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P63267

- ACTH_HUMAN

UniProt

P63267 - ACTH_HUMAN

Protein

Actin, gamma-enteric smooth muscle

Gene

ACTG2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. muscle contraction Source: Reactome

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_20558. Smooth Muscle Contraction.
    SignaLinkiP63267.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, gamma-enteric smooth muscle
    Alternative name(s):
    Alpha-actin-3
    Gamma-2-actin
    Smooth muscle gamma-actin
    Gene namesi
    Name:ACTG2
    Synonyms:ACTA3, ACTL3, ACTSG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:145. ACTG2.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cell periphery Source: Ensembl
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. extracellular space Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2604. Familial visceral myopathy.
    PharmGKBiPA24469.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 22Removed in mature formBy similarityPRO_0000000748
    Chaini3 – 376374Actin, gamma-enteric smooth musclePRO_0000000749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451Methionine (R)-sulfoxideBy similarity
    Modified residuei48 – 481Methionine (R)-sulfoxideBy similarity

    Post-translational modificationi

    Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization By similarity.By similarity
    Monomethylation at Lys-85 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration By similarity.By similarity

    Keywords - PTMi

    Oxidation

    Proteomic databases

    MaxQBiP63267.
    PRIDEiP63267.

    2D gel databases

    OGPiP12718.

    PTM databases

    PhosphoSiteiP63267.

    Miscellaneous databases

    PMAP-CutDBP63267.

    Expressioni

    Gene expression databases

    ArrayExpressiP63267.
    BgeeiP63267.
    CleanExiHS_ACTG2.
    GenevestigatoriP63267.

    Organism-specific databases

    HPAiCAB003761.
    HPA041271.

    Interactioni

    Subunit structurei

    Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.

    Protein-protein interaction databases

    BioGridi106587. 12 interactions.
    IntActiP63267. 9 interactions.
    MINTiMINT-256943.
    STRINGi9606.ENSP00000295137.

    Structurei

    3D structure databases

    ProteinModelPortaliP63267.
    SMRiP63267. Positions 3-376.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    HOGENOMiHOG000233340.
    HOVERGENiHBG003771.
    InParanoidiP63267.
    KOiK12315.
    OMAiASMESAN.
    PhylomeDBiP63267.
    TreeFamiTF354237.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    PRINTSiPR00190. ACTIN.
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]
    PROSITEiPS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 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. Align

    Isoform 1 (identifier: P63267-1) [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

    MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ    50
    KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE 100
    EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT 150
    GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS 200
    FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT 250
    IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL 300
    SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL 350
    STFQQMWISK PEYDEAGPSI VHRKCF 376
    Length:376
    Mass (Da):41,877
    Last modified:October 11, 2004 - v1
    Checksum:i6EC08CD5EEAD445E
    GO
    Isoform 2 (identifier: P63267-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-85: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:333
    Mass (Da):37,083
    Checksum:i1D423B1372E4BFCD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301V → F in CAG38753. 1 PublicationCurated
    Sequence conflicti157 – 1571G → C in BAG65327. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei43 – 8543Missing in isoform 2. 1 PublicationVSP_045861Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16940 mRNA. Translation: CAA34814.1.
    D00654 Genomic DNA. Translation: BAA00546.1.
    AK304523 mRNA. Translation: BAG65327.1.
    AK312955 mRNA. Translation: BAG35794.1.
    CR536515 mRNA. Translation: CAG38753.1.
    CR541794 mRNA. Translation: CAG46593.1.
    AC073046 Genomic DNA. Translation: AAX88909.1.
    CH471053 Genomic DNA. Translation: EAW99713.1.
    BC012617 mRNA. Translation: AAH12617.1.
    BC094877 mRNA. Translation: AAH94877.1.
    CCDSiCCDS1930.1. [P63267-1]
    CCDS56124.1. [P63267-2]
    PIRiA40261.
    RefSeqiNP_001186822.1. NM_001199893.1. [P63267-2]
    NP_001606.1. NM_001615.3. [P63267-1]
    UniGeneiHs.516105.

    Genome annotation databases

    EnsembliENST00000345517; ENSP00000295137; ENSG00000163017. [P63267-1]
    ENST00000409624; ENSP00000386857; ENSG00000163017. [P63267-1]
    ENST00000409731; ENSP00000386929; ENSG00000163017. [P63267-2]
    GeneIDi72.
    KEGGihsa:72.
    UCSCiuc002sjw.3. human. [P63267-1]

    Polymorphism databases

    DMDMi54036679.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16940 mRNA. Translation: CAA34814.1 .
    D00654 Genomic DNA. Translation: BAA00546.1 .
    AK304523 mRNA. Translation: BAG65327.1 .
    AK312955 mRNA. Translation: BAG35794.1 .
    CR536515 mRNA. Translation: CAG38753.1 .
    CR541794 mRNA. Translation: CAG46593.1 .
    AC073046 Genomic DNA. Translation: AAX88909.1 .
    CH471053 Genomic DNA. Translation: EAW99713.1 .
    BC012617 mRNA. Translation: AAH12617.1 .
    BC094877 mRNA. Translation: AAH94877.1 .
    CCDSi CCDS1930.1. [P63267-1 ]
    CCDS56124.1. [P63267-2 ]
    PIRi A40261.
    RefSeqi NP_001186822.1. NM_001199893.1. [P63267-2 ]
    NP_001606.1. NM_001615.3. [P63267-1 ]
    UniGenei Hs.516105.

    3D structure databases

    ProteinModelPortali P63267.
    SMRi P63267. Positions 3-376.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106587. 12 interactions.
    IntActi P63267. 9 interactions.
    MINTi MINT-256943.
    STRINGi 9606.ENSP00000295137.

    PTM databases

    PhosphoSitei P63267.

    Polymorphism databases

    DMDMi 54036679.

    2D gel databases

    OGPi P12718.

    Proteomic databases

    MaxQBi P63267.
    PRIDEi P63267.

    Protocols and materials databases

    DNASUi 72.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345517 ; ENSP00000295137 ; ENSG00000163017 . [P63267-1 ]
    ENST00000409624 ; ENSP00000386857 ; ENSG00000163017 . [P63267-1 ]
    ENST00000409731 ; ENSP00000386929 ; ENSG00000163017 . [P63267-2 ]
    GeneIDi 72.
    KEGGi hsa:72.
    UCSCi uc002sjw.3. human. [P63267-1 ]

    Organism-specific databases

    CTDi 72.
    GeneCardsi GC02P074119.
    HGNCi HGNC:145. ACTG2.
    HPAi CAB003761.
    HPA041271.
    MIMi 102545. gene.
    neXtProti NX_P63267.
    Orphaneti 2604. Familial visceral myopathy.
    PharmGKBi PA24469.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000233340.
    HOVERGENi HBG003771.
    InParanoidi P63267.
    KOi K12315.
    OMAi ASMESAN.
    PhylomeDBi P63267.
    TreeFami TF354237.

    Enzyme and pathway databases

    Reactomei REACT_20558. Smooth Muscle Contraction.
    SignaLinki P63267.

    Miscellaneous databases

    ChiTaRSi ACTG2. human.
    GeneWikii ACTG2.
    GenomeRNAii 72.
    NextBioi 283.
    PMAP-CutDB P63267.
    PROi P63267.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63267.
    Bgeei P63267.
    CleanExi HS_ACTG2.
    Genevestigatori P63267.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    PRINTSi PR00190. ACTIN.
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of a human smooth muscle (enteric type) gamma-actin cDNA."
      Miwa T., Kamada S., Kakunaga T.
      Nucleic Acids Res. 18:4263-4263(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Stomach.
    2. "Structure, chromosome location, and expression of the human smooth muscle (enteric type) gamma-actin gene: evolution of six human actin genes."
      Miwa T., Manabe Y., Kurokawa K., Kamada S., Kanda N., Bruns G., Ueyama H., Kakunaga T.
      Mol. Cell. Biol. 11:3296-3306(1991) [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: Uterus.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Mammary gland and Prostate.

    Entry informationi

    Entry nameiACTH_HUMAN
    AccessioniPrimary (citable) accession number: P63267
    Secondary accession number(s): B2R7E7
    , B4E315, D6W5H8, E9PG30, P12718, Q504R1, Q6FI22
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 102 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

    Miscellaneous

    In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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