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HUMAN:TMOD1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) TMOD1 (synonyms: D9S57E, TMOD)
Protein Name(s) Tropomodulin-1

Erythrocyte tropomodulin E-Tmod

External Links
UniProt P28289
EMBL M77016
AF288155
AF288147
AF288148
AF288149
AF288150
AF288151
AF288152
AF288153
AF288154
AK095748
AK314533
AL162385
BC002660
CCDS CCDS6726.1
PIR A42336
RefSeq NP_001159588.1
NP_003266.1
UniGene Hs.404289
Hs.723236
PDB 4PKG
4PKH
4PKI
PDBsum 4PKG
4PKH
4PKI
ProteinModelPortal P28289
SMR P28289
BioGrid 112966
IntAct P28289
STRING 9606.ENSP00000259365
PhosphoSite P28289
DMDM 135922
MaxQB P28289
PaxDb P28289
PeptideAtlas P28289
PRIDE P28289
DNASU 7111
Ensembl ENST00000259365
ENST00000375175
ENST00000395211
GeneID 7111
KEGG hsa:7111
UCSC uc004axk.2
CTD 7111
GeneCards GC09P100263
HGNC HGNC:11871
HPA HPA051202
MIM 190930
neXtProt NX_P28289
PharmGKB PA36572
eggNOG NOG329422
GeneTree ENSGT00760000119226
HOGENOM HOG000261624
HOVERGEN HBG056172
InParanoid P28289
KO K10370
OMA STIVNKQ
OrthoDB EOG7D59Q1
PhylomeDB P28289
TreeFam TF315841
Reactome REACT_16969
ChiTaRS TMOD1
GeneWiki TMOD1
GenomeRNAi 7111
NextBio 27835
PRO PR:P28289
Proteomes UP000005640
Bgee P28289
CleanEx HS_TMOD1
ExpressionAtlas P28289
Genevestigator P28289
GO GO:0030863
GO:0005829
GO:0016020
GO:0030016
GO:0008344
GO:0030049
GO:0030239
InterPro IPR004934
IPR030135
PANTHER PTHR10901
PTHR10901:SF8
Pfam PF03250

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0030838

positive regulation of actin filament polymerization

PMID:20650902[1]

ECO:0000314

P

FIGURE 1. Mammalian Tmod1–3 promote spontaneous actin polymerization.

complete

enables

GO:0003779

actin binding

PMID:26370058[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005865

striated muscle thin filament

PMID:25250574[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005865

striated muscle thin filament

PMID:25250574[3]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0002372)

Seeded From UniProt

complete

part_of

GO:0030017

sarcomere

PMID:26370058[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030016

myofibril

PMID:26370058[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005884

actin filament

PMID:26370058[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

colocalizes_with

GO:0008180

COP9 signalosome

PMID:18850735[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030239

myofibril assembly

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:98775
PANTHER:PTN000096564

P

Seeded From UniProt

complete

part_of

GO:0030016

myofibril

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:98775
PANTHER:PTN000096564
UniProtKB:P28289
UniProtKB:P29536
UniProtKB:Q6P5Q4

C

Seeded From UniProt

complete

involved_in

GO:0006936

muscle contraction

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:98775
PANTHER:PTN000096567
ZFIN:ZDB-GENE-090313-353

P

Seeded From UniProt

complete

part_of

GO:0005865

striated muscle thin filament

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1355285
MGI:MGI:1355315
PANTHER:PTN000096567
UniProtKB:H9KZU7
UniProtKB:P28289
UniProtKB:Q0VAK6
UniProtKB:Q9NZQ9

C

Seeded From UniProt

complete

enables

GO:0005523

tropomyosin binding

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1355285
MGI:MGI:1355315
MGI:MGI:98775
PANTHER:PTN000096563
RGD:3874
RGD:61948
UniProtKB:Q0VAK6
UniProtKB:Q6P5Q4

F

Seeded From UniProt

complete

involved_in

GO:0070307

lens fiber cell development

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

P

Seeded From UniProt

complete

part_of

GO:0030863

cortical cytoskeleton

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

C

Seeded From UniProt

complete

involved_in

GO:0030239

myofibril assembly

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

P

Seeded From UniProt

complete

part_of

GO:0030017

sarcomere

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

C

Seeded From UniProt

complete

part_of

GO:0030016

myofibril

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

C

Seeded From UniProt

complete

involved_in

GO:0008344

adult locomotory behavior

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

P

Seeded From UniProt

complete

involved_in

GO:0006936

muscle contraction

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

P

Seeded From UniProt

complete

enables

GO:0005523

tropomyosin binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P49813
ensembl:ENSMUSP00000103402

F

Seeded From UniProt

complete

enables

GO:0005523

tropomyosin binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004934
InterPro:IPR030135

F

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR030135

F

Seeded From UniProt

complete

involved_in

GO:0051694

pointed-end actin filament capping

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004934
InterPro:IPR030135

P

Seeded From UniProt

complete

involved_in

GO:0030049

muscle filament sliding

Reactome:R-HSA-390522

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-390598
Reactome:R-HSA-390597
Reactome:R-HSA-390595
Reactome:R-HSA-390593

ECO:0000304

author statement supported by traceable reference used in manual assertion




C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206
UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Yamashiro, S et al. (2010) Mammalian tropomodulins nucleate actin polymerization via their actin monomer binding and filament pointed end-capping activities. J. Biol. Chem. 285 33265-80 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 Boczkowska, M et al. (2015) How Leiomodin and Tropomodulin use a common fold for different actin assembly functions. Nat Commun 6 8314 PubMed GONUTS page
  3. ↑ 3.0 3.1 Yuen, M et al. (2014) Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy. J. Clin. Invest. 124 4693-708 PubMed GONUTS page
  4. ↑ Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 5.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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