Q9NQW6 (ANLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin-binding protein anillin

Gene names

Name:

ANLN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1124 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton. Cytoplasm › cell 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from direct assay Ref.1. Source: MGI mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of exit from mitosis Traceable author statement Ref.1. Source: ProtInc septin ring assembly Traceable author statement Ref.1. Source: ProtInc
Cellular_component	actomyosin contractile ring Inferred from direct assay Ref.1. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin binding Inferred from direct assay Ref.1. Source: MGI phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1124

1124

Actin-binding protein anillin

PRO_0000227965

Regions

Domain

983 – 1107

125

PH

Region

1 – 230

230

Nuclear localization

Region

1 – 155

155

Interaction with CD2AP

Region

1 – 45

45

Required for ubiquitination

Region

231 – 676

446

Interaction with F-actin

Region

730 – 1124

395

Localization to the cleavage furrow

Coiled coil

569 – 604

36

Potential

Amino acid modifications

Modified residue

54

1

Phosphoserine Ref.17 Ref.18 Ref.20 Ref.22

Modified residue

72

1

Phosphoserine Ref.17

Modified residue

102

1

Phosphoserine Ref.17

Modified residue

172

1

Phosphoserine Ref.17

Modified residue

182

1

Phosphoserine Ref.14

Modified residue

194

1

Phosphothreonine Ref.14

Modified residue

320

1

Phosphothreonine Ref.17 Ref.20

Modified residue

323

1

Phosphoserine Ref.17 Ref.18 Ref.20 Ref.22

Modified residue

364

1

Phosphothreonine Ref.17

Modified residue

371

1

N6-acetyllysine Ref.19

Modified residue

397

1

Phosphothreonine Ref.17

Modified residue

401

1

Phosphothreonine Ref.14 Ref.17

Modified residue

449

1

Phosphoserine Ref.20

Modified residue

485

1

Phosphoserine Ref.17 Ref.22

Modified residue

515

1

Phosphothreonine By similarity

Modified residue

518

1

Phosphoserine Ref.17

Modified residue

553

1

Phosphoserine Ref.17 Ref.20

Modified residue

561

1

Phosphoserine Ref.20

Modified residue

642

1

Phosphoserine Ref.20

Modified residue

658

1

Phosphoserine Ref.17 Ref.20

Modified residue

661

1

Phosphoserine Ref.16 Ref.17 Ref.20

Modified residue

664

1

Phosphoserine Ref.17

Modified residue

792

1

Phosphoserine Ref.17 Ref.20 Ref.22

Modified residue

927

1

Phosphoserine Ref.15 Ref.17 Ref.20

Natural variations

Alternative sequence

508 – 544

37

Missing in isoform 2.

VSP_017617

Natural variant

65

1

S → W.
Corresponds to variant rs3735400 [ dbSNP | Ensembl ].

VAR_025661

Natural variant

185

1

R → K. Ref.1 Ref.14
Corresponds to variant rs197367 [ dbSNP | Ensembl ].

VAR_025662

Experimental info

Mutagenesis

32

1

R → A: Abrogates interaction with CD2AP. Ref.12

Mutagenesis

41

1

R → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-44. Ref.9

Mutagenesis

44

1

L → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-41. Ref.9

Sequence conflict

53

1

L → F in AAF75796. Ref.1

Sequence conflict

62

1

T → S in AAF75796. Ref.1

Sequence conflict

294

1

T → TS Ref.1

Sequence conflict

294

1

T → TS Ref.3

Sequence conflict

410

1

R → K in AAH70066. Ref.2

Sequence conflict

625

1

L → S in BAA91711. Ref.4

Sequence conflict

1035

1

A → V in CAI56788. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1124

Helix Strand Turn

Details...

Beta strand

986 – 996

11

Beta strand

999 – 1010

12

Beta strand

1013 – 1019

7

Helix

1020 – 1023

4

Beta strand

1029 – 1033

5

Helix

1034 – 1036

3

Beta strand

1039 – 1041

3

Turn

1047 – 1049

3

Beta strand

1055 – 1063

9

Beta strand

1072 – 1077

6

Beta strand

1080 – 1088

9

Helix

1092 – 1110

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 21, 2006. Version 2. Checksum: 79A8CC25C950DB2D	FASTA	1,124	124,199
	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
	Isoform 2 [UniParc]. Checksum: 5B45A0FFA334747F	FASTA	1,087	120,016
	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 NSSTEPKEVI REIEMSVDDD DINSSKVIND LFSDVLEEGE 550 560 570 580 590 600 LDMEKSQEEM DQALAESSEE QEDALNISSM SLLAPLAQTV GVVSPESLVS TPRLELKDTS 610 620 630 640 650 660 RSDESPKPGK FQRTRVPRAE SGDSLGSEDR DLLYSIDAYR SQRFKETERP SIKQVIVRKE 670 680 690 700 710 720 DVTSKLDEKN NAFPCQVNIK QKMQELNNEI NMQQTVIYQA SQALNCCVDE EHGKGSLEEA 730 740 750 760 770 780 EAERLLLIAT GKRTLLIDEL NKLKNEGPQR KNKASPQSEF MPSKGSVTLS EIRLPLKADF 790 800 810 820 830 840 VCSTVQKPDA ANYYYLIILK AGAENMVATP LASTSNSLNG DALTFTTTFT LQDVSNDFEI 850 860 870 880 890 900 NIEVYSLVQK KDPSGLDKKK KTSKSKAITP KRLLTSITTK SNIHSSVMAS PGGLSAVRTS 910 920 930 940 950 960 NFALVGSYTL SLSSVGNTKF VLDKVPFLSS LEGHIYLKIK CQVNSSVEER GFLTIFEDVS 970 980 990 1000 1010 1020 GFGAWHRRWC VLSGNCISYW TYPDDEKRKN PIGRINLANC TSRQIEPANR EFCARRNTFE 1030 1040 1050 1060 1070 1080 LITVRPQRED DRETLVSQCR DTLCVTKNWL SADTKEERDL WMQKLNQVLV DIRLWQPDAC YKPIGKP

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY.
[20]	"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; THR-320; SER-323; SER-449; SER-553; SER-561; SER-642; SER-658; SER-661; SER-792 AND SER-927, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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-323; SER-485 AND SER-792, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00032958.
IPI00743594.

RefSeq

NP_061155.2. NM_018685.2.

UniGene

Hs.62180.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Y7B	X-ray	1.90	A	980-1113	[»]

ProteinModelPortal

Q9NQW6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NQW6. 2 interactions.

STRING

9606.ENSP00000265748.

PTM databases

PhosphoSite

Q9NQW6.

Polymorphism databases

DMDM

90111962.

Proteomic databases

PaxDb

Q9NQW6.

PRIDE

Q9NQW6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265748; ENSP00000265748; ENSG00000011426.
ENST00000396068; ENSP00000379380; ENSG00000011426.

GeneID

54443.

KEGG

hsa:54443.

UCSC

uc003tff.3. human.
uc003tfg.3. human.

Organism-specific databases

CTD

54443.

GeneCards

GC07P036395.

H-InvDB

HIX0006603.

HGNC

HGNC:14082. ANLN.

neXtProt

NX_Q9NQW6.

PharmGKB

PA24809.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG247921.

HOGENOM

HOG000033950.

HOVERGEN

HBG059477.

InParanoid

Q9NQW6.

OMA

HSKESPA.

OrthoDB

EOG41ZF92.

PhylomeDB

Q9NQW6.

Gene expression databases

ArrayExpress

Q9NQW6.

Bgee

Q9NQW6.

CleanEx

HS_ANLN.

Genevestigator

Q9NQW6.

GermOnline

ENSG00000011426. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR012966. DUF1709.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF08174. Anillin. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

SMART

SM00233. PH. 1 hit.
[Graphical view]

PROSITE

PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

54443.

NextBio

56677.

Entry information

Entry name

ANLN_HUMAN

Accession

Primary (citable) accession number: Q9NQW6
Secondary accession number(s): Q5CZ78 , Q6NSK5, Q9H8Y4, Q9NVN9, Q9NVP0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.