Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Actin-binding protein anillin

Gene

Anln

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Required for cytokinesis (By similarity). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression (By similarity). May play a significant role in podocyte cell migration (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-binding protein anillin
Gene namesi
Name:Anln
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1920174. Anln.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasmcytoskeleton By similarity
  • Cytoplasmcell cortex By similarity

  • Note: Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contractile ring in anaphase. This pattern persists until telophase, when the protein becomes concentrated in the midbody.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11211121Actin-binding protein anillinPRO_0000227966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei73 – 731PhosphoserineCombined sources
Modified residuei96 – 961PhosphoserineCombined sources
Modified residuei180 – 1801PhosphoserineCombined sources
Modified residuei192 – 1921PhosphothreonineCombined sources
Modified residuei223 – 2231PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity
Modified residuei259 – 2591PhosphoserineCombined sources
Modified residuei316 – 3161PhosphothreonineBy similarity
Modified residuei318 – 3181PhosphoserineBy similarity
Modified residuei334 – 3341PhosphoserineBy similarity
Modified residuei359 – 3591PhosphothreonineBy similarity
Modified residuei366 – 3661N6-acetyllysineBy similarity
Modified residuei392 – 3921PhosphothreonineBy similarity
Modified residuei396 – 3961PhosphothreonineBy similarity
Modified residuei414 – 4141PhosphoserineBy similarity
Modified residuei444 – 4441PhosphoserineBy similarity
Modified residuei513 – 5131PhosphoserineBy similarity
Modified residuei548 – 5481PhosphoserineCombined sources
Modified residuei556 – 5561PhosphoserineBy similarity
Modified residuei637 – 6371PhosphoserineCombined sources
Modified residuei653 – 6531PhosphoserineCombined sources
Modified residuei656 – 6561PhosphoserineCombined sources
Modified residuei659 – 6591PhosphoserineCombined sources
Modified residuei666 – 6661PhosphotyrosineCombined sources
Modified residuei673 – 6731PhosphoserineBy similarity
Modified residuei683 – 6831PhosphoserineBy similarity
Modified residuei787 – 7871PhosphoserineBy similarity
Modified residuei924 – 9241PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated during mitosis.By similarity
Ubiquitinated, and this requires FZR1/CDH1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8K298.
MaxQBiQ8K298.
PaxDbiQ8K298.
PeptideAtlasiQ8K298.
PRIDEiQ8K298.

PTM databases

iPTMnetiQ8K298.
PhosphoSiteiQ8K298.

Expressioni

Gene expression databases

BgeeiQ8K298.
GenevisibleiQ8K298. MM.

Interactioni

Subunit structurei

Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213029. 2 interactions.
IntActiQ8K298. 1 interaction.
STRINGi10090.ENSMUSP00000045873.

Structurei

3D structure databases

ProteinModelPortaliQ8K298.
SMRiQ8K298. Positions 709-1110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini980 – 1104125PHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 228228Nuclear localizationBy similarityAdd
BLAST
Regioni1 – 154154Interaction with CD2APBy similarityAdd
BLAST
Regioni1 – 4545Required for ubiquitinationBy similarityAdd
BLAST
Regioni229 – 671443Interaction with F-actinBy similarityAdd
BLAST
Regioni725 – 1121397Localization to the cleavage furrowBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili564 – 59936Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 PH domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ8K298.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG7VHSZ0.
PhylomeDBiQ8K298.
TreeFamiTF106494.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012966. AHD.
IPR031970. Anillin_N.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
PF16018. Anillin_N. 2 hits.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K298-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPFTEKLLE RTRARRENLQ RKMAERPTAV ARSAPHAKRG REPLSEASNQ
60 70 80 90 100
QQPLPGGEEK SCTKPSPSKK RCSDKIEVGA PDLENTEPID VAKPCSPMPA
110 120 130 140 150
PRQAKPPAPA AISESVAAPA ALLSADRGLN SGSEASATSS VKTRMQRLAE
160 170 180 190 200
QRRHWDSDLT DDVSESSYFA PVPTEDKAAS PSKPPISNAS ATPVGRRGRL
210 220 230 240 250
ANLAATICSW EDDVSHSSAK QNSVQEQPGT ACLSKSSSAS GASASINSSS
260 270 280 290 300
VQQEATCCSP RDGNASVRKD PSSNAAHGPL LSASVSSSVK ASSPVTAATF
310 320 330 340 350
ITENREAQNP ELLHKTASPL KTEARKPCEK PTLSQGAQPK EEANREVCLQ
360 370 380 390 400
SQSKDKLATP GGRGIKPFLE RFGERCQEHS KESPSYRASH KTPNITPNTK
410 420 430 440 450
AIQERLFKQN TCSSTTHLAQ QLKQEREKEL ACLRGRLDKG NLWSAEKNEK
460 470 480 490 500
SRSKHLETKQ EVHCQNTPLK KHQTVASTPL TSVTDKVAEN EPAVKLSSTE
510 520 530 540 550
PAGSTESEMT KSSPLKITLF LEEEKSLKVA SDLEVEQNTE AVREVEMSVD
560 570 580 590 600
DEDINSSRVI NDIFSDVLEE GELDVEKSQE EMDQVGAENS EEQEDALNIS
610 620 630 640 650
SMSLLAPLAQ TVGVVSLENV ISSPPSELRD SNLSAASPKP GKFQRTRVPR
660 670 680 690 700
AESADSLGSE DRDLLYSIDA YRSQRFKETE RPSIKQVIVR KEDVTSKLGE
710 720 730 740 750
KKNVFSGQVN IKQKMQELNN DINLQQTVIY QASQALNCCV DEEHGKGSLE
760 770 780 790 800
EAEAERLLLI ATEKRALLID ELNKLKSEGP QRRNKTSVIS QSEFAPSKGS
810 820 830 840 850
VTLSEICLPL KADFVCSTAQ KTDASNYYYL IMLKAGAEQM VATPLASTAN
860 870 880 890 900
SLSGDALTFP TTFTLHDVSN DFEINIEVYS LVQKKDSLGP DKKKKASKSK
910 920 930 940 950
AITPKRLLTS ITSKSSLHSS VMASPGGLGA VRTSNFTLVG SHTLSLSSVG
960 970 980 990 1000
DTKFALDKVP FLSPLEGHIC LKISCQVNSA VEEKGFLTIF EDVSGFGAWH
1010 1020 1030 1040 1050
RRWCVLSGNC ISYWTYPDDE RRKNPIGRIN LANCISHQIE PANREFCARR
1060 1070 1080 1090 1100
NTLELITVRP QREDDRETLV SQCRDTLCVT KNWLSADTKE ERDLWMQKLN
1110 1120
QVIVDIRLWQ PDACYKPVGK P
Length:1,121
Mass (Da):122,794
Last modified:March 21, 2006 - v2
Checksum:i0D23488D3264E525
GO

Sequence cautioni

The sequence AAH30489.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC32605.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661K → N in AAH32164 (PubMed:15489334).Curated
Sequence conflicti613 – 6131G → S in BAC32464 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC030489 mRNA. Translation: AAH30489.1. Different initiation.
BC032164 mRNA. Translation: AAH32164.1.
AK013624 mRNA. Translation: BAB28931.3.
AK045703 mRNA. Translation: BAC32464.1.
AK046102 mRNA. Translation: BAC32605.1. Different initiation.
CCDSiCCDS22927.1.
RefSeqiNP_082666.2. NM_028390.3.
UniGeneiMm.282751.
Mm.453238.

Genome annotation databases

EnsembliENSMUST00000040912; ENSMUSP00000045873; ENSMUSG00000036777.
GeneIDi68743.
KEGGimmu:68743.
UCSCiuc009ook.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC030489 mRNA. Translation: AAH30489.1. Different initiation.
BC032164 mRNA. Translation: AAH32164.1.
AK013624 mRNA. Translation: BAB28931.3.
AK045703 mRNA. Translation: BAC32464.1.
AK046102 mRNA. Translation: BAC32605.1. Different initiation.
CCDSiCCDS22927.1.
RefSeqiNP_082666.2. NM_028390.3.
UniGeneiMm.282751.
Mm.453238.

3D structure databases

ProteinModelPortaliQ8K298.
SMRiQ8K298. Positions 709-1110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213029. 2 interactions.
IntActiQ8K298. 1 interaction.
STRINGi10090.ENSMUSP00000045873.

PTM databases

iPTMnetiQ8K298.
PhosphoSiteiQ8K298.

Proteomic databases

EPDiQ8K298.
MaxQBiQ8K298.
PaxDbiQ8K298.
PeptideAtlasiQ8K298.
PRIDEiQ8K298.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040912; ENSMUSP00000045873; ENSMUSG00000036777.
GeneIDi68743.
KEGGimmu:68743.
UCSCiuc009ook.2. mouse.

Organism-specific databases

CTDi54443.
MGIiMGI:1920174. Anln.

Phylogenomic databases

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ8K298.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG7VHSZ0.
PhylomeDBiQ8K298.
TreeFamiTF106494.

Miscellaneous databases

PROiQ8K298.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K298.
GenevisibleiQ8K298. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR012966. AHD.
IPR031970. Anillin_N.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF08174. Anillin. 1 hit.
PF16018. Anillin_N. 2 hits.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 247-1121.
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Hippocampus.
  3. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-96; SER-180; THR-192; SER-259; SER-548; SER-637; SER-653; SER-656; SER-659 AND TYR-666, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Lung, Spleen and Testis.

Entry informationi

Entry nameiANLN_MOUSE
AccessioniPrimary (citable) accession number: Q8K298
Secondary accession number(s): Q8BL79
, Q8BLB3, Q8K2N0, Q9CUY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 6, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.