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Q9NYL9

- TMOD3_HUMAN

UniProt

Q9NYL9 - TMOD3_HUMAN

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Protein

Tropomodulin-3

Gene

TMOD3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. tropomyosin binding Source: ProtInc
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: Chromosome 15

Organism-specific databases

HGNCiHGNC:11873. TMOD3.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. striated muscle thin filament Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36574.

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 – 251Phosphoserine3 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.
GenevestigatoriQ9NYL9.

Organism-specific databases

HPAiHPA001849.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi118899. 37 interactions.
IntActiQ9NYL9. 21 interactions.
MINTiMINT-1149880.
STRINGi9606.ENSP00000308753.

Structurei

3D structure databases

ProteinModelPortaliQ9NYL9.
SMRiQ9NYL9. Positions 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. Tropomodulin.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 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:
EMBL
GenBank
DDBJ
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.
XP_006720542.1. XM_006720479.1.
UniGeneiHs.4998.

Genome annotation databases

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

Polymorphism databases

DMDMi23396884.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10145.1.
PIRi T46384.
RefSeqi NP_055362.1. NM_014547.4.
XP_006720542.1. XM_006720479.1.
UniGenei Hs.4998.

3D structure databases

ProteinModelPortali Q9NYL9.
SMRi Q9NYL9. Positions 182-347.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118899. 37 interactions.
IntActi Q9NYL9. 21 interactions.
MINTi MINT-1149880.
STRINGi 9606.ENSP00000308753.

PTM databases

PhosphoSitei Q9NYL9.

Polymorphism databases

DMDMi 23396884.

2D gel databases

OGPi Q9NYL9.

Proteomic databases

MaxQBi Q9NYL9.
PaxDbi Q9NYL9.
PeptideAtlasi Q9NYL9.
PRIDEi Q9NYL9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308580 ; ENSP00000308753 ; ENSG00000138594 .
ENST00000544199 ; ENSP00000438909 ; ENSG00000138594 .
GeneIDi 29766.
KEGGi hsa:29766.
UCSCi uc002abn.3. human.

Organism-specific databases

CTDi 29766.
GeneCardsi GC15P052121.
HGNCi HGNC:11873. TMOD3.
HPAi HPA001849.
MIMi 605112. gene.
neXtProti NX_Q9NYL9.
PharmGKBi PA36574.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG329422.
GeneTreei ENSGT00760000119226.
HOGENOMi HOG000261624.
HOVERGENi HBG056172.
InParanoidi Q9NYL9.
KOi K10370.
OMAi NTHVKNF.
PhylomeDBi Q9NYL9.
TreeFami TF315841.

Miscellaneous databases

ChiTaRSi TMOD3. human.
GeneWikii TMOD3.
GenomeRNAii 29766.
NextBioi 52268.
PROi Q9NYL9.
SOURCEi Search...

Gene expression databases

Bgeei Q9NYL9.
CleanExi HS_TMOD3.
ExpressionAtlasi Q9NYL9. baseline and differential.
Genevestigatori Q9NYL9.

Family and domain databases

InterProi IPR004934. Tropomodulin.
[Graphical view ]
PANTHERi PTHR10901. PTHR10901. 1 hit.
Pfami PF03250. Tropomodulin. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: October 29, 2014
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
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