P28289 (TMOD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tropomodulin-1

Alternative name(s):
Erythrocyte tropomodulin
Short name=E-Tmod

Gene names

Name:	TMOD1
Synonyms:	D9S57E, TMOD

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence 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 at its N-terminus. Ref.6
Subunit structure	Binds to the N-terminus of isoforms 2/3 of TPM3 and to actin. Ref.6
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	Highly expressed in the erythrocyte, heart and skeletal muscle.
Sequence similarities	Belongs to the tropomodulin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	Actin-binding
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adult locomotory behavior Inferred from electronic annotation. Source: Compara muscle filament sliding Traceable author statement. Source: Reactome myofibril assembly Inferred from electronic annotation. Source: Compara
Cellular_component	cortical cytoskeleton Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome membrane Inferred from electronic annotation. Source: Compara myofibril Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Tropomodulin-1		PRO_0000186128
Regions
	Region	39 – 138	100	Tropomyosin-binding Potential
Experimental info
	Sequence conflict	17	1	E → K in AAH02660. Ref.5
	Sequence conflict	76	1	K → E in BAG37124. Ref.3
	Sequence conflict	289	1	N → S in BAG37124. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P28289 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 732B7D7798B88A48	FASTA	359	40,569
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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 , 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.
IPI	IPI00002375.
PIR	A42336.
RefSeq	NP_001159588.1. NM_001166116.1. NP_003266.1. NM_003275.3.
UniGene	Hs.404289. Hs.723236.
3D structure databases
ProteinModelPortal	P28289.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28289. 1 interaction.
STRING	9606.ENSP00000259365.
PTM databases
PhosphoSite	P28289.
Polymorphism databases
DMDM	135922.
Proteomic databases
PaxDb	P28289.
PeptideAtlas	P28289.
PRIDE	P28289.
Protocols and materials databases
DNASU	7111.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000259365; ENSP00000259365; ENSG00000136842. ENST00000395211; ENSP00000378637; ENSG00000136842.
GeneID	7111.
KEGG	hsa:7111.
UCSC	uc004axk.2. human.
Organism-specific databases
CTD	7111.
GeneCards	GC09P100263.
HGNC	HGNC:11871. TMOD1.
HPA	HPA051202.
MIM	190930. gene.
neXtProt	NX_P28289.
PharmGKB	PA36572.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG329422.
HOGENOM	HOG000261624.
HOVERGEN	HBG056172.
InParanoid	P28289.
KO	K10370.
OMA	QTKKAPT.
OrthoDB	EOG42FSJ1.
PhylomeDB	P28289.
Enzyme and pathway databases
Reactome	REACT_17044. Muscle contraction.
Gene expression databases
ArrayExpress	P28289.
Bgee	P28289.
CleanEx	HS_TMOD1.
Genevestigator	P28289.
GermOnline	ENSG00000136842. Homo sapiens.
Family and domain databases
InterPro	IPR004934. Tropomodulin. [Graphical view]
PANTHER	PTHR10901. PTHR10901. 1 hit.
Pfam	PF03250. Tropomodulin. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TMOD1. human.
GenomeRNAi	7111.
NextBio	27835.
SOURCE	Search...

Entry information

Entry name

TMOD1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.