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O15143

- ARC1B_HUMAN

UniProt

O15143 - ARC1B_HUMAN

Protein

Actin-related protein 2/3 complex subunit 1B

Gene

ARPC1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. structural constituent of cytoskeleton Source: ProtInc

    GO - Biological processi

    1. cellular component movement Source: ProtInc
    2. regulation of actin filament polymerization Source: InterPro

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    SignaLinkiO15143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-related protein 2/3 complex subunit 1B
    Alternative name(s):
    Arp2/3 complex 41 kDa subunit
    p41-ARC
    Gene namesi
    Name:ARPC1B
    Synonyms:ARC41
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:704. ARPC1B.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. Arp2/3 protein complex Source: ProtInc
    3. cytoplasm Source: UniProtKB-KW
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24998.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 372371Actin-related protein 2/3 complex subunit 1BPRO_0000050855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei82 – 821N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO15143.
    PaxDbiO15143.
    PRIDEiO15143.

    PTM databases

    PhosphoSiteiO15143.

    Expressioni

    Gene expression databases

    ArrayExpressiO15143.
    BgeeiO15143.
    CleanExiHS_ARPC1B.
    GenevestigatoriO15143.

    Organism-specific databases

    HPAiHPA004832.

    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

    BioGridi115402. 42 interactions.
    DIPiDIP-41254N.
    IntActiO15143. 5 interactions.
    MINTiMINT-5003785.
    STRINGi9606.ENSP00000252725.

    Structurei

    3D structure databases

    ProteinModelPortaliO15143.
    SMRiO15143. Positions 2-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati6 – 4540WD 1Add
    BLAST
    Repeati50 – 8940WD 2Add
    BLAST
    Repeati94 – 13542WD 3Add
    BLAST
    Repeati140 – 17940WD 4Add
    BLAST
    Repeati242 – 28039WD 5Add
    BLAST
    Repeati324 – 36744WD 6Add
    BLAST

    Sequence similaritiesi

    Belongs to the WD repeat ARPC1 family.Curated
    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000181752.
    HOVERGENiHBG050560.
    InParanoidiO15143.
    KOiK05757.
    OMAiKWVKVHE.
    PhylomeDBiO15143.
    TreeFamiTF315041.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR017383. ARPC2/3_su1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR10709. PTHR10709. 1 hit.
    PfamiPF00400. WD40. 3 hits.
    [Graphical view]
    PIRSFiPIRSF038093. ARP2/3_su1. 1 hit.
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O15143-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAYHSFLVEP ISCHAWNKDR TQIAICPNNH EVHIYEKSGA KWTKVHELKE    50
    HNGQVTGIDW APESNRIVTC GTDRNAYVWT LKGRTWKPTL VILRINRAAR 100
    CVRWAPNENK FAVGSGSRVI SICYFEQEND WWVCKHIKKP IRSTVLSLDW 150
    HPNNVLLAAG SCDFKCRIFS AYIKEVEERP APTPWGSKMP FGELMFESSS 200
    SCGWVHGVCF SASGSRVAWV SHDSTVCLAD ADKKMAVATL ASETLPLLAL 250
    TFITDNSLVA AGHDCFPVLF TYDAAAGMLS FGGRLDVPKQ SSQRGLTARE 300
    RFQNLDKKAS SEGGTAAGAG LDSLHKNSVS QISVLSGGKA KCSQFCTTGM 350
    DGGMSIWDVK SLESALKDLK IK 372
    Length:372
    Mass (Da):40,950
    Last modified:January 23, 2007 - v3
    Checksum:i1939F5B63D40BD27
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371K → N.
    Corresponds to variant rs1045012 [ dbSNP | Ensembl ].
    VAR_014477

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5661.1.
    RefSeqiNP_005711.1. NM_005720.3.
    XP_006715888.1. XM_006715825.1.
    XP_006715889.1. XM_006715826.1.
    UniGeneiHs.489284.

    Genome annotation databases

    EnsembliENST00000252725; ENSP00000252725; ENSG00000130429.
    ENST00000451682; ENSP00000389631; ENSG00000130429.
    GeneIDi10095.
    KEGGihsa:10095.
    UCSCiuc003upz.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS5661.1.
    RefSeqi NP_005711.1. NM_005720.3.
    XP_006715888.1. XM_006715825.1.
    XP_006715889.1. XM_006715826.1.
    UniGenei Hs.489284.

    3D structure databases

    ProteinModelPortali O15143.
    SMRi O15143. Positions 2-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115402. 42 interactions.
    DIPi DIP-41254N.
    IntActi O15143. 5 interactions.
    MINTi MINT-5003785.
    STRINGi 9606.ENSP00000252725.

    PTM databases

    PhosphoSitei O15143.

    Proteomic databases

    MaxQBi O15143.
    PaxDbi O15143.
    PRIDEi O15143.

    Protocols and materials databases

    DNASUi 10095.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252725 ; ENSP00000252725 ; ENSG00000130429 .
    ENST00000451682 ; ENSP00000389631 ; ENSG00000130429 .
    GeneIDi 10095.
    KEGGi hsa:10095.
    UCSCi uc003upz.3. human.

    Organism-specific databases

    CTDi 10095.
    GeneCardsi GC07P098971.
    HGNCi HGNC:704. ARPC1B.
    HPAi HPA004832.
    MIMi 604223. gene.
    neXtProti NX_O15143.
    PharmGKBi PA24998.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000181752.
    HOVERGENi HBG050560.
    InParanoidi O15143.
    KOi K05757.
    OMAi KWVKVHE.
    PhylomeDBi O15143.
    TreeFami TF315041.

    Enzyme and pathway databases

    SignaLinki O15143.

    Miscellaneous databases

    ChiTaRSi ARPC1B. human.
    GeneWikii ARPC1B.
    GenomeRNAii 10095.
    NextBioi 38181.
    PROi O15143.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15143.
    Bgeei O15143.
    CleanExi HS_ARPC1B.
    Genevestigatori O15143.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR017383. ARPC2/3_su1.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR10709. PTHR10709. 1 hit.
    Pfami PF00400. WD40. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF038093. ARP2/3_su1. 1 hit.
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS50082. WD_REPEATS_2. 1 hit.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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].

    Entry informationi

    Entry nameiARC1B_HUMAN
    AccessioniPrimary (citable) accession number: O15143
    Secondary accession number(s): Q9BU00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 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 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3