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Protein

Tropomodulin-3

Gene

TMOD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 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

  • tropomyosin binding Source: ProtInc

GO - Biological processi

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:11873. TMOD3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36574.

Polymorphism and mutation databases

BioMutaiTMOD3.
DMDMi23396884.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Tropomodulin-3PRO_0000186134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NYL9.
PaxDbiQ9NYL9.
PeptideAtlasiQ9NYL9.
PRIDEiQ9NYL9.

2D gel databases

OGPiQ9NYL9.

PTM databases

PhosphoSiteiQ9NYL9.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9NYL9.
CleanExiHS_TMOD3.
ExpressionAtlasiQ9NYL9. baseline and differential.
GenevisibleiQ9NYL9. HS.

Organism-specific databases

HPAiHPA001849.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi118899. 40 interactions.
IntActiQ9NYL9. 22 interactions.
MINTiMINT-1149880.
STRINGi9606.ENSP00000308753.

Structurei

3D structure databases

ProteinModelPortaliQ9NYL9.
SMRiQ9NYL9. Positions 61-101, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tropomodulin family.Curated

Phylogenomic databases

eggNOGiNOG329422.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9NYL9.
KOiK10370.
OMAiNTHVKNF.
PhylomeDBiQ9NYL9.
TreeFamiTF315841.

Family and domain databases

InterProiIPR004934. TMOD.
IPR030133. TMOD3.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF15. PTHR10901:SF15. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NYL9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPFRKDLE KYKDLDEDEL LGNLSETELK QLETVLDDLD PENALLPAGF
60 70 80 90 100
RQKNQTSKST TGPFDREHLL SYLEKEALEH KDREDYVPYT GEKKGKIFIP
110 120 130 140 150
KQKPVQTFTE EKVSLDPELE EALTSASDTE LCDLAAILGM HNLITNTKFC
160 170 180 190 200
NIMGSSNGVD QEHFSNVVKG EKILPVFDEP PNPTNVEESL KRTKENDAHL
210 220 230 240 250
VEVNLNNIKN IPIPTLKDFA KALETNTHVK CFSLAATRSN DPVATAFAEM
260 270 280 290 300
LKVNKTLKSL NVESNFITGV GILALIDALR DNETLAELKI DNQRQQLGTA
310 320 330 340 350
VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRVEGD

HQ
Length:352
Mass (Da):39,595
Last modified:October 1, 2000 - v1
Checksum:i8B7F2122C1BE9855
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271T → S in AAF31670 (PubMed:10662549).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10145.1.
PIRiT46384.
RefSeqiNP_055362.1. NM_014547.4.
UniGeneiHs.4998.

Genome annotation databases

EnsembliENST00000308580; ENSP00000308753; ENSG00000138594.
ENST00000544199; ENSP00000438909; ENSG00000138594.
GeneIDi29766.
KEGGihsa:29766.
UCSCiuc002abn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10145.1.
PIRiT46384.
RefSeqiNP_055362.1. NM_014547.4.
UniGeneiHs.4998.

3D structure databases

ProteinModelPortaliQ9NYL9.
SMRiQ9NYL9. Positions 61-101, 182-347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118899. 40 interactions.
IntActiQ9NYL9. 22 interactions.
MINTiMINT-1149880.
STRINGi9606.ENSP00000308753.

PTM databases

PhosphoSiteiQ9NYL9.

Polymorphism and mutation databases

BioMutaiTMOD3.
DMDMi23396884.

2D gel databases

OGPiQ9NYL9.

Proteomic databases

MaxQBiQ9NYL9.
PaxDbiQ9NYL9.
PeptideAtlasiQ9NYL9.
PRIDEiQ9NYL9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308580; ENSP00000308753; ENSG00000138594.
ENST00000544199; ENSP00000438909; ENSG00000138594.
GeneIDi29766.
KEGGihsa:29766.
UCSCiuc002abn.3. human.

Organism-specific databases

CTDi29766.
GeneCardsiGC15P052121.
HGNCiHGNC:11873. TMOD3.
HPAiHPA001849.
MIMi605112. gene.
neXtProtiNX_Q9NYL9.
PharmGKBiPA36574.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG329422.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiQ9NYL9.
KOiK10370.
OMAiNTHVKNF.
PhylomeDBiQ9NYL9.
TreeFamiTF315841.

Miscellaneous databases

ChiTaRSiTMOD3. human.
GeneWikiiTMOD3.
GenomeRNAii29766.
NextBioi52268.
PROiQ9NYL9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYL9.
CleanExiHS_TMOD3.
ExpressionAtlasiQ9NYL9. baseline and differential.
GenevisibleiQ9NYL9. HS.

Family and domain databases

InterProiIPR004934. TMOD.
IPR030133. TMOD3.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PTHR10901:SF15. PTHR10901:SF15. 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], 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.
    , 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. 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. 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. 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].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTMOD3_HUMAN
AccessioniPrimary (citable) accession number: Q9NYL9
Secondary accession number(s): B2R6G7, Q9NT43, Q9NZR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: October 1, 2000
Last modified: June 24, 2015
This is version 117 of the entry and version 1 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.