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Protein

Tropomyosin alpha-4 chain

Gene

TPM4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. Binds calcium.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • structural constituent of muscle Source: ProtInc

GO - Biological processi

  • movement of cell or subcellular component Source: UniProtKB
  • muscle contraction Source: Reactome
  • muscle filament sliding Source: Reactome
  • osteoblast differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Names & Taxonomyi

Protein namesi
Recommended name:
Tropomyosin alpha-4 chain
Alternative name(s):
TM30p1
Tropomyosin-4
Gene namesi
Name:TPM4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:12013. TPM4.

Subcellular locationi

GO - Cellular componenti

  • cortical cytoskeleton Source: Ensembl
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • filamentous actin Source: Ensembl
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • muscle thin filament tropomyosin Source: ProtInc
  • podosome Source: Ensembl
  • stress fiber Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

Orphaneti178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA36693.

Polymorphism and mutation databases

BioMutaiTPM4.
DMDMi54039751.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 248247Tropomyosin alpha-4 chainPRO_0000205635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei177 – 1771N6-acetyllysine1 Publication
Modified residuei215 – 2151N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP67936.
PaxDbiP67936.
PeptideAtlasiP67936.
PRIDEiP67936.

2D gel databases

DOSAC-COBS-2DPAGEP67936.
OGPiP07226.

PTM databases

PhosphoSiteiP67936.

Expressioni

Tissue specificityi

Detected in cardiac tissue and platelets, the form found in cardiac tissue is a higher molecular weight than the form found in platelets. Expressed at higher levels in the platelets of hypertensive patients with cardiac hypertrophy than in the platelets of hypertensive patients without cardiac hypertrophy (at protein level).1 Publication

Gene expression databases

BgeeiP67936.
CleanExiHS_TPM4.
ExpressionAtlasiP67936. baseline and differential.
GenevestigatoriP67936.

Organism-specific databases

HPAiCAB004685.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.By similarity

Protein-protein interaction databases

BioGridi113024. 49 interactions.
IntActiP67936. 7 interactions.
MINTiMINT-4138291.

Structurei

3D structure databases

ProteinModelPortaliP67936.
SMRiP67936. Positions 5-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 248247By similarityAdd
BLAST

Domaini

The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

Sequence similaritiesi

Belongs to the tropomyosin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
InParanoidiP67936.
KOiK10375.
OMAiLTICETE.
PhylomeDBiP67936.
TreeFamiTF351519.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P67936-1) [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
MAGLNSLEAV KRKIQALQQQ ADEAEDRAQG LQRELDGERE RREKAEGDVA
60 70 80 90 100
ALNRRIQLVE EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRAMK
110 120 130 140 150
DEEKMEIQEM QLKEAKHIAE EADRKYEEVA RKLVILEGEL ERAEERAEVS
160 170 180 190 200
ELKCGDLEEE LKNVTNNLKS LEAASEKYSE KEDKYEEEIK LLSDKLKEAE
210 220 230 240
TRAEFAERTV AKLEKTIDDL EEKLAQAKEE NVGLHQTLDQ TLNELNCI
Length:248
Mass (Da):28,522
Last modified:January 23, 2007 - v3
Checksum:i5D5CDF6BF76552A8
GO
Isoform 2 (identifier: P67936-2) [UniParc] [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: MAGLNSLEAV...LDGERERREK → MEAIKKKMQM...LELTEKKASD

Show »
Length:284
Mass (Da):32,723
Checksum:i29C0F6ADF4C87F0C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591V → F in AAH02827 (PubMed:15489334).Curated
Sequence conflicti152 – 1521L → S in AAA36774 (PubMed:3865200).Curated
Sequence conflicti162 – 1632KN → RT in AAA36774 (PubMed:3865200).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti204 – 2041E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036535

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4444MAGLN…ERREK → MEAIKKKMQMLKLDKENAID RAEQAEADKKAAEDKCKQVE EELTHLQKKLKGTEDELDKY SEDLKDAQEKLELTEKKASD in isoform 2. 1 PublicationVSP_006611Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05276 mRNA. Translation: CAA28888.1.
AK023385 mRNA. Translation: BAB14554.1.
AK315076 mRNA. Translation: BAG37545.1.
BT019634 mRNA. Translation: AAV38440.1.
CH471106 Genomic DNA. Translation: EAW84521.1.
BC002827 mRNA. Translation: AAH02827.1.
BC037576 mRNA. Translation: AAH37576.1.
BC067225 mRNA. Translation: AAH67225.1.
M12127 mRNA. Translation: AAA36774.1.
CCDSiCCDS12338.1.
CCDS46007.1. [P67936-2]
PIRiS07282.
RefSeqiNP_001138632.1. NM_001145160.1. [P67936-2]
NP_003281.1. NM_003290.2. [P67936-1]
UniGeneiHs.631618.

Genome annotation databases

EnsembliENST00000300933; ENSP00000300933; ENSG00000167460. [P67936-1]
ENST00000344824; ENSP00000345230; ENSG00000167460. [P67936-2]
GeneIDi7171.
KEGGihsa:7171.
UCSCiuc002ndi.2. human. [P67936-2]
uc002ndj.2. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05276 mRNA. Translation: CAA28888.1.
AK023385 mRNA. Translation: BAB14554.1.
AK315076 mRNA. Translation: BAG37545.1.
BT019634 mRNA. Translation: AAV38440.1.
CH471106 Genomic DNA. Translation: EAW84521.1.
BC002827 mRNA. Translation: AAH02827.1.
BC037576 mRNA. Translation: AAH37576.1.
BC067225 mRNA. Translation: AAH67225.1.
M12127 mRNA. Translation: AAA36774.1.
CCDSiCCDS12338.1.
CCDS46007.1. [P67936-2]
PIRiS07282.
RefSeqiNP_001138632.1. NM_001145160.1. [P67936-2]
NP_003281.1. NM_003290.2. [P67936-1]
UniGeneiHs.631618.

3D structure databases

ProteinModelPortaliP67936.
SMRiP67936. Positions 5-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113024. 49 interactions.
IntActiP67936. 7 interactions.
MINTiMINT-4138291.

PTM databases

PhosphoSiteiP67936.

Polymorphism and mutation databases

BioMutaiTPM4.
DMDMi54039751.

2D gel databases

DOSAC-COBS-2DPAGEP67936.
OGPiP07226.

Proteomic databases

MaxQBiP67936.
PaxDbiP67936.
PeptideAtlasiP67936.
PRIDEiP67936.

Protocols and materials databases

DNASUi7171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000300933; ENSP00000300933; ENSG00000167460. [P67936-1]
ENST00000344824; ENSP00000345230; ENSG00000167460. [P67936-2]
GeneIDi7171.
KEGGihsa:7171.
UCSCiuc002ndi.2. human. [P67936-2]
uc002ndj.2. human.

Organism-specific databases

CTDi7171.
GeneCardsiGC19P017852.
H-InvDBHIX0022609.
HGNCiHGNC:12013. TPM4.
HPAiCAB004685.
MIMi600317. gene.
neXtProtiNX_P67936.
Orphaneti178342. Inflammatory myofibroblastic tumor.
PharmGKBiPA36693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304012.
GeneTreeiENSGT00550000074494.
HOVERGENiHBG107404.
InParanoidiP67936.
KOiK10375.
OMAiLTICETE.
PhylomeDBiP67936.
TreeFamiTF351519.

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
REACT_20558. Smooth Muscle Contraction.

Miscellaneous databases

ChiTaRSiTPM4. human.
GeneWikiiTPM4.
GenomeRNAii7171.
NextBioi28104.
PROiP67936.
SOURCEiSearch...

Gene expression databases

BgeeiP67936.
CleanExiHS_TPM4.
ExpressionAtlasiP67936. baseline and differential.
GenevestigatoriP67936.

Family and domain databases

InterProiIPR000533. Tropomyosin.
[Graphical view]
PfamiPF00261. Tropomyosin. 1 hit.
[Graphical view]
PRINTSiPR00194. TROPOMYOSIN.
PROSITEiPS00326. TROPOMYOSIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a cDNA defining a gene family encoding TM30p1, a human fibroblast tropomyosin."
    McLeod A.R., Talbot K., Smillie L.B., Houlker C.
    J. Mol. Biol. 194:1-10(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Fibroblast.
  2. "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: Ovarian carcinoma and Tongue.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. 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: Eye, Placenta and Testis.
  6. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  7. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 45-54; 56-69; 77-89; 133-146 AND 216-223, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  8. "The calcium binding protein tropomyosin in human platelets and cardiac tissue: elevation in hypertensive cardiac hypertrophy."
    Crabos M., Yamakado T., Heizmann C.W., Cerletti N., Buehler F.R., Erne P.
    Eur. J. Clin. Invest. 21:472-478(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-31; 44-61; 89-95; 205-214 AND 231-243 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Platelet.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-27; 45-82; 132-142; 154-169 AND 216-228, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism."
    MacLeod A.R., Houlker C., Reinach F.C., Smillie L.B., Talbot K., Modi G., Walsh F.S.
    Proc. Natl. Acad. Sci. U.S.A. 82:7835-7839(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 118-248.
    Tissue: Fibroblast.
  11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 177-189 AND 228-247.
    Tissue: Keratinocyte.
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-177 AND LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-204.

Entry informationi

Entry nameiTPM4_HUMAN
AccessioniPrimary (citable) accession number: P67936
Secondary accession number(s): P07226
, Q15659, Q5U0D9, Q9BU85, Q9H8Q3, Q9UCS1, Q9UCS2, Q9UCS3, Q9UCS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 117 of the entry and version 3 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.