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Protein

Actin-related protein 2/3 complex subunit 4

Gene

ARPC4

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

Functioni

Functions as actin-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 mother actin filament.

GO - Molecular functioni

  1. enzyme binding Source: BHF-UCL
  2. structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

  1. actin filament polymerization Source: InterPro
  2. actin nucleation Source: UniProtKB
  3. Arp2/3 complex-mediated actin nucleation Source: FlyBase
  4. axon guidance Source: Reactome
  5. ephrin receptor signaling pathway Source: Reactome
  6. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  7. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 4
Alternative name(s):
Arp2/3 complex 20 kDa subunit
Short name:
p20-ARC
Gene namesi
Name:ARPC4
Synonyms:ARC20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:707. ARPC4.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. Cell projection 1 Publication

GO - Cellular componenti

  1. Arp2/3 protein complex Source: UniProtKB
  2. cell projection Source: UniProtKB-SubCell
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25002.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 168167Actin-related protein 2/3 complex subunit 4PRO_0000124049Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP59998.
PaxDbiP59998.
PRIDEiP59998.

PTM databases

PhosphoSiteiP59998.

Expressioni

Gene expression databases

BgeeiP59998.
CleanExiHS_ARPC4.
ExpressionAtlasiP59998. baseline and differential.
GenevestigatoriP59998.

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.

Protein-protein interaction databases

BioGridi115400. 46 interactions.
DIPiDIP-33188N.
IntActiP59998. 9 interactions.
MINTiMINT-5000208.
STRINGi9606.ENSP00000380431.

Structurei

3D structure databases

ProteinModelPortaliP59998.
SMRiP59998. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC4 family.Curated

Phylogenomic databases

eggNOGiNOG261545.
GeneTreeiENSGT00390000016233.
ENSGT00760000118951.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiP59998.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
PhylomeDBiP59998.
TreeFamiTF105621.
TF313087.

Family and domain databases

InterProiIPR008384. ARPC4.
[Graphical view]
PANTHERiPTHR22629. PTHR22629. 1 hit.
PfamiPF05856. ARPC4. 1 hit.
[Graphical view]
PIRSFiPIRSF039100. ARPC4. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P59998-1) [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
MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP
60 70 80 90 100
VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN
110 120 130 140 150
FFILRRKPVE GYDISFLITN FHTEQMYKHK LVDFVIHFME EIDKEISEMK
160
LSVNARARIV AEEFLKNF
Length:168
Mass (Da):19,667
Last modified:January 22, 2007 - v3
Checksum:i273CCB230AC703DF
GO
Isoform 2 (identifier: P59998-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-168: EGYDISFLIT...IVAEEFLKNF → EQKKIFTIQG...LRPCRPQARP

Note: No experimental confirmation available.

Show »
Length:625
Mass (Da):71,719
Checksum:iE05F7DC236DF9674
GO
Isoform 3 (identifier: P59998-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVREPGPRPGTPGCSASGQW

Note: No experimental confirmation available.

Show »
Length:187
Mass (Da):21,588
Checksum:iF61DD748D01B8880
GO
Isoform 4 (identifier: P59998-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-90: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:78
Mass (Da):9,552
Checksum:i32DD605A770B6706
GO

Sequence cautioni

The sequence AAH12596.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941M → T in AAH12596 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9090Missing in isoform 4. CuratedVSP_046753Add
BLAST
Alternative sequencei1 – 11M → MVREPGPRPGTPGCSASGQW in isoform 3. 1 PublicationVSP_046150
Alternative sequencei110 – 16859EGYDI…FLKNF → EQKKIFTIQGCYPVIRCLLR RRGWVEKKMVHRSGPTLLPP QKDLDSSAMGDSDTTEDEDE DEDEEFQPSQLFDFDDLLKF DDLDGTHALMVGLCLNLRNL PWFDEVDANSFFPRCYCLGA EDDKKAFIGDKQPKKQEKNP VLVSPEFVDEALCACEEYLS NLAHMDIDKDLEAPLYLTPE GWSLFLQRYYQVVHEGAELR HLDTQVQRCEDILQQLQAVV PQIDMEGDRNIWIVKPGAKS RGRGIMCMDHLEEMLKLVNG NPVVMKDGKWVVQKYIERPL LIFGTKFDLRQWFLVTDWNP LTVWFYRDSYIRFSTQPFSL KNLDNSVHLCNNSIQKHLEN SCHRHPLLPPDNMWSSQRFQ AHLQEMGAPNAWSTIIVPGM KDAVIHALQTSQDTVQCRKA SFELYGADFVFGEDFQPWLI EINASPTMAPSTAVTARLCA GVQADTLRVVIDRMLDRNCD TGAFELIYKQPVTTSPASTP RPSCLLPMYSDTRARSSDDS TASWWALRPCRPQARP in isoform 2. 1 PublicationVSP_046151Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019888 mRNA. Translation: AAB71548.1.
AF006087 mRNA. Translation: AAB64192.1.
BX419672 mRNA. No translation available.
AC022382 Genomic DNA. No translation available.
BC012596 mRNA. Translation: AAH12596.3. Different initiation.
BC025289 mRNA. No translation available.
CCDSiCCDS43047.1. [P59998-1]
CCDS46743.1. [P59998-4]
CCDS56238.1. [P59998-3]
RefSeqiNP_001020130.1. NM_001024959.2. [P59998-4]
NP_001020131.1. NM_001024960.2. [P59998-4]
NP_001185709.1. NM_001198780.1. [P59998-3]
NP_005709.1. NM_005718.4. [P59998-1]
UniGeneiHs.323342.

Genome annotation databases

EnsembliENST00000397261; ENSP00000380431; ENSG00000241553. [P59998-1]
ENST00000433034; ENSP00000388169; ENSG00000241553. [P59998-3]
ENST00000498623; ENSP00000432235; ENSG00000241553. [P59998-4]
GeneIDi10093.
KEGGihsa:100526693.
hsa:10093.
UCSCiuc003bsz.2. human. [P59998-1]
uc003bta.2. human.
uc003btd.4. human.

Polymorphism databases

DMDMi38372625.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF019888 mRNA. Translation: AAB71548.1.
AF006087 mRNA. Translation: AAB64192.1.
BX419672 mRNA. No translation available.
AC022382 Genomic DNA. No translation available.
BC012596 mRNA. Translation: AAH12596.3. Different initiation.
BC025289 mRNA. No translation available.
CCDSiCCDS43047.1. [P59998-1]
CCDS46743.1. [P59998-4]
CCDS56238.1. [P59998-3]
RefSeqiNP_001020130.1. NM_001024959.2. [P59998-4]
NP_001020131.1. NM_001024960.2. [P59998-4]
NP_001185709.1. NM_001198780.1. [P59998-3]
NP_005709.1. NM_005718.4. [P59998-1]
UniGeneiHs.323342.

3D structure databases

ProteinModelPortaliP59998.
SMRiP59998. Positions 2-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115400. 46 interactions.
DIPiDIP-33188N.
IntActiP59998. 9 interactions.
MINTiMINT-5000208.
STRINGi9606.ENSP00000380431.

PTM databases

PhosphoSiteiP59998.

Polymorphism databases

DMDMi38372625.

Proteomic databases

MaxQBiP59998.
PaxDbiP59998.
PRIDEiP59998.

Protocols and materials databases

DNASUi10093.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000397261; ENSP00000380431; ENSG00000241553. [P59998-1]
ENST00000433034; ENSP00000388169; ENSG00000241553. [P59998-3]
ENST00000498623; ENSP00000432235; ENSG00000241553. [P59998-4]
GeneIDi10093.
KEGGihsa:100526693.
hsa:10093.
UCSCiuc003bsz.2. human. [P59998-1]
uc003bta.2. human.
uc003btd.4. human.

Organism-specific databases

CTDi100526693.
10093.
GeneCardsiGC03P009834.
HGNCiHGNC:707. ARPC4.
MIMi604226. gene.
neXtProtiNX_P59998.
PharmGKBiPA25002.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG261545.
GeneTreeiENSGT00390000016233.
ENSGT00760000118951.
HOGENOMiHOG000202303.
HOVERGENiHBG050582.
InParanoidiP59998.
KOiK05755.
OMAiMLKHKIV.
OrthoDBiEOG7VTDPM.
PhylomeDBiP59998.
TreeFamiTF105621.
TF313087.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.

Miscellaneous databases

ChiTaRSiARPC4. human.
GeneWikiiARPC4.
NextBioi34054911.
PROiP59998.
SOURCEiSearch...

Gene expression databases

BgeeiP59998.
CleanExiHS_ARPC4.
ExpressionAtlasiP59998. baseline and differential.
GenevestigatoriP59998.

Family and domain databases

InterProiIPR008384. ARPC4.
[Graphical view]
PANTHERiPTHR22629. PTHR22629. 1 hit.
PfamiPF05856. ARPC4. 1 hit.
[Graphical view]
PIRSFiPIRSF039100. ARPC4. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins."
    Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A., Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.
    Biochem. J. 328:105-112(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
  2. "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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Fetal brain.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2005) [PubMed] [Europe PMC] [Abstract]
    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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-168 (ISOFORM 1).
    Tissue: Choriocarcinoma and Prostate.
  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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT THR-2.
    Tissue: Platelet.
  7. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIN-BINDING, RECONSTITUTION OF THE ARP2/3 COMPLEX.

Entry informationi

Entry nameiARPC4_HUMAN
AccessioniPrimary (citable) accession number: P59998
Secondary accession number(s): C9JWM7
, E7ETI0, F6TTL5, O15509, Q6P0W5, Q96QJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2003
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 115 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 3
    Human chromosome 3: 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

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.