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Protein

Actin, gamma-enteric smooth muscle

Gene

ACTG2

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

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:145. ACTG2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cell body Source: AgBase
  • cell periphery Source: Ensembl
  • cytoplasm Source: AgBase
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • filopodium Source: AgBase
  • lamellipodium Source: AgBase
  • myosin filament Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Visceral myopathy (VSCM)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare inherited form of myopathic pseudo-obstruction characterized by impaired function of enteric smooth muscle cells, resulting in abnormal intestinal motility, severe abdominal pain, malnutrition, and even death. The disease shows inter- and intrafamilial variability. Most severely affected patients exhibit prenatal bladder enlargement, intestinal malrotation, neonatal functional gastrointestinal obstruction, and dependence on total parenteral nutrition and urinary catheterization.

See also OMIM:155310
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401R → C in VSCM. 1 Publication
VAR_071279
Natural varianti40 – 401R → H in VSCM. 1 Publication
VAR_071280
Natural varianti45 – 451M → T in VSCM. 1 Publication
VAR_071281
Natural varianti63 – 631R → G in VSCM. 1 Publication
VAR_071282
Natural varianti110 – 1101P → L in VSCM. 1 Publication
VAR_071283
Natural varianti134 – 1341Y → N in VSCM. 1 Publication
VAR_071284
Natural varianti148 – 1481R → S in VSCM. 2 Publications
VAR_071285
Natural varianti178 – 1781R → C in VSCM; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle. 2 Publications
VAR_071286
Natural varianti178 – 1781R → H in VSCM. 1 Publication
VAR_071287
Natural varianti178 – 1781R → L in VSCM; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle. 1 Publication
VAR_071288
Natural varianti198 – 1981G → D in VSCM. 1 Publication
VAR_071289
Natural varianti257 – 2571R → C in VSCM. 1 Publication
VAR_071290

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi155310. phenotype.
Orphaneti2604. Familial visceral myopathy.
2241. Megacystis-microcolon-intestinal hypoperistalsis syndrome.
104077. Myopathic intestinal pseudoobstruction.
PharmGKBiPA24469.

Polymorphism and mutation databases

BioMutaiACTG2.
DMDMi54036679.

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

BgeeiP63267.
CleanExiHS_ACTG2.
ExpressionAtlasiP63267. baseline and differential.
GenevisibleiP63267. HS.

Organism-specific databases

HPAiHPA041264.
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. 13 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

GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63267.
KOiK12315.
OMAiATLAMCE.
PhylomeDBiP63267.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin.
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. AlignAdd to basket

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

        10         20         30         40         50
MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ
60 70 80 90 100
KDSYVGDEAQ SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE
110 120 130 140 150
EHPTLLTEAP LNPKANREKM TQIMFETFNV PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVLDSGDGV THNVPIYEGY ALPHAIMRLD LAGRDLTDYL MKILTERGYS
210 220 230 240 250
FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
310 320 330 340 350
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK PEYDEAGPSI VHRKCF
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 (Ref. 4) Curated
Sequence conflicti157 – 1571G → C in BAG65327 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401R → C in VSCM. 1 Publication
VAR_071279
Natural varianti40 – 401R → H in VSCM. 1 Publication
VAR_071280
Natural varianti45 – 451M → T in VSCM. 1 Publication
VAR_071281
Natural varianti63 – 631R → G in VSCM. 1 Publication
VAR_071282
Natural varianti110 – 1101P → L in VSCM. 1 Publication
VAR_071283
Natural varianti134 – 1341Y → N in VSCM. 1 Publication
VAR_071284
Natural varianti148 – 1481R → S in VSCM. 2 Publications
VAR_071285
Natural varianti178 – 1781R → C in VSCM; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle. 2 Publications
VAR_071286
Natural varianti178 – 1781R → H in VSCM. 1 Publication
VAR_071287
Natural varianti178 – 1781R → L in VSCM; interferes with proper polymerization into thin filaments leading to impaired contractility of the smooth muscle. 1 Publication
VAR_071288
Natural varianti198 – 1981G → D in VSCM. 1 Publication
VAR_071289
Natural varianti257 – 2571R → C in VSCM. 1 Publication
VAR_071290

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
ENST00000409624; ENSP00000386857; ENSG00000163017.
ENST00000409731; ENSP00000386929; ENSG00000163017. [P63267-2]
GeneIDi72.
KEGGihsa:72.
UCSCiuc002sjw.3. human. [P63267-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi106587. 13 interactions.
IntActiP63267. 9 interactions.
MINTiMINT-256943.
STRINGi9606.ENSP00000295137.

PTM databases

PhosphoSiteiP63267.

Polymorphism and mutation databases

BioMutaiACTG2.
DMDMi54036679.

2D gel databases

OGPiP12718.

Proteomic databases

MaxQBiP63267.
PRIDEiP63267.

Protocols and materials databases

DNASUi72.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi72.
GeneCardsiGC02P074119.
HGNCiHGNC:145. ACTG2.
HPAiHPA041264.
HPA041271.
MIMi102545. gene.
155310. phenotype.
neXtProtiNX_P63267.
Orphaneti2604. Familial visceral myopathy.
2241. Megacystis-microcolon-intestinal hypoperistalsis syndrome.
104077. Myopathic intestinal pseudoobstruction.
PharmGKBiPA24469.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63267.
KOiK12315.
OMAiATLAMCE.
PhylomeDBiP63267.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiREACT_20558. Smooth Muscle Contraction.
SignaLinkiP63267.

Miscellaneous databases

ChiTaRSiACTG2. human.
GeneWikiiACTG2.
GenomeRNAii72.
NextBioi20816142.
PMAP-CutDBP63267.
PROiP63267.
SOURCEiSearch...

Gene expression databases

BgeeiP63267.
CleanExiHS_ACTG2.
ExpressionAtlasiP63267. baseline and differential.
GenevisibleiP63267. HS.

Family and domain databases

InterProiIPR004000. Actin.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  8. "Segregation of a missense variant in enteric smooth muscle actin gamma-2 with autosomal dominant familial visceral myopathy."
    Lehtonen H.J., Sipponen T., Tojkander S., Karikoski R., Jarvinen H., Laing N.G., Lappalainen P., Aaltonen L.A., Tuupanen S.
    Gastroenterology 143:1482-1491(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VSCM SER-148.
  9. "Familial visceral myopathy diagnosed by exome sequencing of a patient with chronic intestinal pseudo-obstruction."
    Holla O.L., Bock G., Busk O.L., Isfoss B.L.
    Endoscopy 46:533-537(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT VSCM SER-148.
  10. "De novo ACTG2 mutations cause congenital distended bladder, microcolon, and intestinal hypoperistalsis."
    Thorson W., Diaz-Horta O., Foster J. II, Spiliopoulos M., Quintero R., Farooq A., Blanton S., Tekin M.
    Hum. Genet. 133:737-742(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VSCM CYS-178 AND LEU-178, CHARACTERIZATION OF VARIANTS VSCM CYS-178 AND LEU-178.
  11. Cited for: VARIANTS VSCM CYS-40; HIS-40; THR-45; GLY-63; LEU-110; ASN-134; CYS-178; HIS-178; ASP-198 AND CYS-257.

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: July 22, 2015
This is version 110 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. 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.