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Q9NQW6 (ANLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-binding protein anillin
Gene names
Name:ANLN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1124 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Ref.1 Ref.5 Ref.7 Ref.9 Ref.10

Subunit structure

Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit. Ref.1 Ref.7 Ref.9 Ref.12

Subcellular location

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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13

Tissue specificity

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. Ref.8

Developmental stage

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. Ref.7 Ref.8 Ref.9 Ref.12

Post-translational modification

Phosphorylated during mitosis. Ref.7 Ref.12

Ubiquitinated, and this requires FZR1/CDH1. Ref.9

Sequence similarities

Contains 1 PH domain.

Sequence caution

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.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQW6-1)

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.
Isoform 2 (identifier: Q9NQW6-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11241124Actin-binding protein anillin
PRO_0000227965

Regions

Domain983 – 1107125PH
Region1 – 230230Nuclear localization
Region1 – 155155Interaction with CD2AP
Region1 – 4545Required for ubiquitination
Region231 – 676446Interaction with F-actin
Region730 – 1124395Localization to the cleavage furrow
Coiled coil569 – 60436 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.24
Modified residue541Phosphoserine Ref.17 Ref.19 Ref.21 Ref.23
Modified residue721Phosphoserine Ref.17
Modified residue1021Phosphoserine Ref.17
Modified residue1721Phosphoserine Ref.17
Modified residue1821Phosphoserine Ref.14
Modified residue1941Phosphothreonine Ref.14
Modified residue3201Phosphothreonine Ref.17
Modified residue3231Phosphoserine Ref.17 Ref.19
Modified residue3641Phosphothreonine Ref.17
Modified residue3711N6-acetyllysine Ref.20
Modified residue3971Phosphothreonine Ref.17
Modified residue4011Phosphothreonine Ref.14 Ref.17
Modified residue4491Phosphoserine Ref.21
Modified residue4851Phosphoserine Ref.17 Ref.23
Modified residue5181Phosphoserine Ref.17
Modified residue5531Phosphoserine Ref.17 Ref.21
Modified residue5611Phosphoserine Ref.21
Modified residue6421Phosphoserine Ref.21
Modified residue6581Phosphoserine Ref.17 Ref.21
Modified residue6611Phosphoserine Ref.16 Ref.17 Ref.21
Modified residue6641Phosphoserine Ref.17
Modified residue7921Phosphoserine Ref.17 Ref.21 Ref.23
Modified residue9271Phosphoserine Ref.15 Ref.17 Ref.21

Natural variations

Alternative sequence508 – 54437Missing in isoform 2.
VSP_017617
Natural variant651S → W.
Corresponds to variant rs3735400 [ dbSNP | Ensembl ].
VAR_025661
Natural variant1851R → K. Ref.1 Ref.14
Corresponds to variant rs197367 [ dbSNP | Ensembl ].
VAR_025662

Experimental info

Mutagenesis321R → A: Abrogates interaction with CD2AP. Ref.12
Mutagenesis411R → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-44. Ref.9
Mutagenesis441L → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-41. Ref.9
Sequence conflict531L → F in AAF75796. Ref.1
Sequence conflict621T → S in AAF75796. Ref.1
Sequence conflict2941T → TS Ref.1
Sequence conflict2941T → TS Ref.3
Sequence conflict4101R → K in AAH70066. Ref.2
Sequence conflict6251L → S in BAA91711. Ref.4
Sequence conflict10351A → V in CAI56788. Ref.3

Secondary structure

....................... 1124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 21, 2006. Version 2.
Checksum: 79A8CC25C950DB2D

FASTA1,124124,199
        10         20         30         40         50         60 
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS 

        70         80         90        100        110        120 
CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP 

       130        140        150        160        170        180 
ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA 

       190        200        210        220        230        240 
ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS 

       250        260        270        280        290        300 
ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST 

       310        320        330        340        350        360 
TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD 

       370        380        390        400        410        420 
KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST 

       430        440        450        460        470        480 
THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV 

       490        500        510        520        530        540 
SKTQSLPVTE KVTENQIPAK NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV 

       550        560        570        580        590        600 
EQKIEVIREI EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED 

       610        620        630        640        650        660 
ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR TRVPRAESGD 

       670        680        690        700        710        720 
SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT SKLDEKNNAF PCQVNIKQKM 

       730        740        750        760        770        780 
QELNNEINMQ QTVIYQASQA LNCCVDEEHG KGSLEEAEAE RLLLIATGKR TLLIDELNKL 

       790        800        810        820        830        840 
KNEGPQRKNK ASPQSEFMPS KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA 

       850        860        870        880        890        900 
ENMVATPLAS TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS 

       910        920        930        940        950        960 
KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS SVGNTKFVLD 

       970        980        990       1000       1010       1020 
KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG AWHRRWCVLS GNCISYWTYP 

      1030       1040       1050       1060       1070       1080 
DDEKRKNPIG RINLANCTSR QIEPANREFC ARRNTFELIT VRPQREDDRE TLVSQCRDTL 

      1090       1100       1110       1120 
CVTKNWLSAD TKEERDLWMQ KLNQVLVDIR LWQPDACYKP IGKP 

« Hide

Isoform 2 [UniParc].

Checksum: 5B45A0FFA334747F
Show »

FASTA1,087120,016

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Clues to CD2-associated protein involvement in cytokinesis."
Monzo P., Gauthier N.C., Keslair F., Loubat A., Field C.M., Le Marchand-Brustel Y., Cormont M.
Mol. Biol. Cell 16:2891-2902(2005) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5447.1. [Q9NQW6-1]
CCDS64628.1. [Q9NQW6-2]
RefSeqNP_001271230.1. NM_001284301.1. [Q9NQW6-2]
NP_001271231.1. NM_001284302.1.
NP_061155.2. NM_018685.3. [Q9NQW6-1]
UniGeneHs.62180.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y7BX-ray1.90A980-1113[»]
ProteinModelPortalQ9NQW6.
SMRQ9NQW6. Positions 980-1113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119959. 8 interactions.
IntActQ9NQW6. 4 interactions.
MINTMINT-3072308.
STRING9606.ENSP00000265748.

PTM databases

PhosphoSiteQ9NQW6.

Polymorphism databases

DMDM90111962.

Proteomic databases

MaxQBQ9NQW6.
PaxDbQ9NQW6.
PRIDEQ9NQW6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265748; ENSP00000265748; ENSG00000011426. [Q9NQW6-1]
ENST00000396068; ENSP00000379380; ENSG00000011426. [Q9NQW6-2]
GeneID54443.
KEGGhsa:54443.
UCSCuc003tff.3. human. [Q9NQW6-1]
uc003tfg.3. human. [Q9NQW6-2]

Organism-specific databases

CTD54443.
GeneCardsGC07P036395.
H-InvDBHIX0006603.
HGNCHGNC:14082. ANLN.
HPACAB062547.
HPA005680.
HPA050556.
neXtProtNX_Q9NQW6.
PharmGKBPA24809.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247921.
HOGENOMHOG000033950.
HOVERGENHBG059477.
InParanoidQ9NQW6.
OMAFCARPNT.
OrthoDBEOG7VHSZ0.
PhylomeDBQ9NQW6.
TreeFamTF106494.

Gene expression databases

ArrayExpressQ9NQW6.
BgeeQ9NQW6.
CleanExHS_ANLN.
GenevestigatorQ9NQW6.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR012966. DUF1709.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF08174. Anillin. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00233. PH. 1 hit.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiANLN.
GenomeRNAi54443.
NextBio56677.
PROQ9NQW6.

Entry information

Entry nameANLN_HUMAN
AccessionPrimary (citable) accession number: Q9NQW6
Secondary accession number(s): Q5CZ78 expand/collapse secondary AC list , Q6NSK5, Q9H8Y4, Q9NVN9, Q9NVP0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

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