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Protein

Actin-binding protein anillin

Gene

ANLN

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

Functioni

Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. May play a significant role in podocyte cell migration (PubMed:24676636).6 Publications

GO - Molecular functioni

  • actin binding Source: MGI

GO - Biological processi

  • glomerular visceral epithelial cell migration Source: UniProtKB
  • hematopoietic progenitor cell differentiation Source: Ensembl
  • mitotic cytokinesis Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • regulation of exit from mitosis Source: ProtInc
  • 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
Proteomesi
  • UP000005640 Componenti: 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

  • actin cytoskeleton Source: MGI
  • actomyosin contractile ring Source: MGI
  • intracellular membrane-bounded organelle Source: HPA
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 8 (FSGS8)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
See also OMIM:616032
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti431 – 4311R → C in FSGS8; results in decreased interaction with CD2AP. 1 Publication
Corresponds to variant rs587777741 [ dbSNP | Ensembl ].
VAR_072418
Natural varianti618 – 6181G → C in FSGS8. 1 Publication
VAR_072419

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiANLN.
MIMi616032. phenotype.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA24809.

Polymorphism and mutation databases

BioMutaiANLN.
DMDMi90111962.

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-acetylmethionineCombined sources
Modified residuei54 – 541PhosphoserineCombined sources
Modified residuei72 – 721PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei182 – 1821Phosphoserine; in variant Lys-185Combined sources
Modified residuei194 – 1941Phosphothreonine; in variant Lys-185Combined sources
Modified residuei225 – 2251PhosphoserineCombined sources
Modified residuei252 – 2521PhosphoserineCombined sources
Cross-linki254 – 254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei261 – 2611PhosphoserineBy similarity
Modified residuei320 – 3201PhosphothreonineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei364 – 3641PhosphothreonineCombined sources
Modified residuei371 – 3711N6-acetyllysineCombined sources
Modified residuei397 – 3971PhosphothreonineCombined sources
Modified residuei401 – 4011PhosphothreonineCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei419 – 4191PhosphoserineCombined sources
Modified residuei449 – 4491PhosphoserineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei518 – 5181PhosphoserineCombined sources
Modified residuei553 – 5531PhosphoserineCombined sources
Modified residuei561 – 5611PhosphoserineCombined sources
Modified residuei637 – 6371PhosphoserineCombined sources
Modified residuei642 – 6421PhosphoserineCombined sources
Modified residuei658 – 6581PhosphoserineCombined sources
Modified residuei661 – 6611PhosphoserineCombined sources
Modified residuei664 – 6641PhosphoserineCombined sources
Modified residuei671 – 6711PhosphotyrosineBy similarity
Modified residuei678 – 6781PhosphoserineCombined sources
Modified residuei688 – 6881PhosphoserineCombined sources
Modified residuei792 – 7921PhosphoserineCombined sources
Modified residuei927 – 9271PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis.2 Publications
Ubiquitinated, and this requires FZR1/CDH1.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9NQW6.
MaxQBiQ9NQW6.
PaxDbiQ9NQW6.
PeptideAtlasiQ9NQW6.
PRIDEiQ9NQW6.

PTM databases

iPTMnetiQ9NQW6.
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. In the kidney, it is widely expressed in tubules, but sparsely expressed in the glomerulus (PubMed:24676636). Expression is significantly increased in renal biopsy specimens from idiopathic FSGS (PubMed:24676636). Overexpressed in many tumor types including breast, colorectal, endometrial, hepatic, kidney, lung, ovarian and pancreatic tumors.2 Publications

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.
GenevisibleiQ9NQW6. HS.

Organism-specific databases

HPAiCAB033902.
CAB062547.
CAB068175.
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

Binary interactionsi

WithEntry#Exp.IntActNotes
MARCH10Q8NA823EBI-10312488,EBI-2341554

GO - Molecular functioni

  • actin binding Source: MGI

Protein-protein interaction databases

BioGridi119959. 144 interactions.
IntActiQ9NQW6. 141 interactions.
MINTiMINT-3072308.
STRINGi9606.ENSP00000265748.

Structurei

Secondary structure

1
1124
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi716 – 74227Combined sources
Helixi747 – 7493Combined sources
Turni750 – 7523Combined sources
Helixi754 – 78128Combined sources
Beta strandi802 – 81312Combined sources
Helixi815 – 8239Combined sources
Beta strandi827 – 84519Combined sources
Turni851 – 8533Combined sources
Beta strandi854 – 8563Combined sources
Beta strandi859 – 8613Combined sources
Beta strandi866 – 8716Combined sources
Beta strandi877 – 88711Combined sources
Beta strandi940 – 9478Combined sources
Helixi949 – 9513Combined sources
Beta strandi956 – 9583Combined sources
Beta strandi970 – 97910Combined sources
Beta strandi986 – 99611Combined sources
Beta strandi999 – 101012Combined sources
Beta strandi1013 – 10197Combined sources
Helixi1020 – 10234Combined sources
Beta strandi1029 – 10335Combined sources
Helixi1034 – 10363Combined sources
Beta strandi1039 – 10413Combined sources
Turni1047 – 10493Combined sources
Beta strandi1055 – 10639Combined sources
Beta strandi1072 – 10776Combined sources
Beta strandi1080 – 10889Combined sources
Helixi1092 – 111019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y7BX-ray1.90A980-1113[»]
4XH3X-ray2.10A712-1124[»]
4XOIX-ray2.09B/D712-981[»]
ProteinModelPortaliQ9NQW6.
SMRiQ9NQW6. Positions 714-1113.
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

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ9NQW6.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG7VHSZ0.
PhylomeDBiQ9NQW6.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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

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.Combined sources1 Publication
Corresponds to variant rs197367 [ dbSNP | Ensembl ].
VAR_025662
Natural varianti431 – 4311R → C in FSGS8; results in decreased interaction with CD2AP. 1 Publication
Corresponds to variant rs587777741 [ dbSNP | Ensembl ].
VAR_072418
Natural varianti618 – 6181G → C in FSGS8. 1 Publication
VAR_072419

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001284301.2. [Q9NQW6-2]
NP_001271231.1. NM_001284302.2.
NP_061155.2. NM_018685.4. [Q9NQW6-1]
UniGeneiHs.62180.

Genome annotation databases

EnsembliENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
GeneIDi54443.
KEGGihsa:54443.
UCSCiuc003tff.4. human. [Q9NQW6-1]

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:
EMBLi
GenBanki
DDBJi
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_001284301.2. [Q9NQW6-2]
NP_001271231.1. NM_001284302.2.
NP_061155.2. NM_018685.4. [Q9NQW6-1]
UniGeneiHs.62180.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y7BX-ray1.90A980-1113[»]
4XH3X-ray2.10A712-1124[»]
4XOIX-ray2.09B/D712-981[»]
ProteinModelPortaliQ9NQW6.
SMRiQ9NQW6. Positions 714-1113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119959. 144 interactions.
IntActiQ9NQW6. 141 interactions.
MINTiMINT-3072308.
STRINGi9606.ENSP00000265748.

PTM databases

iPTMnetiQ9NQW6.
PhosphoSiteiQ9NQW6.

Polymorphism and mutation databases

BioMutaiANLN.
DMDMi90111962.

Proteomic databases

EPDiQ9NQW6.
MaxQBiQ9NQW6.
PaxDbiQ9NQW6.
PeptideAtlasiQ9NQW6.
PRIDEiQ9NQW6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
GeneIDi54443.
KEGGihsa:54443.
UCSCiuc003tff.4. human. [Q9NQW6-1]

Organism-specific databases

CTDi54443.
GeneCardsiANLN.
H-InvDBHIX0006603.
HGNCiHGNC:14082. ANLN.
HPAiCAB033902.
CAB062547.
CAB068175.
HPA005680.
HPA050556.
MalaCardsiANLN.
MIMi616027. gene.
616032. phenotype.
neXtProtiNX_Q9NQW6.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA24809.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3640. Eukaryota.
ENOG4110J5Z. LUCA.
GeneTreeiENSGT00390000008749.
HOGENOMiHOG000033950.
HOVERGENiHBG059477.
InParanoidiQ9NQW6.
KOiK18621.
OMAiHSKESPA.
OrthoDBiEOG7VHSZ0.
PhylomeDBiQ9NQW6.
TreeFamiTF106494.

Miscellaneous databases

ChiTaRSiANLN. human.
GeneWikiiANLN.
GenomeRNAii54443.
PROiQ9NQW6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQW6.
CleanExiHS_ANLN.
ExpressionAtlasiQ9NQW6. baseline and differential.
GenevisibleiQ9NQW6. HS.

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

« 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 THR-401, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND THR-194 (VARIANT LYS-185), 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-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].
  25. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-225; SER-252; SER-339; THR-364; THR-401; SER-417; SER-419; SER-485; SER-518; SER-637; SER-642; SER-658; SER-661; SER-678; SER-688; SER-792 AND SER-927, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  26. Cited for: FUNCTION, INVOLVEMENT IN FSGS8, TISSUE SPECIFICITY, VARIANTS FSGS8 CYS-431 AND CYS-618, CHARACTERIZATION OF VARIANT FSGS8 CYS-431.
  27. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-254, 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: July 6, 2016
This is version 125 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.