Reviewed, UniProtKB/Swiss-Prot O15143 (ARC1B_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton.
Sequence similarities	Belongs to the WD repeat ARPC1 family. Contains 6 WD repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Domain	Repeat WD repeat
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular component movement Ref.1 Traceable author statement. Source: ProtInc regulation of actin filament polymerization Inferred from electronic annotation. Source: InterPro
Cellular component	Arp2/3 protein complex Ref.1 Traceable author statement. Source: ProtInc cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of cytoskeleton Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACTR3B	Q9P1U1	1	EBI-1044647,EBI-1047175

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 372	371	Actin-related protein 2/3 complex subunit 1B		PRO_0000050855
Regions
	Repeat	6 – 45	40	WD 1
	Repeat	50 – 89	40	WD 2
	Repeat	94 – 135	42	WD 3
	Repeat	140 – 179	40	WD 4
	Repeat	242 – 280	39	WD 5
	Repeat	324 – 367	44	WD 6
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	44	1	N6-acetyllysine Ref.9
	Modified residue	82	1	N6-acetyllysine Ref.9
	Modified residue	310	1	Phosphoserine Ref.6
Natural variations
	Natural variant	37	1	K → N: dbSNP rs1045012.		VAR_014477

Sequences

	Sequence		Length	Mass (Da)
	O15143-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1939F5B63D40BD27	FASTA	372	40,950
	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

References

	« Hide 'large scale' referencesShow '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: 9230079] [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. , 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: 12853948] [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: 15489334] [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: 12665801] [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: 11741539] [Abstract] Cited for: RECONSTITUTION OF THE ARP2/3 COMPLEX.
[6]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, MASS SPECTROMETRY.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44 AND LYS-82, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00005160.
RefSeq	NP_005711.1.
UniGene	Hs.489284
3D structure databases
SMR	O15143. Positions 1-370, 2-371.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15143. 1 interaction.
STRING	O15143.
PTM databases
PhosphoSite	O15143.
Proteomic databases
PRIDE	O15143.
Genome annotation databases
Ensembl	ENST00000252725; ENSP00000252725; ENSG00000130429; Homo sapiens. [Genome view] ENST00000451682; ENSP00000389631; ENSG00000130429; Homo sapiens. [Genome view]
GeneID	10095.
KEGG	hsa:10095.
UCSC	uc003upz.1. human.
Organism-specific databases
CTD	10095.
GeneCards	GC07P098810. GC07P098811.
H-InvDB	HIX0006888.
HGNC	HGNC:704. ARPC1B.
HPA	HPA004832.
MIM	604223. gene.
PharmGKB	PA24998.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG716994.
HOVERGEN	O15143.
InParanoid	O15143.
Gene expression databases
ArrayExpress	O15143.
Bgee	O15143.
CleanEx	HS_ARPC1B.
Genevestigator	O15143.
Family and domain databases
InterPro	IPR017383. ARPC2/3_su1. IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR019782. WD40_repeat_2. IPR017986. WD40_repeat_dom. IPR019781. WD40_repeat_sg. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
Pfam	PF00400. WD40. 2 hits. [Graphical view]
PIRSF	PIRSF038093. ARP2/3_su1. 1 hit.
SMART	SM00320. WD40. 6 hits. [Graphical view]
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. 1 hit. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	38181.
SOURCE	Search...

Entry information

Entry name

ARC1B_HUMAN

Accession

Primary (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:	December 15, 2009
This is version 95 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.