ANLN_MOUSE
ID ANLN_MOUSE Reviewed; 1121 AA.
AC Q8K298; Q8BL79; Q8BLB3; Q8K2N0; Q9CUY0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Anillin;
GN Name=Anln;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 247-1121.
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-96; SER-180; THR-192;
RP SER-259; SER-548; SER-637; SER-653; SER-656; SER-659 AND TYR-666, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC integrity of the cleavage furrow and for completion of cleavage furrow
CC ingression. Plays a role in bleb assembly during metaphase and anaphase
CC of mitosis. May play a significant role in podocyte cell migration.
CC {ECO:0000250|UniProtKB:Q9NQW6}.
CC -!- SUBUNIT: Interacts with F-actin. Interacts with CD2AP. May interact
CC with RHOA. Interacts with FZR1/CDH1 during mitotic exit.
CC {ECO:0000250|UniProtKB:Q9NQW6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9NQW6}.
CC Cell projection, bleb {ECO:0000250|UniProtKB:Q9NQW6}. Note=Mainly found
CC in the nucleus during interphase. Colocalizes with cortical F-actin
CC upon nuclear envelope breakdown in mitosis and subsequently
CC concentrates in the area of the prospective contractile ring in
CC anaphase. This pattern persists until telophase, when the protein
CC becomes concentrated in the midbody. {ECO:0000250|UniProtKB:Q9NQW6}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250}.
CC -!- PTM: Ubiquitinated, and this requires FZR1/CDH1. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH30489.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC32605.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC030489; AAH30489.1; ALT_INIT; mRNA.
DR EMBL; BC032164; AAH32164.1; -; mRNA.
DR EMBL; AK013624; BAB28931.3; -; mRNA.
DR EMBL; AK045703; BAC32464.1; -; mRNA.
DR EMBL; AK046102; BAC32605.1; ALT_INIT; mRNA.
DR CCDS; CCDS22927.1; -.
DR RefSeq; NP_082666.2; NM_028390.3.
DR AlphaFoldDB; Q8K298; -.
DR SMR; Q8K298; -.
DR BioGRID; 213029; 4.
DR IntAct; Q8K298; 2.
DR MINT; Q8K298; -.
DR STRING; 10090.ENSMUSP00000045873; -.
DR GlyConnect; 2105; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K298; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K298; -.
DR PhosphoSitePlus; Q8K298; -.
DR SwissPalm; Q8K298; -.
DR EPD; Q8K298; -.
DR jPOST; Q8K298; -.
DR MaxQB; Q8K298; -.
DR PaxDb; Q8K298; -.
DR PeptideAtlas; Q8K298; -.
DR PRIDE; Q8K298; -.
DR ProteomicsDB; 281869; -.
DR Antibodypedia; 26544; 254 antibodies from 34 providers.
DR DNASU; 68743; -.
DR Ensembl; ENSMUST00000040912; ENSMUSP00000045873; ENSMUSG00000036777.
DR GeneID; 68743; -.
DR KEGG; mmu:68743; -.
DR UCSC; uc009ook.2; mouse.
DR CTD; 54443; -.
DR MGI; MGI:1920174; Anln.
DR VEuPathDB; HostDB:ENSMUSG00000036777; -.
DR eggNOG; KOG3640; Eukaryota.
DR GeneTree; ENSGT00390000008749; -.
DR HOGENOM; CLU_009118_0_0_1; -.
DR InParanoid; Q8K298; -.
DR OMA; FIMKSTT; -.
DR OrthoDB; 130192at2759; -.
DR PhylomeDB; Q8K298; -.
DR TreeFam; TF106494; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR BioGRID-ORCS; 68743; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Anln; mouse.
DR PRO; PR:Q8K298; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8K298; protein.
DR Bgee; ENSMUSG00000036777; Expressed in cerebellar nuclear complex and 223 other tissues.
DR ExpressionAtlas; Q8K298; baseline and differential.
DR Genevisible; Q8K298; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005826; C:actomyosin contractile ring; ISO:MGI.
DR GO; GO:0032059; C:bleb; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0090521; P:podocyte cell migration; ISS:UniProtKB.
DR GO; GO:1904172; P:positive regulation of bleb assembly; ISS:UniProtKB.
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 Acetylation; Actin-binding; Cell cycle; Cell division; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1121
FT /note="Anillin"
FT /id="PRO_0000227966"
FT DOMAIN 980..1104
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..228
FT /note="Nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 1..154
FT /note="Interaction with CD2AP"
FT /evidence="ECO:0000250"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..45
FT /note="Required for ubiquitination"
FT /evidence="ECO:0000250"
FT REGION 125..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..671
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 490..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..1121
FT /note="Localization to the cleavage furrow"
FT /evidence="ECO:0000250"
FT COILED 564..599
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 359
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 366
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQW6"
FT CONFLICT 366
FT /note="K -> N (in Ref. 1; AAH32164)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="G -> S (in Ref. 2; BAC32464)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1121 AA; 122794 MW; 0D23488D3264E525 CRC64;
MDPFTEKLLE RTRARRENLQ RKMAERPTAV ARSAPHAKRG REPLSEASNQ QQPLPGGEEK
SCTKPSPSKK RCSDKIEVGA PDLENTEPID VAKPCSPMPA PRQAKPPAPA AISESVAAPA
ALLSADRGLN SGSEASATSS VKTRMQRLAE QRRHWDSDLT DDVSESSYFA PVPTEDKAAS
PSKPPISNAS ATPVGRRGRL ANLAATICSW EDDVSHSSAK QNSVQEQPGT ACLSKSSSAS
GASASINSSS VQQEATCCSP RDGNASVRKD PSSNAAHGPL LSASVSSSVK ASSPVTAATF
ITENREAQNP ELLHKTASPL KTEARKPCEK PTLSQGAQPK EEANREVCLQ SQSKDKLATP
GGRGIKPFLE RFGERCQEHS KESPSYRASH KTPNITPNTK AIQERLFKQN TCSSTTHLAQ
QLKQEREKEL ACLRGRLDKG NLWSAEKNEK SRSKHLETKQ EVHCQNTPLK KHQTVASTPL
TSVTDKVAEN EPAVKLSSTE PAGSTESEMT KSSPLKITLF LEEEKSLKVA SDLEVEQNTE
AVREVEMSVD DEDINSSRVI NDIFSDVLEE GELDVEKSQE EMDQVGAENS EEQEDALNIS
SMSLLAPLAQ TVGVVSLENV ISSPPSELRD SNLSAASPKP GKFQRTRVPR AESADSLGSE
DRDLLYSIDA YRSQRFKETE RPSIKQVIVR KEDVTSKLGE KKNVFSGQVN IKQKMQELNN
DINLQQTVIY QASQALNCCV DEEHGKGSLE EAEAERLLLI ATEKRALLID ELNKLKSEGP
QRRNKTSVIS QSEFAPSKGS VTLSEICLPL KADFVCSTAQ KTDASNYYYL IMLKAGAEQM
VATPLASTAN SLSGDALTFP TTFTLHDVSN DFEINIEVYS LVQKKDSLGP DKKKKASKSK
AITPKRLLTS ITSKSSLHSS VMASPGGLGA VRTSNFTLVG SHTLSLSSVG DTKFALDKVP
FLSPLEGHIC LKISCQVNSA VEEKGFLTIF EDVSGFGAWH RRWCVLSGNC ISYWTYPDDE
RRKNPIGRIN LANCISHQIE PANREFCARR NTLELITVRP QREDDRETLV SQCRDTLCVT
KNWLSADTKE ERDLWMQKLN QVIVDIRLWQ PDACYKPVGK P
