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Q9NQW6

- ANLN_HUMAN

UniProt

Q9NQW6 - ANLN_HUMAN

Protein

Actin-binding protein anillin

Gene

ANLN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (21 Mar 2006)
      Previous versions | rss
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    Functioni

    Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression.5 Publications

    GO - Molecular functioni

    1. actin binding Source: MGI

    GO - Biological processi

    1. mitotic cytokinesis Source: MGI
    2. mitotic nuclear division Source: UniProtKB-KW
    3. regulation of exit from mitosis Source: ProtInc
    4. septin ring assembly Source: ProtInc

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:14082. ANLN.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeleton. Cytoplasmcell cortex
    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

    1. actin cytoskeleton Source: MGI
    2. actomyosin contractile ring Source: MGI
    3. intracellular membrane-bounded organelle Source: HPA
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 321R → A: Abrogates interaction with CD2AP. 1 Publication
    Mutagenesisi41 – 411R → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-44. 1 Publication
    Mutagenesisi44 – 441L → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-41. 1 Publication

    Organism-specific databases

    PharmGKBiPA24809.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11241124Actin-binding protein anillinPRO_0000227965Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei54 – 541Phosphoserine4 Publications
    Modified residuei72 – 721Phosphoserine1 Publication
    Modified residuei102 – 1021Phosphoserine1 Publication
    Modified residuei172 – 1721Phosphoserine1 Publication
    Modified residuei182 – 1821Phosphoserine1 Publication
    Modified residuei194 – 1941Phosphothreonine1 Publication
    Modified residuei320 – 3201Phosphothreonine1 Publication
    Modified residuei323 – 3231Phosphoserine2 Publications
    Modified residuei364 – 3641Phosphothreonine1 Publication
    Modified residuei371 – 3711N6-acetyllysine1 Publication
    Modified residuei397 – 3971Phosphothreonine1 Publication
    Modified residuei401 – 4011Phosphothreonine2 Publications
    Modified residuei449 – 4491Phosphoserine1 Publication
    Modified residuei485 – 4851Phosphoserine2 Publications
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei553 – 5531Phosphoserine2 Publications
    Modified residuei561 – 5611Phosphoserine1 Publication
    Modified residuei642 – 6421Phosphoserine1 Publication
    Modified residuei658 – 6581Phosphoserine2 Publications
    Modified residuei661 – 6611Phosphoserine3 Publications
    Modified residuei664 – 6641Phosphoserine1 Publication
    Modified residuei792 – 7921Phosphoserine3 Publications
    Modified residuei927 – 9271Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated during mitosis.9 Publications
    Ubiquitinated, and this requires FZR1/CDH1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NQW6.
    PaxDbiQ9NQW6.
    PRIDEiQ9NQW6.

    PTM databases

    PhosphoSiteiQ9NQW6.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Present at highest levels in the brain, at high levels in the placenta and testis, at intermediate levels in the intestine, ovary, skeletal muscle and thymus and at lower levels in heart, kidney, liver, lung, pancreas, prostate and spleen. Overexpressed in many tumor types including breast, colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic tumors.1 Publication

    Developmental stagei

    Expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen and thymus. In dividing cells expression increases during S and G2 phases, peaks at mitosis and subsequently drops as cells enter G1 phase.4 Publications

    Gene expression databases

    ArrayExpressiQ9NQW6.
    BgeeiQ9NQW6.
    CleanExiHS_ANLN.
    GenevestigatoriQ9NQW6.

    Organism-specific databases

    HPAiCAB062547.
    HPA005680.
    HPA050556.

    Interactioni

    Subunit structurei

    Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit.4 Publications

    Protein-protein interaction databases

    BioGridi119959. 8 interactions.
    IntActiQ9NQW6. 4 interactions.
    MINTiMINT-3072308.
    STRINGi9606.ENSP00000265748.

    Structurei

    Secondary structure

    1
    1124
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi986 – 99611
    Beta strandi999 – 101012
    Beta strandi1013 – 10197
    Helixi1020 – 10234
    Beta strandi1029 – 10335
    Helixi1034 – 10363
    Beta strandi1039 – 10413
    Turni1047 – 10493
    Beta strandi1055 – 10639
    Beta strandi1072 – 10776
    Beta strandi1080 – 10889
    Helixi1092 – 111019

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y7BX-ray1.90A980-1113[»]
    ProteinModelPortaliQ9NQW6.
    SMRiQ9NQW6. Positions 980-1113.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini983 – 1107125PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 230230Nuclear localizationAdd
    BLAST
    Regioni1 – 155155Interaction with CD2APAdd
    BLAST
    Regioni1 – 4545Required for ubiquitinationAdd
    BLAST
    Regioni231 – 676446Interaction with F-actinAdd
    BLAST
    Regioni730 – 1124395Localization to the cleavage furrowAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili569 – 60436Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 PH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG247921.
    HOGENOMiHOG000033950.
    HOVERGENiHBG059477.
    InParanoidiQ9NQW6.
    OMAiFCARPNT.
    OrthoDBiEOG7VHSZ0.
    PhylomeDBiQ9NQW6.
    TreeFamiTF106494.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR012966. DUF1709.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF08174. Anillin. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQW6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ     50
    QPLSGGEEKS CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP 100
    VSPQVQPQAA DTISDSVAVP ASLLGMRRGL NSRLEATAAS SVKTRMQKLA 150
    EQRRRWDNDD MTDDIPESSL FSPMPSEEKA ASPPRPLLSN ASATPVGRRG 200
    RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS ASGASARINS 250
    SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST 300
    TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR 350
    EICLQSQSKD KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII 400
    TPNTKAIQER LFKQDTSSST THLAQQLKQE RQKELACLRG RFDKGNIWSA 450
    EKGGNSKSKQ LETKQETHCQ STPLKKHQGV SKTQSLPVTE KVTENQIPAK 500
    NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV EQKIEVIREI 550
    EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED 600
    ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR 650
    TRVPRAESGD SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT 700
    SKLDEKNNAF PCQVNIKQKM QELNNEINMQ QTVIYQASQA LNCCVDEEHG 750
    KGSLEEAEAE RLLLIATGKR TLLIDELNKL KNEGPQRKNK ASPQSEFMPS 800
    KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA ENMVATPLAS 850
    TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS 900
    KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS 950
    SVGNTKFVLD KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG 1000
    AWHRRWCVLS GNCISYWTYP DDEKRKNPIG RINLANCTSR QIEPANREFC 1050
    ARRNTFELIT VRPQREDDRE TLVSQCRDTL CVTKNWLSAD TKEERDLWMQ 1100
    KLNQVLVDIR LWQPDACYKP IGKP 1124
    Length:1,124
    Mass (Da):124,199
    Last modified:March 21, 2006 - v2
    Checksum:i79A8CC25C950DB2D
    GO
    Isoform 2 (identifier: Q9NQW6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         508-544: Missing.

    Show »
    Length:1,087
    Mass (Da):120,016
    Checksum:i5B45A0FFA334747F
    GO

    Sequence cautioni

    The sequence AAH34692.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91710.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91711.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531L → F in AAF75796. (PubMed:10931866)Curated
    Sequence conflicti62 – 621T → S in AAF75796. (PubMed:10931866)Curated
    Sequence conflicti294 – 2941T → TS(PubMed:10931866)Curated
    Sequence conflicti294 – 2941T → TS(PubMed:17974005)Curated
    Sequence conflicti410 – 4101R → K in AAH70066. (PubMed:15489334)Curated
    Sequence conflicti625 – 6251L → S in BAA91711. (PubMed:14702039)Curated
    Sequence conflicti1035 – 10351A → V in CAI56788. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti65 – 651S → W.
    Corresponds to variant rs3735400 [ dbSNP | Ensembl ].
    VAR_025661
    Natural varianti185 – 1851R → K.2 Publications
    Corresponds to variant rs197367 [ dbSNP | Ensembl ].
    VAR_025662

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei508 – 54437Missing in isoform 2. 2 PublicationsVSP_017617Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF273437 mRNA. Translation: AAF75796.1.
    BC034692 mRNA. Translation: AAH34692.1. Different initiation.
    BC070066 mRNA. Translation: AAH70066.1.
    CR936650 mRNA. Translation: CAI56788.1.
    AK001468 mRNA. Translation: BAA91710.1. Different initiation.
    AK001472 mRNA. Translation: BAA91711.1. Different initiation.
    AK023208 mRNA. Translation: BAB14463.1.
    CCDSiCCDS5447.1. [Q9NQW6-1]
    CCDS64628.1. [Q9NQW6-2]
    RefSeqiNP_001271230.1. NM_001284301.1. [Q9NQW6-2]
    NP_001271231.1. NM_001284302.1.
    NP_061155.2. NM_018685.3. [Q9NQW6-1]
    UniGeneiHs.62180.

    Genome annotation databases

    EnsembliENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
    ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
    GeneIDi54443.
    KEGGihsa:54443.
    UCSCiuc003tff.3. human. [Q9NQW6-1]
    uc003tfg.3. human. [Q9NQW6-2]

    Polymorphism databases

    DMDMi90111962.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF273437 mRNA. Translation: AAF75796.1 .
    BC034692 mRNA. Translation: AAH34692.1 . Different initiation.
    BC070066 mRNA. Translation: AAH70066.1 .
    CR936650 mRNA. Translation: CAI56788.1 .
    AK001468 mRNA. Translation: BAA91710.1 . Different initiation.
    AK001472 mRNA. Translation: BAA91711.1 . Different initiation.
    AK023208 mRNA. Translation: BAB14463.1 .
    CCDSi CCDS5447.1. [Q9NQW6-1 ]
    CCDS64628.1. [Q9NQW6-2 ]
    RefSeqi NP_001271230.1. NM_001284301.1. [Q9NQW6-2 ]
    NP_001271231.1. NM_001284302.1.
    NP_061155.2. NM_018685.3. [Q9NQW6-1 ]
    UniGenei Hs.62180.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y7B X-ray 1.90 A 980-1113 [» ]
    ProteinModelPortali Q9NQW6.
    SMRi Q9NQW6. Positions 980-1113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119959. 8 interactions.
    IntActi Q9NQW6. 4 interactions.
    MINTi MINT-3072308.
    STRINGi 9606.ENSP00000265748.

    PTM databases

    PhosphoSitei Q9NQW6.

    Polymorphism databases

    DMDMi 90111962.

    Proteomic databases

    MaxQBi Q9NQW6.
    PaxDbi Q9NQW6.
    PRIDEi Q9NQW6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265748 ; ENSP00000265748 ; ENSG00000011426 . [Q9NQW6-1 ]
    ENST00000396068 ; ENSP00000379380 ; ENSG00000011426 . [Q9NQW6-2 ]
    GeneIDi 54443.
    KEGGi hsa:54443.
    UCSCi uc003tff.3. human. [Q9NQW6-1 ]
    uc003tfg.3. human. [Q9NQW6-2 ]

    Organism-specific databases

    CTDi 54443.
    GeneCardsi GC07P036395.
    H-InvDB HIX0006603.
    HGNCi HGNC:14082. ANLN.
    HPAi CAB062547.
    HPA005680.
    HPA050556.
    neXtProti NX_Q9NQW6.
    PharmGKBi PA24809.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247921.
    HOGENOMi HOG000033950.
    HOVERGENi HBG059477.
    InParanoidi Q9NQW6.
    OMAi FCARPNT.
    OrthoDBi EOG7VHSZ0.
    PhylomeDBi Q9NQW6.
    TreeFami TF106494.

    Miscellaneous databases

    GeneWikii ANLN.
    GenomeRNAii 54443.
    NextBioi 56677.
    PROi Q9NQW6.

    Gene expression databases

    ArrayExpressi Q9NQW6.
    Bgeei Q9NQW6.
    CleanExi HS_ANLN.
    Genevestigatori Q9NQW6.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR012966. DUF1709.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF08174. Anillin. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Functional analysis of a human homolog of the Drosophila actin binding protein anillin suggests a role in cytokinesis."
      Oegema K., Savoian M.S., Mitchison T.J., Field C.M.
      J. Cell Biol. 150:539-552(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-185, FUNCTION, INTERACTION WITH ACTIN, SUBCELLULAR LOCATION.
    2. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 696-1124 (ISOFORMS 1/2).
      Tissue: Squamous cell carcinoma and Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1124 (ISOFORM 1).
      Tissue: Liver.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-1124 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 580-1124 (ISOFORMS 1/2).
      Tissue: Teratocarcinoma.
    5. "Self- and actin-templated assembly of mammalian septins."
      Kinoshita M., Field C.M., Coughlin M.L., Straight A.F., Mitchison T.J.
      Dev. Cell 3:791-802(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor."
      Straight A.F., Cheung A., Limouze J., Chen I., Westwood N.J., Sellers J.R., Mitchison T.J.
      Science 299:1743-1747(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "ANLN plays a critical role in human lung carcinogenesis through the activation of RHOA and by involvement in the phosphoinositide 3-kinase/AKT pathway."
      Suzuki C., Daigo Y., Ishikawa N., Kato T., Hayama S., Ito T., Tsuchiya E., Nakamura Y.
      Cancer Res. 65:11314-11325(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, OVEREXPRESSION IN LUNG CANCER, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
    8. "The septin-binding protein anillin is overexpressed in diverse human tumors."
      Hall P.A., Todd C.B., Hyland P.L., McDade S.S., Grabsch H., Dattani M., Hillan K.J., Russell S.E.H.
      Clin. Cancer Res. 11:6780-6786(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, OVEREXPRESSION IN CANCERS.
    9. "Anillin is a substrate of anaphase-promoting complex/cyclosome (APC/C) that controls spatial contractility of myosin during late cytokinesis."
      Zhao W.-M., Fang G.
      J. Biol. Chem. 280:33516-33524(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FZR1, DEVELOPMENTAL STAGE, UBIQUITINATION, MUTAGENESIS OF ARG-41 AND LEU-44.
    10. "Anillin binds nonmuscle myosin II and regulates the contractile ring."
      Straight A.F., Field C.M., Mitchison T.J.
      Mol. Biol. Cell 16:193-201(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Ablation of PRC1 by small interfering RNA demonstrates that cytokinetic abscission requires a central spindle bundle in mammalian cells, whereas completion of furrowing does not."
      Mollinari C., Kleman J.-P., Saoudi Y., Jablonski S.A., Perard J., Yen T.J., Margolis R.L.
      Mol. Biol. Cell 16:1043-1055(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. Cited for: INTERACTION WITH CD2AP, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, MUTAGENESIS OF ARG-32.
    13. "MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis."
      Zhao W.-M., Fang G.
      Proc. Natl. Acad. Sci. U.S.A. 102:13158-13163(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; THR-194 AND THR-401, VARIANT [LARGE SCALE ANALYSIS] LYS-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-72; SER-102; SER-172; THR-320; SER-323; THR-364; THR-397; THR-401; SER-485; SER-518; SER-553; SER-658; SER-661; SER-664; SER-792 AND SER-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-449; SER-553; SER-561; SER-642; SER-658; SER-661; SER-792 AND SER-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-485 AND SER-792, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiANLN_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQW6
    Secondary accession number(s): Q5CZ78
    , Q6NSK5, Q9H8Y4, Q9NVN9, Q9NVP0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3