ANLN_HUMAN
ID ANLN_HUMAN Reviewed; 1124 AA.
AC Q9NQW6; Q5CZ78; Q6NSK5; Q9H8Y4; Q9NVN9; Q9NVP0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Anillin;
GN Name=ANLN;
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), 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 binding
RT 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 SEQUENCE
RP [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 project:
RT 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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., 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 [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., 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., Sellers J.R.,
RA Mitchison T.J.;
RT "Dissecting temporal and spatial control of cytokinesis with a myosin II
RT inhibitor.";
RL Science 299:1743-1747(2003).
RN [7]
RP FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, OVEREXPRESSION IN
RP 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., Tsuchiya E.,
RA 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-kinase/AKT
RT 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., Dattani M.,
RA 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, AND
RP 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 (APC/C)
RT that controls spatial contractility of myosin during late 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 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., Yen T.J.,
RA Margolis R.L.;
RT "Ablation of PRC1 by small interfering RNA demonstrates that cytokinetic
RT abscission requires a central spindle bundle in mammalian cells, whereas
RT 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 initiation
RT 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 THR-401,
RP VARIANT [LARGE SCALE ANALYSIS] LYS-185, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 cells
RT and high confident phosphopeptide identification by cross-validation of
RT 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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-72; SER-102; SER-172;
RP THR-320; SER-323; THR-364; THR-397; THR-401; SER-485; SER-518; SER-553;
RP SER-658; SER-661; SER-664; SER-792 AND SER-927, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-323, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-449; SER-553;
RP SER-561; SER-642; SER-658; SER-661; SER-792 AND SER-927, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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-485 AND SER-792, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23870127; DOI=10.1016/j.cell.2013.06.010;
RA Kiyomitsu T., Cheeseman I.M.;
RT "Cortical dynein and asymmetric membrane elongation coordinately position
RT the spindle in anaphase.";
RL Cell 154:391-402(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-225; SER-252;
RP SER-339; THR-364; THR-401; SER-417; SER-419; SER-485; SER-518; SER-637;
RP SER-642; SER-658; SER-661; SER-678; SER-688; SER-792 AND SER-927, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP FUNCTION, INVOLVEMENT IN FSGS8, TISSUE SPECIFICITY, VARIANTS FSGS8 CYS-431
RP AND CYS-618, AND CHARACTERIZATION OF VARIANT FSGS8 CYS-431.
RX PubMed=24676636; DOI=10.1681/asn.2013090976;
RA Gbadegesin R.A., Hall G., Adeyemo A., Hanke N., Tossidou I., Burchette J.,
RA Wu G., Homstad A., Sparks M.A., Gomez J., Jiang R., Alonso A., Lavin P.,
RA Conlon P., Korstanje R., Stander M.C., Shamsan G., Barua M., Spurney R.,
RA Singhal P.C., Kopp J.B., Haller H., Howell D., Pollak M.R., Shaw A.S.,
RA Schiffer M., Winn M.P.;
RT "Mutations in the gene that encodes the F-actin binding protein anillin
RT cause FSGS.";
RL J. Am. Soc. Nephrol. 25:1991-2002(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
CC -!- FUNCTION: Required for cytokinesis (PubMed:16040610). Essential for the
CC structural integrity of the cleavage furrow and for completion of
CC cleavage furrow ingression. Plays a role in bleb assembly during
CC metaphase and anaphase of mitosis (PubMed:23870127). May play a
CC significant role in podocyte cell migration (PubMed:24676636).
CC {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:12479805,
CC ECO:0000269|PubMed:15496454, ECO:0000269|PubMed:16040610,
CC ECO:0000269|PubMed:16357138, ECO:0000269|PubMed:23870127,
CC ECO:0000269|PubMed:24676636}.
CC -!- SUBUNIT: Interacts with F-actin (PubMed:10931866). Interacts with CD2AP
CC (PubMed:15800069). May interact with RHOA (PubMed:16357138). Interacts
CC with FZR1/CDH1 during mitotic exit (PubMed:16040610).
CC {ECO:0000269|PubMed:10931866, ECO:0000269|PubMed:15800069,
CC ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16357138}.
CC -!- INTERACTION:
CC Q9NQW6-2; Q8NA82: MARCHF10; NbExp=3; IntAct=EBI-10312488, EBI-2341554;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell
CC cortex {ECO:0000269|PubMed:23870127}. Cell projection, bleb
CC {ECO:0000269|PubMed:23870127}. Note=Mainly found in the nucleus during
CC interphase. Colocalizes with cortical F-actin upon nuclear envelope
CC breakdown in mitosis and subsequently concentrates in the area of the
CC prospective contractile ring in anaphase. This pattern persists until
CC telophase, when the protein becomes concentrated in the 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 levels
CC in the brain, at high levels in the placenta and testis, at
CC intermediate levels in the intestine, ovary, skeletal muscle and thymus
CC and at lower levels in heart, kidney, liver, lung, pancreas, prostate
CC and spleen. In the kidney, it is widely expressed in tubules, but
CC sparsely expressed in the glomerulus (PubMed:24676636). Expression is
CC significantly increased in renal biopsy specimens from idiopathic FSGS
CC (PubMed:24676636). Overexpressed in many tumor types including breast,
CC colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic
CC tumors. {ECO:0000269|PubMed:16203764, ECO:0000269|PubMed:24676636}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, heart, kidney, liver,
CC lung, skeletal muscle, spleen and thymus. In dividing cells expression
CC increases during S and G2 phases, peaks at mitosis and subsequently
CC drops as cells enter G1 phase. {ECO:0000269|PubMed:15800069,
CC ECO:0000269|PubMed:16040610, ECO:0000269|PubMed:16203764,
CC ECO:0000269|PubMed:16357138}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000269|PubMed:15800069,
CC ECO:0000269|PubMed:16357138}.
CC -!- PTM: Ubiquitinated, and this requires FZR1/CDH1.
CC {ECO:0000269|PubMed:16040610}.
CC -!- DISEASE: Focal segmental glomerulosclerosis 8 (FSGS8) [MIM:616032]: A
CC renal pathology defined by the presence of segmental sclerosis in
CC glomeruli and resulting in proteinuria, reduced glomerular filtration
CC rate and progressive decline in renal function. Renal insufficiency
CC often progresses to end-stage renal disease, a highly morbid state
CC requiring either dialysis therapy or kidney transplantation.
CC {ECO:0000269|PubMed:24676636}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91711.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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 CCDS; CCDS5447.1; -. [Q9NQW6-1]
DR CCDS; CCDS64628.1; -. [Q9NQW6-2]
DR RefSeq; NP_001271230.1; NM_001284301.2. [Q9NQW6-2]
DR RefSeq; NP_001271231.1; NM_001284302.2.
DR RefSeq; NP_061155.2; NM_018685.4. [Q9NQW6-1]
DR PDB; 2Y7B; X-ray; 1.90 A; A=980-1113.
DR PDB; 4XH3; X-ray; 2.10 A; A=712-1124.
DR PDB; 4XOI; X-ray; 2.09 A; B/D=712-981.
DR PDBsum; 2Y7B; -.
DR PDBsum; 4XH3; -.
DR PDBsum; 4XOI; -.
DR AlphaFoldDB; Q9NQW6; -.
DR SMR; Q9NQW6; -.
DR BioGRID; 119959; 1039.
DR IntAct; Q9NQW6; 148.
DR MINT; Q9NQW6; -.
DR STRING; 9606.ENSP00000265748; -.
DR GlyGen; Q9NQW6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQW6; -.
DR MetOSite; Q9NQW6; -.
DR PhosphoSitePlus; Q9NQW6; -.
DR BioMuta; ANLN; -.
DR DMDM; 90111962; -.
DR EPD; Q9NQW6; -.
DR jPOST; Q9NQW6; -.
DR MassIVE; Q9NQW6; -.
DR MaxQB; Q9NQW6; -.
DR PaxDb; Q9NQW6; -.
DR PeptideAtlas; Q9NQW6; -.
DR PRIDE; Q9NQW6; -.
DR ProteomicsDB; 82209; -. [Q9NQW6-1]
DR ProteomicsDB; 82210; -. [Q9NQW6-2]
DR Antibodypedia; 26544; 254 antibodies from 34 providers.
DR DNASU; 54443; -.
DR Ensembl; ENST00000265748.7; ENSP00000265748.2; ENSG00000011426.11. [Q9NQW6-1]
DR Ensembl; ENST00000396068.6; ENSP00000379380.2; ENSG00000011426.11. [Q9NQW6-2]
DR GeneID; 54443; -.
DR KEGG; hsa:54443; -.
DR MANE-Select; ENST00000265748.7; ENSP00000265748.2; NM_018685.5; NP_061155.2.
DR UCSC; uc003tff.4; human. [Q9NQW6-1]
DR CTD; 54443; -.
DR DisGeNET; 54443; -.
DR GeneCards; ANLN; -.
DR HGNC; HGNC:14082; ANLN.
DR HPA; ENSG00000011426; Tissue enriched (brain).
DR MalaCards; ANLN; -.
DR MIM; 616027; gene.
DR MIM; 616032; phenotype.
DR neXtProt; NX_Q9NQW6; -.
DR OpenTargets; ENSG00000011426; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA24809; -.
DR VEuPathDB; HostDB:ENSG00000011426; -.
DR eggNOG; KOG3640; Eukaryota.
DR GeneTree; ENSGT00390000008749; -.
DR HOGENOM; CLU_009118_0_0_1; -.
DR InParanoid; Q9NQW6; -.
DR OMA; FIMKSTT; -.
DR OrthoDB; 130192at2759; -.
DR PhylomeDB; Q9NQW6; -.
DR TreeFam; TF106494; -.
DR PathwayCommons; Q9NQW6; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR SignaLink; Q9NQW6; -.
DR BioGRID-ORCS; 54443; 391 hits in 1085 CRISPR screens.
DR ChiTaRS; ANLN; human.
DR GeneWiki; ANLN; -.
DR GenomeRNAi; 54443; -.
DR Pharos; Q9NQW6; Tbio.
DR PRO; PR:Q9NQW6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NQW6; protein.
DR Bgee; ENSG00000011426; Expressed in corpus callosum and 154 other tissues.
DR ExpressionAtlas; Q9NQW6; baseline and differential.
DR Genevisible; Q9NQW6; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:MGI.
DR GO; GO:0032059; C:bleb; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:MGI.
DR GO; GO:0090521; P:podocyte cell migration; IMP:UniProtKB.
DR GO; GO:1904172; P:positive regulation of bleb assembly; IMP:UniProtKB.
DR GO; GO:0007096; P:regulation of exit from mitosis; TAS:ProtInc.
DR GO; GO:0000921; P:septin ring assembly; TAS:ProtInc.
DR GO; GO:0031106; P:septin ring organization; IBA:GO_Central.
DR CDD; cd01263; PH_anillin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012966; AHD.
DR InterPro; IPR031970; Anillin_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037840; PH_Anillin.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF08174; Anillin; 1.
DR Pfam; PF16018; Anillin_N; 2.
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; Cell cycle;
KW Cell division; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Isopeptide bond; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1124
FT /note="Anillin"
FT /id="PRO_0000227965"
FT DOMAIN 983..1107
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..230
FT /note="Nuclear localization"
FT REGION 1..155
FT /note="Interaction with CD2AP"
FT /evidence="ECO:0000269|PubMed:15800069"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..45
FT /note="Required for ubiquitination"
FT REGION 136..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..676
FT /note="Interaction with F-actin"
FT REGION 294..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..1124
FT /note="Localization to the cleavage furrow"
FT COILED 569..604
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K298"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K298"
FT MOD_RES 320
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 371
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 671
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8K298"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 254
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 508..544
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_017617"
FT VARIANT 65
FT /note="S -> W (in dbSNP:rs3735400)"
FT /id="VAR_025661"
FT VARIANT 185
FT /note="R -> K (in dbSNP:rs197367)"
FT /evidence="ECO:0000269|PubMed:10931866,
FT ECO:0007744|PubMed:16964243"
FT /id="VAR_025662"
FT VARIANT 431
FT /note="R -> C (in FSGS8; results in decreased interaction
FT with CD2AP; dbSNP:rs587777741)"
FT /evidence="ECO:0000269|PubMed:24676636"
FT /id="VAR_072418"
FT VARIANT 618
FT /note="G -> C (in FSGS8; dbSNP:rs1184529372)"
FT /evidence="ECO:0000269|PubMed:24676636"
FT /id="VAR_072419"
FT MUTAGEN 32
FT /note="R->A: Abrogates interaction with CD2AP."
FT /evidence="ECO:0000269|PubMed:15800069"
FT MUTAGEN 41
FT /note="R->A: Abrogates ubiquitin-mediated proteolysis; when
FT associated with A-44."
FT /evidence="ECO:0000269|PubMed:16040610"
FT MUTAGEN 44
FT /note="L->A: Abrogates ubiquitin-mediated proteolysis; when
FT associated with A-41."
FT /evidence="ECO:0000269|PubMed:16040610"
FT CONFLICT 53
FT /note="L -> F (in Ref. 1; AAF75796)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="T -> S (in Ref. 1; AAF75796)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="T -> TS (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="R -> K (in Ref. 2; AAH70066)"
FT /evidence="ECO:0000305"
FT CONFLICT 625
FT /note="L -> S (in Ref. 4; BAA91711)"
FT /evidence="ECO:0000305"
FT CONFLICT 1035
FT /note="A -> V (in Ref. 3; CAI56788)"
FT /evidence="ECO:0000305"
FT HELIX 716..742
FT /evidence="ECO:0007829|PDB:4XOI"
FT HELIX 747..749
FT /evidence="ECO:0007829|PDB:4XOI"
FT TURN 750..752
FT /evidence="ECO:0007829|PDB:4XOI"
FT HELIX 754..781
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 802..813
FT /evidence="ECO:0007829|PDB:4XOI"
FT HELIX 815..823
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 827..845
FT /evidence="ECO:0007829|PDB:4XOI"
FT TURN 851..853
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 866..871
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 877..887
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 940..947
FT /evidence="ECO:0007829|PDB:4XOI"
FT HELIX 949..951
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 956..958
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 970..979
FT /evidence="ECO:0007829|PDB:4XOI"
FT STRAND 986..996
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 999..1010
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1013..1019
FT /evidence="ECO:0007829|PDB:2Y7B"
FT HELIX 1020..1023
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1029..1033
FT /evidence="ECO:0007829|PDB:2Y7B"
FT HELIX 1034..1036
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:2Y7B"
FT TURN 1047..1049
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1055..1063
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1072..1077
FT /evidence="ECO:0007829|PDB:2Y7B"
FT STRAND 1080..1088
FT /evidence="ECO:0007829|PDB:2Y7B"
FT HELIX 1092..1110
FT /evidence="ECO:0007829|PDB:2Y7B"
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
