SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P61160

- ARP2_HUMAN

UniProt

P61160 - ARP2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Actin-related protein 2
Gene
ACTR2, ARP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 1623ATP By similarity
Nucleotide bindingi214 – 2185ATP By similarity
Nucleotide bindingi305 – 3106ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. actin cytoskeleton organization Source: Ensembl
  3. asymmetric cell division Source: Ensembl
  4. cellular component movement Source: UniProtKB
  5. cytoplasmic transport Source: Ensembl
  6. establishment or maintenance of cell polarity Source: Ensembl
  7. innate immune response Source: Reactome
  8. meiotic cytokinesis Source: Ensembl
  9. spindle localization Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-binding, ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinkiP61160.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2
Alternative name(s):
Actin-like protein 2
Gene namesi
Name:ACTR2
Synonyms:ARP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:169. ACTR2.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projection 1 Publication

GO - Cellular componenti

  1. Arp2/3 protein complex Source: UniProtKB
  2. actin cap Source: Ensembl
  3. actin cytoskeleton Source: UniProtKB
  4. cell projection Source: UniProtKB-SubCell
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24488.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Actin-related protein 2
PRO_0000089067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei299 – 2991N6-acetyllysine1 Publication
Modified residuei322 – 3221N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP61160.
PaxDbiP61160.
PRIDEiP61160.

2D gel databases

SWISS-2DPAGEP61160.

PTM databases

PhosphoSiteiP61160.

Expressioni

Gene expression databases

ArrayExpressiP61160.
BgeeiP61160.
CleanExiHS_ACTR2.
GenevestigatoriP61160.

Organism-specific databases

HPAiCAB005083.
HPA015050.

Interactioni

Subunit structurei

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC.1 Publication

Protein-protein interaction databases

BioGridi115404. 66 interactions.
DIPiDIP-33165N.
IntActiP61160. 8 interactions.
MINTiMINT-5000145.
STRINGi9606.ENSP00000367220.

Structurei

3D structure databases

ProteinModelPortaliP61160.
SMRiP61160. Positions 4-388.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family. ARP2 subfamily.

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
KOiK17260.
OMAiDYTFNEK.
OrthoDBiEOG78D7K6.
PhylomeDBiP61160.
TreeFamiTF300467.

Family and domain databases

InterProiIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P61160-1) [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

MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI    50
EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI 100
DTRNCKILLT EPPMNPTKNR EKIVEVMFET YQFSGVYVAI QAVLTLYAQG 150
LLTGVVVDSG DGVTHICPVY EGFSLPHLTR RLDIAGRDIT RYLIKLLLLR 200
GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL VESYTLPDGR 250
IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH 300
IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR 350
KHMVFLGGAV LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR 394
Length:394
Mass (Da):44,761
Last modified:May 10, 2004 - v1
Checksum:i1BFA6B442ED1A797
GO
Isoform 2 (identifier: P61160-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: K → KNNKKM

Note: No experimental confirmation available.

Show »
Length:399
Mass (Da):45,377
Checksum:iCF06512483DAD60A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei53 – 531K → KNNKKM in isoform 2.
VSP_046178

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671M → T in AAH14546. 1 Publication
Sequence conflicti172 – 1721G → S in AAH14546. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006082 mRNA. Translation: AAB64187.1.
AK315205 mRNA. Translation: BAG37642.1.
BX649080 mRNA. No translation available.
AC007318 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99908.1.
CH471053 Genomic DNA. Translation: EAW99910.1.
CH471053 Genomic DNA. Translation: EAW99912.1.
CH471053 Genomic DNA. Translation: EAW99913.1.
BC014546 mRNA. Translation: AAH14546.1.
CCDSiCCDS1881.1. [P61160-1]
CCDS46307.1. [P61160-2]
RefSeqiNP_001005386.1. NM_001005386.2. [P61160-2]
NP_005713.1. NM_005722.3. [P61160-1]
UniGeneiHs.643727.
Hs.744913.

Genome annotation databases

EnsembliENST00000260641; ENSP00000260641; ENSG00000138071. [P61160-1]
ENST00000377982; ENSP00000367220; ENSG00000138071. [P61160-2]
GeneIDi10097.
KEGGihsa:10097.
UCSCiuc002sdq.3. human. [P61160-1]

Polymorphism databases

DMDMi47117648.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006082 mRNA. Translation: AAB64187.1 .
AK315205 mRNA. Translation: BAG37642.1 .
BX649080 mRNA. No translation available.
AC007318 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAW99908.1 .
CH471053 Genomic DNA. Translation: EAW99910.1 .
CH471053 Genomic DNA. Translation: EAW99912.1 .
CH471053 Genomic DNA. Translation: EAW99913.1 .
BC014546 mRNA. Translation: AAH14546.1 .
CCDSi CCDS1881.1. [P61160-1 ]
CCDS46307.1. [P61160-2 ]
RefSeqi NP_001005386.1. NM_001005386.2. [P61160-2 ]
NP_005713.1. NM_005722.3. [P61160-1 ]
UniGenei Hs.643727.
Hs.744913.

3D structure databases

ProteinModelPortali P61160.
SMRi P61160. Positions 4-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115404. 66 interactions.
DIPi DIP-33165N.
IntActi P61160. 8 interactions.
MINTi MINT-5000145.
STRINGi 9606.ENSP00000367220.

Chemistry

ChEMBLi CHEMBL6090.

PTM databases

PhosphoSitei P61160.

Polymorphism databases

DMDMi 47117648.

2D gel databases

SWISS-2DPAGE P61160.

Proteomic databases

MaxQBi P61160.
PaxDbi P61160.
PRIDEi P61160.

Protocols and materials databases

DNASUi 10097.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000260641 ; ENSP00000260641 ; ENSG00000138071 . [P61160-1 ]
ENST00000377982 ; ENSP00000367220 ; ENSG00000138071 . [P61160-2 ]
GeneIDi 10097.
KEGGi hsa:10097.
UCSCi uc002sdq.3. human. [P61160-1 ]

Organism-specific databases

CTDi 10097.
GeneCardsi GC02P065454.
HGNCi HGNC:169. ACTR2.
HPAi CAB005083.
HPA015050.
MIMi 604221. gene.
neXtProti NX_P61160.
PharmGKBi PA24488.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5277.
HOGENOMi HOG000233340.
HOVERGENi HBG003771.
KOi K17260.
OMAi DYTFNEK.
OrthoDBi EOG78D7K6.
PhylomeDBi P61160.
TreeFami TF300467.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
SignaLinki P61160.

Miscellaneous databases

ChiTaRSi ACTR2. human.
GeneWikii ACTR2.
GenomeRNAii 10097.
NextBioi 38189.
PROi P61160.
SOURCEi Search...

Gene expression databases

ArrayExpressi P61160.
Bgeei P61160.
CleanExi HS_ACTR2.
Genevestigatori P61160.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_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 PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly."
    Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.
    J. Cell Biol. 138:375-384(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Liver.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Skeletal muscle.
  7. "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes."
    Welch M.D., Iwamatsu A., Mitchison T.J.
    Nature 385:265-269(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
  8. "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity."
    Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.
    Mol. Cell 8:1041-1052(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
  9. "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-299 AND LYS-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARP2_HUMAN
AccessioniPrimary (citable) accession number: P61160
Secondary accession number(s): B2RCP5
, D6W5F4, E9PF41, O15142, Q96C82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: September 3, 2014
This is version 107 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

Similar proteinsi