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Protein

Beta-actin-like protein 2

Gene

Actbl2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-actin-like protein 2
Alternative name(s):
Kappa-actin
Gene namesi
Name:Actbl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2444552. Actbl2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Beta-actin-like protein 2PRO_0000318850Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei45 – 451Methionine (R)-sulfoxide1 Publication
Modified residuei48 – 481Methionine (R)-sulfoxide1 Publication

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.1 Publication
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

EPDiQ8BFZ3.
MaxQBiQ8BFZ3.
PaxDbiQ8BFZ3.
PeptideAtlasiQ8BFZ3.
PRIDEiQ8BFZ3.

2D gel databases

UCD-2DPAGEQ8BFZ3.

PTM databases

iPTMnetiQ8BFZ3.
PhosphoSiteiQ8BFZ3.
SwissPalmiQ8BFZ3.

Expressioni

Gene expression databases

BgeeiQ8BFZ3.
CleanExiMM_ACTBL2.

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 (By similarity). Interacts with PFN1 and PFDN1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi232025. 4 interactions.
IntActiQ8BFZ3. 6 interactions.
MINTiMINT-4110149.
STRINGi10090.ENSMUSP00000052086.

Structurei

3D structure databases

ProteinModelPortaliQ8BFZ3.
SMRiQ8BFZ3. Positions 8-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ8BFZ3.
OMAiMIGRPRH.
OrthoDBiEOG72RMZ1.
PhylomeDBiQ8BFZ3.
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]

Sequencei

Sequence statusi: Complete.

Q8BFZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDDELTALV VDNGSGMCKA GFGGDDAPRA VFPSMVGRPR HQGVMVGMGQ
60 70 80 90 100
KDCYVGDEAQ SKRGILTLKY PIEHGVVTNW DDMEKIWYHT FYNELRVAPD
110 120 130 140 150
EHPILLTEAP LNPKINREKM TQIMFEAFNT PAMYVAIQAV LSLYASGRTT
160 170 180 190 200
GIVMDSGDGV THTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYN
210 220 230 240 250
FTTTAEREIV RDVKEKLCYV ALDFEQEMVT AAASSSLERS YELPDGQVIT
260 270 280 290 300
IGNERFRCPE AIFQPSFLGI ESRGIHETTF NSIMKCDVDI RKDLFANTVL
310 320 330 340 350
SGGSTMYPGI ADRMQKEIVT LAPSTMKIKI IAPPERKYSV WIGGSILASL
360 370
STFQQMWISK QEYDEAGPPI VHRKCF
Length:376
Mass (Da):42,004
Last modified:March 1, 2003 - v1
Checksum:iDB6C8377BAE3A8BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029110 mRNA. Translation: BAC26303.1.
AK029130 mRNA. Translation: BAC26313.1.
BC111904 mRNA. Translation: AAI11905.1.
BC112429 mRNA. Translation: AAI12430.1.
CCDSiCCDS26768.1.
RefSeqiNP_780706.1. NM_175497.3.
UniGeneiMm.107293.

Genome annotation databases

EnsembliENSMUST00000054716; ENSMUSP00000052086; ENSMUSG00000055194.
GeneIDi238880.
KEGGimmu:238880.
UCSCiuc007rvu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029110 mRNA. Translation: BAC26303.1.
AK029130 mRNA. Translation: BAC26313.1.
BC111904 mRNA. Translation: AAI11905.1.
BC112429 mRNA. Translation: AAI12430.1.
CCDSiCCDS26768.1.
RefSeqiNP_780706.1. NM_175497.3.
UniGeneiMm.107293.

3D structure databases

ProteinModelPortaliQ8BFZ3.
SMRiQ8BFZ3. Positions 8-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232025. 4 interactions.
IntActiQ8BFZ3. 6 interactions.
MINTiMINT-4110149.
STRINGi10090.ENSMUSP00000052086.

PTM databases

iPTMnetiQ8BFZ3.
PhosphoSiteiQ8BFZ3.
SwissPalmiQ8BFZ3.

2D gel databases

UCD-2DPAGEQ8BFZ3.

Proteomic databases

EPDiQ8BFZ3.
MaxQBiQ8BFZ3.
PaxDbiQ8BFZ3.
PeptideAtlasiQ8BFZ3.
PRIDEiQ8BFZ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054716; ENSMUSP00000052086; ENSMUSG00000055194.
GeneIDi238880.
KEGGimmu:238880.
UCSCiuc007rvu.1. mouse.

Organism-specific databases

CTDi345651.
MGIiMGI:2444552. Actbl2.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ8BFZ3.
OMAiMIGRPRH.
OrthoDBiEOG72RMZ1.
PhylomeDBiQ8BFZ3.
TreeFamiTF354237.

Miscellaneous databases

PROiQ8BFZ3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BFZ3.
CleanExiMM_ACTBL2.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  2. "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].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  4. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
    Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
    Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION AT MET-45 AND MET-48, DEOXIDATION AT MET-45 AND MET-48.

Entry informationi

Entry nameiACTBL_MOUSE
AccessioniPrimary (citable) accession number: Q8BFZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.