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P28289

- TMOD1_HUMAN

UniProt

P28289 - TMOD1_HUMAN

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Protein

Tropomodulin-1

Gene

TMOD1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus.1 Publication

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. muscle filament sliding Source: Reactome
  3. myofibril assembly Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomodulin-1
Alternative name(s):
Erythrocyte tropomodulin
Short name:
E-Tmod
Gene namesi
Name:TMOD1
Synonyms:D9S57E, TMOD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:11871. TMOD1.

Subcellular locationi

GO - Cellular componenti

  1. cortical cytoskeleton Source: Ensembl
  2. cytosol Source: Reactome
  3. membrane Source: Ensembl
  4. myofibril Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36572.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Tropomodulin-1PRO_0000186128Add
BLAST

Proteomic databases

MaxQBiP28289.
PaxDbiP28289.
PeptideAtlasiP28289.
PRIDEiP28289.

PTM databases

PhosphoSiteiP28289.

Expressioni

Tissue specificityi

Highly expressed in the erythrocyte, heart and skeletal muscle.

Gene expression databases

BgeeiP28289.
CleanExiHS_TMOD1.
ExpressionAtlasiP28289. baseline and differential.
GenevestigatoriP28289.

Organism-specific databases

HPAiHPA051202.

Interactioni

Subunit structurei

Binds to the N-terminus of isoforms 2/3 of TPM3 and to actin.

Protein-protein interaction databases

BioGridi112966. 14 interactions.
IntActiP28289. 1 interaction.
STRINGi9606.ENSP00000259365.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PKGX-ray1.80G50-101[»]
4PKHX-ray2.15B/E/G/J50-101[»]
4PKIX-ray2.30G160-349[»]
ProteinModelPortaliP28289.
SMRiP28289. Positions 179-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni39 – 138100Tropomyosin-bindingSequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the tropomodulin family.Curated

Phylogenomic databases

eggNOGiNOG329422.
GeneTreeiENSGT00760000119226.
HOGENOMiHOG000261624.
HOVERGENiHBG056172.
InParanoidiP28289.
KOiK10370.
OMAiSTIVNKQ.
OrthoDBiEOG7D59Q1.
PhylomeDBiP28289.
TreeFamiTF315841.

Family and domain databases

InterProiIPR004934. Tropomodulin.
[Graphical view]
PANTHERiPTHR10901. PTHR10901. 1 hit.
PfamiPF03250. Tropomodulin. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28289-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ
60 70 80 90 100
KDQTTKAPTG PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ
110 120 130 140 150
KPLDPVLESV TLEPELEEAL ANASDAELCD IAAILGMHTL MSNQQYYQAL
160 170 180 190 200
SSSSIMNKEG LNSVIKPTQY KPVPDEEPNS TDVEETLERI KNNDPKLEEV
210 220 230 240 250
NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV AYALAEMLKE
260 270 280 290 300
NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVEMKIDNQ SQPLGNKVEM
310 320 330 340 350
EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP

IIPKCRSGV
Length:359
Mass (Da):40,569
Last modified:December 1, 1992 - v1
Checksum:i732B7D7798B88A48
GO
Isoform 2 (identifier: P28289-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MSYRRE → MSQVLS
     7-133: Missing.

Note: No experimental confirmation available

Show »
Length:232
Mass (Da):26,014
Checksum:i80DEC95EB154DF1F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171E → K in AAH02660. (PubMed:15489334)Curated
Sequence conflicti76 – 761K → E in BAG37124. (PubMed:14702039)Curated
Sequence conflicti289 – 2891N → S in BAG37124. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MSYRRE → MSQVLS in isoform 2. 1 PublicationVSP_056863
Alternative sequencei7 – 133127Missing in isoform 2. 1 PublicationVSP_056864Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77016 mRNA. Translation: AAA61224.1.
AF288155
, AF288147, AF288148, AF288149, AF288150, AF288151, AF288152, AF288153, AF288154 Genomic DNA. Translation: AAG30124.1.
AK095748 mRNA. Translation: BAG53119.1.
AK314533 mRNA. Translation: BAG37124.1.
AL162385 Genomic DNA. Translation: CAI12854.1.
BC002660 mRNA. Translation: AAH02660.1.
CCDSiCCDS6726.1.
PIRiA42336.
RefSeqiNP_001159588.1. NM_001166116.1.
NP_003266.1. NM_003275.3.
UniGeneiHs.404289.
Hs.723236.

Genome annotation databases

EnsembliENST00000259365; ENSP00000259365; ENSG00000136842.
ENST00000395211; ENSP00000378637; ENSG00000136842.
GeneIDi7111.
KEGGihsa:7111.
UCSCiuc004axk.2. human.

Polymorphism databases

DMDMi135922.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M77016 mRNA. Translation: AAA61224.1 .
AF288155
, AF288147 , AF288148 , AF288149 , AF288150 , AF288151 , AF288152 , AF288153 , AF288154 Genomic DNA. Translation: AAG30124.1 .
AK095748 mRNA. Translation: BAG53119.1 .
AK314533 mRNA. Translation: BAG37124.1 .
AL162385 Genomic DNA. Translation: CAI12854.1 .
BC002660 mRNA. Translation: AAH02660.1 .
CCDSi CCDS6726.1.
PIRi A42336.
RefSeqi NP_001159588.1. NM_001166116.1.
NP_003266.1. NM_003275.3.
UniGenei Hs.404289.
Hs.723236.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4PKG X-ray 1.80 G 50-101 [» ]
4PKH X-ray 2.15 B/E/G/J 50-101 [» ]
4PKI X-ray 2.30 G 160-349 [» ]
ProteinModelPortali P28289.
SMRi P28289. Positions 179-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112966. 14 interactions.
IntActi P28289. 1 interaction.
STRINGi 9606.ENSP00000259365.

PTM databases

PhosphoSitei P28289.

Polymorphism databases

DMDMi 135922.

Proteomic databases

MaxQBi P28289.
PaxDbi P28289.
PeptideAtlasi P28289.
PRIDEi P28289.

Protocols and materials databases

DNASUi 7111.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259365 ; ENSP00000259365 ; ENSG00000136842 .
ENST00000395211 ; ENSP00000378637 ; ENSG00000136842 .
GeneIDi 7111.
KEGGi hsa:7111.
UCSCi uc004axk.2. human.

Organism-specific databases

CTDi 7111.
GeneCardsi GC09P100263.
HGNCi HGNC:11871. TMOD1.
HPAi HPA051202.
MIMi 190930. gene.
neXtProti NX_P28289.
PharmGKBi PA36572.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG329422.
GeneTreei ENSGT00760000119226.
HOGENOMi HOG000261624.
HOVERGENi HBG056172.
InParanoidi P28289.
KOi K10370.
OMAi STIVNKQ.
OrthoDBi EOG7D59Q1.
PhylomeDBi P28289.
TreeFami TF315841.

Enzyme and pathway databases

Reactomei REACT_16969. Striated Muscle Contraction.

Miscellaneous databases

ChiTaRSi TMOD1. human.
GeneWikii TMOD1.
GenomeRNAii 7111.
NextBioi 27835.
PROi P28289.
SOURCEi Search...

Gene expression databases

Bgeei P28289.
CleanExi HS_TMOD1.
ExpressionAtlasi P28289. baseline and differential.
Genevestigatori P28289.

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. "Molecular cloning and characterization of human fetal liver tropomodulin. A tropomyosin-binding protein."
    Sung L.A., Fowler V.M., Lambert K., Sussman M.A., Karr D., Chien S.
    J. Biol. Chem. 267:2616-2621(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Fetal liver.
  2. "Genomic organization of mouse and human erythrocyte tropomodulin genes encoding the pointed end capping protein for the actin filaments."
    Chu X., Thompson D., Yee L.J., Sung L.A.
    Gene 256:271-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORMS 1 AND 2).
    Tissue: Brain.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Uterus.
  6. "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a tropomyosin isoform encoded by the gamma-tropomyosin gene."
    Sung L.A., Lin J.J.-C.
    Biochem. Biophys. Res. Commun. 201:627-634(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TPM3.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTMOD1_HUMAN
AccessioniPrimary (citable) accession number: P28289
Secondary accession number(s): B2RB77, Q5T7W3, Q9BUF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 121 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3