAFADM
260 270 280 290 300
LKVNKTLKSL NMESNFITGA GVLALIDALR DNETLMELKI DNQRQQLGTS
310 320 330 340 350
VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRIEGD

HQ
Length:352
Mass (Da):39,503
Last modified:October 1, 2000 - v1
Checksum:i6F8602C74C2AEF9C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237630 mRNA. Translation: AAF45298.1.
AF177172 mRNA. Translation: AAF31671.1.
AK050372 mRNA. Translation: BAC34216.1.
AK167723 mRNA. Translation: BAE39765.1.
BC082595 mRNA. Translation: AAH82595.1.
CCDSiCCDS23344.1.
RefSeqiNP_058659.1. NM_016963.2.
UniGeneiMm.38445.

Genome annotation databases

EnsembliENSMUST00000072232; ENSMUSP00000072087; ENSMUSG00000058587.
GeneIDi50875.
KEGGimmu:50875.
UCSCiuc009qsi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237630 mRNA. Translation: AAF45298.1.
AF177172 mRNA. Translation: AAF31671.1.
AK050372 mRNA. Translation: BAC34216.1.
AK167723 mRNA. Translation: BAE39765.1.
BC082595 mRNA. Translation: AAH82595.1.
CCDSiCCDS23344.1.
RefSeqiNP_058659.1. NM_016963.2.
UniGeneiMm.38445.

3D structure databases

ProteinModelPortaliQ9JHJ0.
SMRiQ9JHJ0. Positions 61-101, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206138. 91 interactions.
IntActiQ9JHJ0. 91 interactions.
MINTiMINT-1852170.
STRINGi10090.ENSMUSP00000072087.

PTM databases

iPTMnetiQ9JHJ0.
PhosphoSiteiQ9JHJ0.

Proteomic databases

EPDiQ9JHJ0.
MaxQBiQ9JHJ0.
PaxDbiQ9JHJ0.
PRIDEiQ9JHJ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072232; ENSMUSP00000072087; ENSMUSG00000058587.
GeneIDi50875.
KEGGimmu:50875.
UCSCiuc009qsi.1. mouse.

Organism-specific databases

CTDi29766.
MGIiMGI:1355315. Tmod3.

Phylogenomic databases

eggNOGiKOG3735. Eukaryota.
ENOG410YAHM. LUCA.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9JHJ0.
KOiK10370.
OMAiNTHVKNF.
OrthoDBiEOG7D59Q1.
PhylomeDBiQ9JHJ0.
TreeFamiTF315841.

Miscellaneous databases

ChiTaRSiTmod3. mouse.
PMAP-CutDBQ9JHJ0.
PROiQ9JHJ0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHJ0.
CleanExiMM_TMOD3.
GenevisibleiQ9JHJ0. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR004934. TMOD.
IPR030133. TMOD3.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF18. PTHR10901:SF18. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  3. "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.
    , 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: Liver and Placenta.
  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].
    Strain: C57BL/6J.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTMOD3_MOUSE
AccessioniPrimary (citable) accession number: Q9JHJ0
Secondary accession number(s): Q3TIT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.