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O15143 (ARC1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 2/3 complex subunit 1B
Alternative name(s):
Arp2/3 complex 41 kDa subunit
p41-ARC
Gene names
Name:ARPC1B
Synonyms:ARC41
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as 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.

Subunit structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Sequence similarities

Belongs to the WD repeat ARPC1 family.

Contains 6 WD repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 372371Actin-related protein 2/3 complex subunit 1B
PRO_0000050855

Regions

Repeat6 – 4540WD 1
Repeat50 – 8940WD 2
Repeat94 – 13542WD 3
Repeat140 – 17940WD 4
Repeat242 – 28039WD 5
Repeat324 – 36744WD 6

Amino acid modifications

Modified residue821N6-acetyllysine Ref.8

Natural variations

Natural variant371K → N.
Corresponds to variant rs1045012 [ dbSNP | Ensembl ].
VAR_014477

Sequences

Sequence LengthMass (Da)Tools
O15143 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1939F5B63D40BD27

FASTA37240,950
        10         20         30         40         50         60 
MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWTKVHELKE HNGQVTGIDW 

        70         80         90        100        110        120 
APESNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR CVRWAPNENK FAVGSGSRVI 

       130        140        150        160        170        180 
SICYFEQEND WWVCKHIKKP IRSTVLSLDW HPNNVLLAAG SCDFKCRIFS AYIKEVEERP 

       190        200        210        220        230        240 
APTPWGSKMP FGELMFESSS SCGWVHGVCF SASGSRVAWV SHDSTVCLAD ADKKMAVATL 

       250        260        270        280        290        300 
ASETLPLLAL TFITDNSLVA AGHDCFPVLF TYDAAAGMLS FGGRLDVPKQ SSQRGLTARE 

       310        320        330        340        350        360 
RFQNLDKKAS SEGGTAAGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM DGGMSIWDVK 

       370 
SLESALKDLK IK 

« Hide

References

« Hide 'large scale' references
[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].
[2]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Lung, Placenta and Skin.
[4]"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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20.
Tissue: Platelet.
[5]"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.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF006084 mRNA. Translation: AAB64189.1.
AC004922 Genomic DNA. No translation available.
BC002562 mRNA. Translation: AAH02562.1.
BC002988 mRNA. Translation: AAH02988.2.
BC007555 mRNA. Translation: AAH07555.1.
RefSeqNP_005711.1. NM_005720.3.
UniGeneHs.489284.

3D structure databases

ProteinModelPortalO15143.
SMRO15143. Positions 2-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115402. 41 interactions.
DIPDIP-41254N.
IntActO15143. 5 interactions.
MINTMINT-5003785.
STRING9606.ENSP00000252725.

PTM databases

PhosphoSiteO15143.

Proteomic databases

PaxDbO15143.
PRIDEO15143.

Protocols and materials databases

DNASU10095.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252725; ENSP00000252725; ENSG00000130429.
ENST00000451682; ENSP00000389631; ENSG00000130429.
GeneID10095.
KEGGhsa:10095.
UCSCuc003upz.3. human.

Organism-specific databases

CTD10095.
GeneCardsGC07P098971.
HGNCHGNC:704. ARPC1B.
HPAHPA004832.
MIM604223. gene.
neXtProtNX_O15143.
PharmGKBPA24998.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000181752.
HOVERGENHBG050560.
InParanoidO15143.
KOK05757.
OMAVLFTYDS.
PhylomeDBO15143.
TreeFamTF315041.

Enzyme and pathway databases

SignaLinkO15143.

Gene expression databases

ArrayExpressO15143.
BgeeO15143.
CleanExHS_ARPC1B.
GenevestigatorO15143.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR017383. ARPC2/3_su1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR10709. PTHR10709. 1 hit.
PfamPF00400. WD40. 3 hits.
[Graphical view]
PIRSFPIRSF038093. ARP2/3_su1. 1 hit.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARPC1B. human.
GeneWikiARPC1B.
GenomeRNAi10095.
NextBio38181.
PROO15143.
SOURCESearch...

Entry information

Entry nameARC1B_HUMAN
AccessionPrimary (citable) accession number: O15143
Secondary accession number(s): Q9BU00
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM