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P28289 (TMOD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tropomodulin-1
Alternative name(s):
Erythrocyte tropomodulin
Short name=E-Tmod
Gene names
Name:TMOD1
Synonyms:D9S57E, TMOD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 atits N-terminus. Ref.6

Subunit structure

Binds to the N-terminus of isoforms 2/3 of TPM3 and to actin. Ref.6

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Highly expressed in the erythrocyte, heart and skeletal muscle.

Sequence similarities

Belongs to the tropomodulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Tropomodulin-1
PRO_0000186128

Regions

Region39 – 138100Tropomyosin-binding Potential

Experimental info

Sequence conflict171E → K in AAH02660. Ref.5
Sequence conflict761K → E in BAG37124. Ref.3
Sequence conflict2891N → S in BAG37124. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P28289 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 732B7D7798B88A48

FASTA35940,569
        10         20         30         40         50         60 
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG 

        70         80         90        100        110        120 
PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ KPLDPVLESV TLEPELEEAL 

       130        140        150        160        170        180 
ANASDAELCD IAAILGMHTL MSNQQYYQAL SSSSIMNKEG LNSVIKPTQY KPVPDEEPNS 

       190        200        210        220        230        240 
TDVEETLERI KNNDPKLEEV NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV 

       250        260        270        280        290        300 
AYALAEMLKE NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVEMKIDNQ SQPLGNKVEM 

       310        320        330        340        350 
EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP IIPKCRSGV 

« Hide

References

« Hide 'large scale' references
[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], 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. expand/collapse author list , 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]"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. expand/collapse author list , 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].
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77016 mRNA. Translation: AAA61224.1.
AF288155 expand/collapse EMBL AC list , AF288147, AF288148, AF288149, AF288150, AF288151, AF288152, AF288153, AF288154 Genomic DNA. Translation: AAG30124.1.
AK314533 mRNA. Translation: BAG37124.1.
AL162385 Genomic DNA. Translation: CAI12854.1.
BC002660 mRNA. Translation: AAH02660.1.
CCDSCCDS6726.1.
PIRA42336.
RefSeqNP_001159588.1. NM_001166116.1.
NP_003266.1. NM_003275.3.
UniGeneHs.404289.
Hs.723236.

3D structure databases

ProteinModelPortalP28289.
SMRP28289. Positions 179-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112966. 3 interactions.
IntActP28289. 1 interaction.
STRING9606.ENSP00000259365.

PTM databases

PhosphoSiteP28289.

Polymorphism databases

DMDM135922.

Proteomic databases

MaxQBP28289.
PaxDbP28289.
PeptideAtlasP28289.
PRIDEP28289.

Protocols and materials databases

DNASU7111.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259365; ENSP00000259365; ENSG00000136842.
ENST00000395211; ENSP00000378637; ENSG00000136842.
GeneID7111.
KEGGhsa:7111.
UCSCuc004axk.2. human.

Organism-specific databases

CTD7111.
GeneCardsGC09P100263.
HGNCHGNC:11871. TMOD1.
HPAHPA051202.
MIM190930. gene.
neXtProtNX_P28289.
PharmGKBPA36572.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG329422.
HOGENOMHOG000261624.
HOVERGENHBG056172.
InParanoidP28289.
KOK10370.
OMASTIVNKQ.
OrthoDBEOG7D59Q1.
PhylomeDBP28289.
TreeFamTF315841.

Enzyme and pathway databases

ReactomeREACT_17044. Muscle contraction.

Gene expression databases

ArrayExpressP28289.
BgeeP28289.
CleanExHS_TMOD1.
GenevestigatorP28289.

Family and domain databases

InterProIPR004934. Tropomodulin.
[Graphical view]
PANTHERPTHR10901. PTHR10901. 1 hit.
PfamPF03250. Tropomodulin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTMOD1. human.
GeneWikiTMOD1.
GenomeRNAi7111.
NextBio27835.
PROP28289.
SOURCESearch...

Entry information

Entry nameTMOD1_HUMAN
AccessionPrimary (citable) accession number: P28289
Secondary accession number(s): B2RB77, Q9BUF1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM