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Q9NQW6

- ANLN_HUMAN

UniProt

Q9NQW6 - ANLN_HUMAN

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Protein

Actin-binding protein anillin

Gene

ANLN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. hematopoietic progenitor cell differentiation Source: Ensembl
  2. mitotic cytokinesis Source: MGI
  3. mitotic nuclear division Source: UniProtKB-KW
  4. regulation of exit from mitosis Source: ProtInc
  5. septin ring assembly Source: ProtInc
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
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
Complete GO annotation...

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

BgeeiQ9NQW6.
CleanExiHS_ANLN.
ExpressionAtlasiQ9NQW6. baseline and differential.
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.
GeneTreeiENSGT00390000008749.
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) [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

        10         20         30         40         50
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ
60 70 80 90 100
QPLSGGEEKS CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP
110 120 130 140 150
VSPQVQPQAA DTISDSVAVP ASLLGMRRGL NSRLEATAAS SVKTRMQKLA
160 170 180 190 200
EQRRRWDNDD MTDDIPESSL FSPMPSEEKA ASPPRPLLSN ASATPVGRRG
210 220 230 240 250
RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS ASGASARINS
260 270 280 290 300
SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST
310 320 330 340 350
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR
360 370 380 390 400
EICLQSQSKD KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII
410 420 430 440 450
TPNTKAIQER LFKQDTSSST THLAQQLKQE RQKELACLRG RFDKGNIWSA
460 470 480 490 500
EKGGNSKSKQ LETKQETHCQ STPLKKHQGV SKTQSLPVTE KVTENQIPAK
510 520 530 540 550
NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV EQKIEVIREI
560 570 580 590 600
EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED
610 620 630 640 650
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR
660 670 680 690 700
TRVPRAESGD SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT
710 720 730 740 750
SKLDEKNNAF PCQVNIKQKM QELNNEINMQ QTVIYQASQA LNCCVDEEHG
760 770 780 790 800
KGSLEEAEAE RLLLIATGKR TLLIDELNKL KNEGPQRKNK ASPQSEFMPS
810 820 830 840 850
KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA ENMVATPLAS
860 870 880 890 900
TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS
910 920 930 940 950
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS
960 970 980 990 1000
SVGNTKFVLD KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG
1010 1020 1030 1040 1050
AWHRRWCVLS GNCISYWTYP DDEKRKNPIG RINLANCTSR QIEPANREFC
1060 1070 1080 1090 1100
ARRNTFELIT VRPQREDDRE TLVSQCRDTL CVTKNWLSAD TKEERDLWMQ
1110 1120
KLNQVLVDIR LWQPDACYKP IGKP
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.
GeneTreei ENSGT00390000008749.
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

Bgeei Q9NQW6.
CleanExi HS_ANLN.
ExpressionAtlasi Q9NQW6. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 107 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