ARP6_HUMAN
ID ARP6_HUMAN Reviewed; 396 AA.
AC Q9GZN1; B3KW37; B4DLG9; Q53GH2; Q9BY39; Q9H8H6;
DT 27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Actin-related protein 6;
DE Short=hArp6;
DE AltName: Full=hARPX;
GN Name=ACTR6; ORFNames=CDA12;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11368909; DOI=10.1016/s0378-1119(01)00420-6;
RA Kato M., Sasaki M., Mizuno S., Harata M.;
RT "Novel actin-related proteins in vertebrates: similarities of structure and
RT expression pattern to Arp6 localized on Drosophila heterochromatin.";
RL Gene 268:133-140(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CBX1; CBX3 AND CBX5.
RX PubMed=16487625; DOI=10.1016/j.ejcb.2005.12.006;
RA Ohfuchi E., Kato M., Sasaki M., Sugimoto K., Oma Y., Harata M.;
RT "Vertebrate Arp6, a novel nuclear actin-related protein, interacts with
RT heterochromatin protein 1.";
RL Eur. J. Cell Biol. 85:411-421(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26164235; DOI=10.1016/j.bbrc.2015.07.005;
RA Kitamura H., Matsumori H., Kalendova A., Hozak P., Goldberg I.G., Nakao M.,
RA Saitoh N., Harata M.;
RT "The actin family protein ARP6 contributes to the structure and the
RT function of the nucleolus.";
RL Biochem. Biophys. Res. Commun. 464:554-560(2015).
CC -!- FUNCTION: Required for formation and/or maintenance of the proper
CC nucleolar structure and function (PubMed:26164235). Plays a dual role
CC in the regulation of ribosomal DNA (rDNA) transcription (By
CC similarity). In the presence of high glucose, it maintains active rDNA
CC transcription through H2A.Z deposition and under glucose starvation, is
CC required for the repression of rDNA transcription, and this function
CC may be independent of H2A.Z (By similarity).
CC {ECO:0000250|UniProtKB:Q9DEE9, ECO:0000269|PubMed:26164235}.
CC -!- SUBUNIT: Interacts with CBX1, CBX3 and CBX5.
CC {ECO:0000269|PubMed:16487625}.
CC -!- INTERACTION:
CC Q9GZN1; P0C0S5: H2AZ1; NbExp=3; IntAct=EBI-769329, EBI-1199859;
CC Q9GZN1; O43257: ZNHIT1; NbExp=5; IntAct=EBI-769329, EBI-347522;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P45890}. Nucleus {ECO:0000269|PubMed:16487625}.
CC Nucleus, nucleolus {ECO:0000269|PubMed:26164235}. Note=Colocalizes with
CC HP1 family proteins at pericentric heterochromatin.
CC {ECO:0000269|PubMed:16487625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9GZN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9GZN1-2; Sequence=VSP_054637, VSP_054638;
CC -!- SIMILARITY: Belongs to the actin family. ARP6 subfamily. {ECO:0000305}.
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DR EMBL; AB038229; BAB20762.1; -; mRNA.
DR EMBL; AF212251; AAK14934.1; -; mRNA.
DR EMBL; AK023495; BAB14588.1; -; mRNA.
DR EMBL; AK023684; BAB14640.1; -; mRNA.
DR EMBL; AK124075; BAG53999.1; -; mRNA.
DR EMBL; AK296991; BAG59531.1; -; mRNA.
DR EMBL; AK222959; BAD96679.1; -; mRNA.
DR EMBL; CH471054; EAW97623.1; -; Genomic_DNA.
DR EMBL; BC015107; AAH15107.1; -; mRNA.
DR CCDS; CCDS9074.1; -. [Q9GZN1-1]
DR RefSeq; NP_071941.1; NM_022496.4. [Q9GZN1-1]
DR RefSeq; XP_016875310.1; XM_017019821.1.
DR PDB; 6IGM; EM; 4.00 A; G=1-396.
DR PDBsum; 6IGM; -.
DR AlphaFoldDB; Q9GZN1; -.
DR SMR; Q9GZN1; -.
DR BioGRID; 122179; 41.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR CORUM; Q9GZN1; -.
DR IntAct; Q9GZN1; 28.
DR MINT; Q9GZN1; -.
DR STRING; 9606.ENSP00000188312; -.
DR iPTMnet; Q9GZN1; -.
DR PhosphoSitePlus; Q9GZN1; -.
DR BioMuta; ACTR6; -.
DR DMDM; 27923737; -.
DR EPD; Q9GZN1; -.
DR jPOST; Q9GZN1; -.
DR MassIVE; Q9GZN1; -.
DR MaxQB; Q9GZN1; -.
DR PaxDb; Q9GZN1; -.
DR PeptideAtlas; Q9GZN1; -.
DR PRIDE; Q9GZN1; -.
DR ProteomicsDB; 80095; -. [Q9GZN1-1]
DR Antibodypedia; 30297; 100 antibodies from 19 providers.
DR DNASU; 64431; -.
DR Ensembl; ENST00000188312.7; ENSP00000188312.2; ENSG00000075089.10. [Q9GZN1-1]
DR GeneID; 64431; -.
DR KEGG; hsa:64431; -.
DR MANE-Select; ENST00000188312.7; ENSP00000188312.2; NM_022496.5; NP_071941.1.
DR UCSC; uc001thb.3; human. [Q9GZN1-1]
DR CTD; 64431; -.
DR DisGeNET; 64431; -.
DR GeneCards; ACTR6; -.
DR HGNC; HGNC:24025; ACTR6.
DR HPA; ENSG00000075089; Low tissue specificity.
DR MIM; 619729; gene.
DR neXtProt; NX_Q9GZN1; -.
DR OpenTargets; ENSG00000075089; -.
DR PharmGKB; PA134984466; -.
DR VEuPathDB; HostDB:ENSG00000075089; -.
DR eggNOG; KOG0680; Eukaryota.
DR GeneTree; ENSGT00720000108833; -.
DR HOGENOM; CLU_027965_1_1_1; -.
DR InParanoid; Q9GZN1; -.
DR OMA; FFEEYEC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q9GZN1; -.
DR TreeFam; TF105780; -.
DR PathwayCommons; Q9GZN1; -.
DR SignaLink; Q9GZN1; -.
DR BioGRID-ORCS; 64431; 626 hits in 1098 CRISPR screens.
DR ChiTaRS; ACTR6; human.
DR GenomeRNAi; 64431; -.
DR Pharos; Q9GZN1; Tbio.
DR PRO; PR:Q9GZN1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9GZN1; protein.
DR Bgee; ENSG00000075089; Expressed in ganglionic eminence and 186 other tissues.
DR ExpressionAtlas; Q9GZN1; baseline and differential.
DR Genevisible; Q9GZN1; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; IMP:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR030054; Arp6.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR PANTHER; PTHR11937:SF47; PTHR11937:SF47; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..396
FT /note="Actin-related protein 6"
FT /id="PRO_0000089105"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 127..182
FT /note="AGALSAHRYFRDNPSELCCIIVDSGYSFTHIVPYCRSKKKKEAIIRINVGGK
FT LLTN -> GEFKFSLKLSYMTMDMNRVILIKSQNIKWHSWLAQWLTPVTPSVWEAEASR
FT SLEFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054637"
FT VAR_SEQ 183..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054638"
FT CONFLICT 218
FT /note="R -> G (in Ref. 4; BAD96679)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="K -> E (in Ref. 2; AAK14934)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="V -> A (in Ref. 2; AAK14934)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 45810 MW; E7F77190F60D1700 CRC64;
MTTLVLDNGA YNAKIGYSHE NVSVIPNCQF RSKTARLKTF TANQIDEIKD PSGLFYILPF
QKGYLVNWDV QRQVWDYLFG KEMYQVDFLD TNIIITEPYF NFTSIQESMN EILFEEYQFQ
AVLRVNAGAL SAHRYFRDNP SELCCIIVDS GYSFTHIVPY CRSKKKKEAI IRINVGGKLL
TNHLKEIISY RQLHVMDETH VINQVKEDVC YVSQDFYRDM DIAKLKGEEN TVMIDYVLPD
FSTIKKGFCK PREEMVLSGK YKSGEQILRL ANERFAVPEI LFNPSDIGIQ EMGIPEAIVY
SIQNLPEEMQ PHFFKNIVLT GGNSLFPGFR DRVYSEVRCL TPTDYDVSVV LPENPITYAW
EGGKLISEND DFEDMVVTRE DYEENGHSVC EEKFDI
