Full text data of ANLN
ANLN
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Actin-binding protein anillin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Actin-binding protein anillin
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00032958
IPI00032958 Actin binding protein anillin no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00032958 Actin binding protein anillin no information available soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q9NQW6
ID ANLN_HUMAN Reviewed; 1124 AA.
AC Q9NQW6; Q5CZ78; Q6NSK5; Q9H8Y4; Q9NVN9; Q9NVP0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Actin-binding protein anillin;
GN Name=ANLN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-185, FUNCTION,
RP INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=10931866; DOI=10.1083/jcb.150.3.539;
RA Oegema K., Savoian M.S., Mitchison T.J., Field C.M.;
RT "Functional analysis of a human homolog of the Drosophila actin
RT binding protein anillin suggests a role in cytokinesis.";
RL J. Cell Biol. 150:539-552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 696-1124 (ISOFORMS 1/2).
RC TISSUE=Squamous cell carcinoma, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1124 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-1124 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 580-1124 (ISOFORMS 1/2).
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP FUNCTION.
RX PubMed=12479805; DOI=10.1016/S1534-5807(02)00366-0;
RA Kinoshita M., Field C.M., Coughlin M.L., Straight A.F.,
RA Mitchison T.J.;
RT "Self- and actin-templated assembly of mammalian septins.";
RL Dev. Cell 3:791-802(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12637748; DOI=10.1126/science.1081412;
RA Straight A.F., Cheung A., Limouze J., Chen I., Westwood N.J.,
RA Sellers J.R., Mitchison T.J.;
RT "Dissecting temporal and spatial control of cytokinesis with a myosin
RT II inhibitor.";
RL Science 299:1743-1747(2003).
RN [7]
RP FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, OVEREXPRESSION
RP IN LUNG CANCER, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=16357138; DOI=10.1158/0008-5472.CAN-05-1507;
RA Suzuki C., Daigo Y., Ishikawa N., Kato T., Hayama S., Ito T.,
RA Tsuchiya E., Nakamura Y.;
RT "ANLN plays a critical role in human lung carcinogenesis through the
RT activation of RHOA and by involvement in the phosphoinositide 3-
RT kinase/AKT pathway.";
RL Cancer Res. 65:11314-11325(2005).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP OVEREXPRESSION IN CANCERS.
RX PubMed=16203764; DOI=10.1158/1078-0432.CCR-05-0997;
RA Hall P.A., Todd C.B., Hyland P.L., McDade S.S., Grabsch H.,
RA Dattani M., Hillan K.J., Russell S.E.H.;
RT "The septin-binding protein anillin is overexpressed in diverse human
RT tumors.";
RL Clin. Cancer Res. 11:6780-6786(2005).
RN [9]
RP FUNCTION, INTERACTION WITH FZR1, DEVELOPMENTAL STAGE, UBIQUITINATION,
RP AND MUTAGENESIS OF ARG-41 AND LEU-44.
RX PubMed=16040610; DOI=10.1074/jbc.M504657200;
RA Zhao W.-M., Fang G.;
RT "Anillin is a substrate of anaphase-promoting complex/cyclosome
RT (APC/C) that controls spatial contractility of myosin during late
RT cytokinesis.";
RL J. Biol. Chem. 280:33516-33524(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15496454; DOI=10.1091/mbc.E04-08-0758;
RA Straight A.F., Field C.M., Mitchison T.J.;
RT "Anillin binds nonmuscle myosin II and regulates the contractile
RT ring.";
RL Mol. Biol. Cell 16:193-201(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15616196; DOI=10.1091/mbc.E04-04-0346;
RA Mollinari C., Kleman J.-P., Saoudi Y., Jablonski S.A., Perard J.,
RA Yen T.J., Margolis R.L.;
RT "Ablation of PRC1 by small interfering RNA demonstrates that
RT cytokinetic abscission requires a central spindle bundle in mammalian
RT cells, whereas completion of furrowing does not.";
RL Mol. Biol. Cell 16:1043-1055(2005).
RN [12]
RP INTERACTION WITH CD2AP, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION, AND MUTAGENESIS OF ARG-32.
RX PubMed=15800069; DOI=10.1091/mbc.E04-09-0773;
RA Monzo P., Gauthier N.C., Keslair F., Loubat A., Field C.M.,
RA Le Marchand-Brustel Y., Cormont M.;
RT "Clues to CD2-associated protein involvement in cytokinesis.";
RL Mol. Biol. Cell 16:2891-2902(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16129829; DOI=10.1073/pnas.0504145102;
RA Zhao W.-M., Fang G.;
RT "MgcRacGAP controls the assembly of the contractile ring and the
RT initiation of cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; THR-194 AND
RP THR-401, VARIANT [LARGE SCALE ANALYSIS] LYS-185, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-72; SER-102;
RP SER-172; THR-320; SER-323; THR-364; THR-397; THR-401; SER-485;
RP SER-518; SER-553; SER-658; SER-661; SER-664; SER-792 AND SER-927, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-323, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-371, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-320; SER-323;
RP SER-449; SER-553; SER-561; SER-642; SER-658; SER-661; SER-792 AND
RP SER-927, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-323; SER-485 AND
RP SER-792, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC integrity of the cleavage furrow and for completion of cleavage
CC furrow ingression.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with CD2AP. May
CC interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm,
CC cell cortex. Note=Mainly found in the nucleus during interphase.
CC Colocalizes with cortical F-actin upon nuclear envelope breakdown
CC in mitosis and subsequently concentrates in the area of the
CC prospective contractile ring in anaphase. This pattern persists
CC until telophase, when the protein becomes concentrated in the
CC midbody.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQW6-2; Sequence=VSP_017617;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present at highest
CC levels in the brain, at high levels in the placenta and testis, at
CC intermediate levels in the intestine, ovary, skeletal muscle and
CC thymus and at lower levels in heart, kidney, liver, lung,
CC pancreas, prostate and spleen. Overexpressed in many tumor types
CC including breast, colorectal, endometrial, hepatic, kidney, lung,
CC ovarian and pancreatic tumors.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, heart, kidney,
CC liver, lung, skeletal muscle, spleen and thymus. In dividing cells
CC expression increases during S and G2 phases, peaks at mitosis and
CC subsequently drops as cells enter G1 phase.
CC -!- PTM: Phosphorylated during mitosis.
CC -!- PTM: Ubiquitinated, and this requires FZR1/CDH1.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34692.1; Type=Erroneous initiation;
CC Sequence=BAA91710.1; Type=Erroneous initiation;
CC Sequence=BAA91711.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ANLNID44318ch7p14.html";
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DR EMBL; AF273437; AAF75796.1; -; mRNA.
DR EMBL; BC034692; AAH34692.1; ALT_INIT; mRNA.
DR EMBL; BC070066; AAH70066.1; -; mRNA.
DR EMBL; CR936650; CAI56788.1; -; mRNA.
DR EMBL; AK001468; BAA91710.1; ALT_INIT; mRNA.
DR EMBL; AK001472; BAA91711.1; ALT_INIT; mRNA.
DR EMBL; AK023208; BAB14463.1; -; mRNA.
DR RefSeq; NP_001271230.1; NM_001284301.1.
DR RefSeq; NP_001271231.1; NM_001284302.1.
DR RefSeq; NP_061155.2; NM_018685.3.
DR UniGene; Hs.62180; -.
DR PDB; 2Y7B; X-ray; 1.90 A; A=980-1113.
DR PDBsum; 2Y7B; -.
DR ProteinModelPortal; Q9NQW6; -.
DR SMR; Q9NQW6; 980-1113.
DR IntAct; Q9NQW6; 4.
DR MINT; MINT-3072308; -.
DR STRING; 9606.ENSP00000265748; -.
DR PhosphoSite; Q9NQW6; -.
DR DMDM; 90111962; -.
DR PaxDb; Q9NQW6; -.
DR PRIDE; Q9NQW6; -.
DR Ensembl; ENST00000265748; ENSP00000265748; ENSG00000011426.
DR Ensembl; ENST00000396068; ENSP00000379380; ENSG00000011426.
DR GeneID; 54443; -.
DR KEGG; hsa:54443; -.
DR UCSC; uc003tff.3; human.
DR CTD; 54443; -.
DR GeneCards; GC07P036395; -.
DR H-InvDB; HIX0006603; -.
DR HGNC; HGNC:14082; ANLN.
DR neXtProt; NX_Q9NQW6; -.
DR PharmGKB; PA24809; -.
DR eggNOG; NOG247921; -.
DR HOGENOM; HOG000033950; -.
DR HOVERGEN; HBG059477; -.
DR InParanoid; Q9NQW6; -.
DR OMA; GAGIKPF; -.
DR OrthoDB; EOG7VHSZ0; -.
DR PhylomeDB; Q9NQW6; -.
DR GeneWiki; ANLN; -.
DR GenomeRNAi; 54443; -.
DR NextBio; 56677; -.
DR PRO; PR:Q9NQW6; -.
DR ArrayExpress; Q9NQW6; -.
DR Bgee; Q9NQW6; -.
DR CleanEx; HS_ANLN; -.
DR Genevestigator; Q9NQW6; -.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
DR GO; GO:0000921; P:septin ring assembly; TAS:ProtInc.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; DUF1709.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 1124 Actin-binding protein anillin.
FT /FTId=PRO_0000227965.
FT DOMAIN 983 1107 PH.
FT REGION 1 230 Nuclear localization.
FT REGION 1 155 Interaction with CD2AP.
FT REGION 1 45 Required for ubiquitination.
FT REGION 231 676 Interaction with F-actin.
FT REGION 730 1124 Localization to the cleavage furrow.
FT COILED 569 604 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 54 54 Phosphoserine.
FT MOD_RES 72 72 Phosphoserine.
FT MOD_RES 102 102 Phosphoserine.
FT MOD_RES 172 172 Phosphoserine.
FT MOD_RES 182 182 Phosphoserine.
FT MOD_RES 194 194 Phosphothreonine.
FT MOD_RES 320 320 Phosphothreonine.
FT MOD_RES 323 323 Phosphoserine.
FT MOD_RES 364 364 Phosphothreonine.
FT MOD_RES 371 371 N6-acetyllysine.
FT MOD_RES 397 397 Phosphothreonine.
FT MOD_RES 401 401 Phosphothreonine.
FT MOD_RES 449 449 Phosphoserine.
FT MOD_RES 485 485 Phosphoserine.
FT MOD_RES 518 518 Phosphoserine.
FT MOD_RES 553 553 Phosphoserine.
FT MOD_RES 561 561 Phosphoserine.
FT MOD_RES 642 642 Phosphoserine.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 661 661 Phosphoserine.
FT MOD_RES 664 664 Phosphoserine.
FT MOD_RES 792 792 Phosphoserine.
FT MOD_RES 927 927 Phosphoserine.
FT VAR_SEQ 508 544 Missing (in isoform 2).
FT /FTId=VSP_017617.
FT VARIANT 65 65 S -> W (in dbSNP:rs3735400).
FT /FTId=VAR_025661.
FT VARIANT 185 185 R -> K (in dbSNP:rs197367).
FT /FTId=VAR_025662.
FT MUTAGEN 32 32 R->A: Abrogates interaction with CD2AP.
FT MUTAGEN 41 41 R->A: Abrogates ubiquitin-mediated
FT proteolysis; when associated with A-44.
FT MUTAGEN 44 44 L->A: Abrogates ubiquitin-mediated
FT proteolysis; when associated with A-41.
FT CONFLICT 53 53 L -> F (in Ref. 1; AAF75796).
FT CONFLICT 62 62 T -> S (in Ref. 1; AAF75796).
FT CONFLICT 294 294 T -> TS (in Ref. 1 and 3).
FT CONFLICT 410 410 R -> K (in Ref. 2; AAH70066).
FT CONFLICT 625 625 L -> S (in Ref. 4; BAA91711).
FT CONFLICT 1035 1035 A -> V (in Ref. 3; CAI56788).
FT STRAND 986 996
FT STRAND 999 1010
FT STRAND 1013 1019
FT HELIX 1020 1023
FT STRAND 1029 1033
FT HELIX 1034 1036
FT STRAND 1039 1041
FT TURN 1047 1049
FT STRAND 1055 1063
FT STRAND 1072 1077
FT STRAND 1080 1088
FT HELIX 1092 1110
SQ SEQUENCE 1124 AA; 124199 MW; 79A8CC25C950DB2D CRC64;
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS
CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP
ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA
ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS
ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD
KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST
THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV
SKTQSLPVTE KVTENQIPAK NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV
EQKIEVIREI EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR TRVPRAESGD
SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT SKLDEKNNAF PCQVNIKQKM
QELNNEINMQ QTVIYQASQA LNCCVDEEHG KGSLEEAEAE RLLLIATGKR TLLIDELNKL
KNEGPQRKNK ASPQSEFMPS KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA
ENMVATPLAS TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS SVGNTKFVLD
KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG AWHRRWCVLS GNCISYWTYP
DDEKRKNPIG RINLANCTSR QIEPANREFC ARRNTFELIT VRPQREDDRE TLVSQCRDTL
CVTKNWLSAD TKEERDLWMQ KLNQVLVDIR LWQPDACYKP IGKP
//
ID ANLN_HUMAN Reviewed; 1124 AA.
AC Q9NQW6; Q5CZ78; Q6NSK5; Q9H8Y4; Q9NVN9; Q9NVP0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 21-MAR-2006, sequence version 2.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Actin-binding protein anillin;
GN Name=ANLN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-185, FUNCTION,
RP INTERACTION WITH ACTIN, AND SUBCELLULAR LOCATION.
RX PubMed=10931866; DOI=10.1083/jcb.150.3.539;
RA Oegema K., Savoian M.S., Mitchison T.J., Field C.M.;
RT "Functional analysis of a human homolog of the Drosophila actin
RT binding protein anillin suggests a role in cytokinesis.";
RL J. Cell Biol. 150:539-552(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 696-1124 (ISOFORMS 1/2).
RC TISSUE=Squamous cell carcinoma, and Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1124 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-1124 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 580-1124 (ISOFORMS 1/2).
RC TISSUE=Teratocarcinoma;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP FUNCTION.
RX PubMed=12479805; DOI=10.1016/S1534-5807(02)00366-0;
RA Kinoshita M., Field C.M., Coughlin M.L., Straight A.F.,
RA Mitchison T.J.;
RT "Self- and actin-templated assembly of mammalian septins.";
RL Dev. Cell 3:791-802(2002).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=12637748; DOI=10.1126/science.1081412;
RA Straight A.F., Cheung A., Limouze J., Chen I., Westwood N.J.,
RA Sellers J.R., Mitchison T.J.;
RT "Dissecting temporal and spatial control of cytokinesis with a myosin
RT II inhibitor.";
RL Science 299:1743-1747(2003).
RN [7]
RP FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, OVEREXPRESSION
RP IN LUNG CANCER, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RX PubMed=16357138; DOI=10.1158/0008-5472.CAN-05-1507;
RA Suzuki C., Daigo Y., Ishikawa N., Kato T., Hayama S., Ito T.,
RA Tsuchiya E., Nakamura Y.;
RT "ANLN plays a critical role in human lung carcinogenesis through the
RT activation of RHOA and by involvement in the phosphoinositide 3-
RT kinase/AKT pathway.";
RL Cancer Res. 65:11314-11325(2005).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP OVEREXPRESSION IN CANCERS.
RX PubMed=16203764; DOI=10.1158/1078-0432.CCR-05-0997;
RA Hall P.A., Todd C.B., Hyland P.L., McDade S.S., Grabsch H.,
RA Dattani M., Hillan K.J., Russell S.E.H.;
RT "The septin-binding protein anillin is overexpressed in diverse human
RT tumors.";
RL Clin. Cancer Res. 11:6780-6786(2005).
RN [9]
RP FUNCTION, INTERACTION WITH FZR1, DEVELOPMENTAL STAGE, UBIQUITINATION,
RP AND MUTAGENESIS OF ARG-41 AND LEU-44.
RX PubMed=16040610; DOI=10.1074/jbc.M504657200;
RA Zhao W.-M., Fang G.;
RT "Anillin is a substrate of anaphase-promoting complex/cyclosome
RT (APC/C) that controls spatial contractility of myosin during late
RT cytokinesis.";
RL J. Biol. Chem. 280:33516-33524(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15496454; DOI=10.1091/mbc.E04-08-0758;
RA Straight A.F., Field C.M., Mitchison T.J.;
RT "Anillin binds nonmuscle myosin II and regulates the contractile
RT ring.";
RL Mol. Biol. Cell 16:193-201(2005).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=15616196; DOI=10.1091/mbc.E04-04-0346;
RA Mollinari C., Kleman J.-P., Saoudi Y., Jablonski S.A., Perard J.,
RA Yen T.J., Margolis R.L.;
RT "Ablation of PRC1 by small interfering RNA demonstrates that
RT cytokinetic abscission requires a central spindle bundle in mammalian
RT cells, whereas completion of furrowing does not.";
RL Mol. Biol. Cell 16:1043-1055(2005).
RN [12]
RP INTERACTION WITH CD2AP, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION, AND MUTAGENESIS OF ARG-32.
RX PubMed=15800069; DOI=10.1091/mbc.E04-09-0773;
RA Monzo P., Gauthier N.C., Keslair F., Loubat A., Field C.M.,
RA Le Marchand-Brustel Y., Cormont M.;
RT "Clues to CD2-associated protein involvement in cytokinesis.";
RL Mol. Biol. Cell 16:2891-2902(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16129829; DOI=10.1073/pnas.0504145102;
RA Zhao W.-M., Fang G.;
RT "MgcRacGAP controls the assembly of the contractile ring and the
RT initiation of cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; THR-194 AND
RP THR-401, VARIANT [LARGE SCALE ANALYSIS] LYS-185, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-72; SER-102;
RP SER-172; THR-320; SER-323; THR-364; THR-397; THR-401; SER-485;
RP SER-518; SER-553; SER-658; SER-661; SER-664; SER-792 AND SER-927, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-323, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-371, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; THR-320; SER-323;
RP SER-449; SER-553; SER-561; SER-642; SER-658; SER-661; SER-792 AND
RP SER-927, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-323; SER-485 AND
RP SER-792, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC integrity of the cleavage furrow and for completion of cleavage
CC furrow ingression.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with CD2AP. May
CC interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm,
CC cell cortex. Note=Mainly found in the nucleus during interphase.
CC Colocalizes with cortical F-actin upon nuclear envelope breakdown
CC in mitosis and subsequently concentrates in the area of the
CC prospective contractile ring in anaphase. This pattern persists
CC until telophase, when the protein becomes concentrated in the
CC midbody.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NQW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NQW6-2; Sequence=VSP_017617;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Present at highest
CC levels in the brain, at high levels in the placenta and testis, at
CC intermediate levels in the intestine, ovary, skeletal muscle and
CC thymus and at lower levels in heart, kidney, liver, lung,
CC pancreas, prostate and spleen. Overexpressed in many tumor types
CC including breast, colorectal, endometrial, hepatic, kidney, lung,
CC ovarian and pancreatic tumors.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, heart, kidney,
CC liver, lung, skeletal muscle, spleen and thymus. In dividing cells
CC expression increases during S and G2 phases, peaks at mitosis and
CC subsequently drops as cells enter G1 phase.
CC -!- PTM: Phosphorylated during mitosis.
CC -!- PTM: Ubiquitinated, and this requires FZR1/CDH1.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34692.1; Type=Erroneous initiation;
CC Sequence=BAA91710.1; Type=Erroneous initiation;
CC Sequence=BAA91711.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ANLNID44318ch7p14.html";
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DR EMBL; AF273437; AAF75796.1; -; mRNA.
DR EMBL; BC034692; AAH34692.1; ALT_INIT; mRNA.
DR EMBL; BC070066; AAH70066.1; -; mRNA.
DR EMBL; CR936650; CAI56788.1; -; mRNA.
DR EMBL; AK001468; BAA91710.1; ALT_INIT; mRNA.
DR EMBL; AK001472; BAA91711.1; ALT_INIT; mRNA.
DR EMBL; AK023208; BAB14463.1; -; mRNA.
DR RefSeq; NP_001271230.1; NM_001284301.1.
DR RefSeq; NP_001271231.1; NM_001284302.1.
DR RefSeq; NP_061155.2; NM_018685.3.
DR UniGene; Hs.62180; -.
DR PDB; 2Y7B; X-ray; 1.90 A; A=980-1113.
DR PDBsum; 2Y7B; -.
DR ProteinModelPortal; Q9NQW6; -.
DR SMR; Q9NQW6; 980-1113.
DR IntAct; Q9NQW6; 4.
DR MINT; MINT-3072308; -.
DR STRING; 9606.ENSP00000265748; -.
DR PhosphoSite; Q9NQW6; -.
DR DMDM; 90111962; -.
DR PaxDb; Q9NQW6; -.
DR PRIDE; Q9NQW6; -.
DR Ensembl; ENST00000265748; ENSP00000265748; ENSG00000011426.
DR Ensembl; ENST00000396068; ENSP00000379380; ENSG00000011426.
DR GeneID; 54443; -.
DR KEGG; hsa:54443; -.
DR UCSC; uc003tff.3; human.
DR CTD; 54443; -.
DR GeneCards; GC07P036395; -.
DR H-InvDB; HIX0006603; -.
DR HGNC; HGNC:14082; ANLN.
DR neXtProt; NX_Q9NQW6; -.
DR PharmGKB; PA24809; -.
DR eggNOG; NOG247921; -.
DR HOGENOM; HOG000033950; -.
DR HOVERGEN; HBG059477; -.
DR InParanoid; Q9NQW6; -.
DR OMA; GAGIKPF; -.
DR OrthoDB; EOG7VHSZ0; -.
DR PhylomeDB; Q9NQW6; -.
DR GeneWiki; ANLN; -.
DR GenomeRNAi; 54443; -.
DR NextBio; 56677; -.
DR PRO; PR:Q9NQW6; -.
DR ArrayExpress; Q9NQW6; -.
DR Bgee; Q9NQW6; -.
DR CleanEx; HS_ANLN; -.
DR Genevestigator; Q9NQW6; -.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
DR GO; GO:0000921; P:septin ring assembly; TAS:ProtInc.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; DUF1709.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 1124 Actin-binding protein anillin.
FT /FTId=PRO_0000227965.
FT DOMAIN 983 1107 PH.
FT REGION 1 230 Nuclear localization.
FT REGION 1 155 Interaction with CD2AP.
FT REGION 1 45 Required for ubiquitination.
FT REGION 231 676 Interaction with F-actin.
FT REGION 730 1124 Localization to the cleavage furrow.
FT COILED 569 604 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 54 54 Phosphoserine.
FT MOD_RES 72 72 Phosphoserine.
FT MOD_RES 102 102 Phosphoserine.
FT MOD_RES 172 172 Phosphoserine.
FT MOD_RES 182 182 Phosphoserine.
FT MOD_RES 194 194 Phosphothreonine.
FT MOD_RES 320 320 Phosphothreonine.
FT MOD_RES 323 323 Phosphoserine.
FT MOD_RES 364 364 Phosphothreonine.
FT MOD_RES 371 371 N6-acetyllysine.
FT MOD_RES 397 397 Phosphothreonine.
FT MOD_RES 401 401 Phosphothreonine.
FT MOD_RES 449 449 Phosphoserine.
FT MOD_RES 485 485 Phosphoserine.
FT MOD_RES 518 518 Phosphoserine.
FT MOD_RES 553 553 Phosphoserine.
FT MOD_RES 561 561 Phosphoserine.
FT MOD_RES 642 642 Phosphoserine.
FT MOD_RES 658 658 Phosphoserine.
FT MOD_RES 661 661 Phosphoserine.
FT MOD_RES 664 664 Phosphoserine.
FT MOD_RES 792 792 Phosphoserine.
FT MOD_RES 927 927 Phosphoserine.
FT VAR_SEQ 508 544 Missing (in isoform 2).
FT /FTId=VSP_017617.
FT VARIANT 65 65 S -> W (in dbSNP:rs3735400).
FT /FTId=VAR_025661.
FT VARIANT 185 185 R -> K (in dbSNP:rs197367).
FT /FTId=VAR_025662.
FT MUTAGEN 32 32 R->A: Abrogates interaction with CD2AP.
FT MUTAGEN 41 41 R->A: Abrogates ubiquitin-mediated
FT proteolysis; when associated with A-44.
FT MUTAGEN 44 44 L->A: Abrogates ubiquitin-mediated
FT proteolysis; when associated with A-41.
FT CONFLICT 53 53 L -> F (in Ref. 1; AAF75796).
FT CONFLICT 62 62 T -> S (in Ref. 1; AAF75796).
FT CONFLICT 294 294 T -> TS (in Ref. 1 and 3).
FT CONFLICT 410 410 R -> K (in Ref. 2; AAH70066).
FT CONFLICT 625 625 L -> S (in Ref. 4; BAA91711).
FT CONFLICT 1035 1035 A -> V (in Ref. 3; CAI56788).
FT STRAND 986 996
FT STRAND 999 1010
FT STRAND 1013 1019
FT HELIX 1020 1023
FT STRAND 1029 1033
FT HELIX 1034 1036
FT STRAND 1039 1041
FT TURN 1047 1049
FT STRAND 1055 1063
FT STRAND 1072 1077
FT STRAND 1080 1088
FT HELIX 1092 1110
SQ SEQUENCE 1124 AA; 124199 MW; 79A8CC25C950DB2D CRC64;
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS
CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP
ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA
ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS
ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD
KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST
THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV
SKTQSLPVTE KVTENQIPAK NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV
EQKIEVIREI EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR TRVPRAESGD
SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT SKLDEKNNAF PCQVNIKQKM
QELNNEINMQ QTVIYQASQA LNCCVDEEHG KGSLEEAEAE RLLLIATGKR TLLIDELNKL
KNEGPQRKNK ASPQSEFMPS KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA
ENMVATPLAS TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS SVGNTKFVLD
KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG AWHRRWCVLS GNCISYWTYP
DDEKRKNPIG RINLANCTSR QIEPANREFC ARRNTFELIT VRPQREDDRE TLVSQCRDTL
CVTKNWLSAD TKEERDLWMQ KLNQVLVDIR LWQPDACYKP IGKP
//