Reviewed, UniProtKB/Swiss-Prot Q9NQW6 (ANLN_HUMAN)

Names and origin

Protein names

Recommended name:
    Actin-binding protein anillin

Gene names

Name:

ANLN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1124 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.8 Ref.10 Ref.11
Subunit structure	Interacts with F-actin. Interacts with CD2AP. May interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit. Ref.1 Ref.8 Ref.10 Ref.13
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.8 Ref.11 Ref.13 Ref.6 Ref.9 Ref.12 Ref.14
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.9
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.8 Ref.10 Ref.13 Ref.9
Post-translational modification	Phosphorylated during mitosis. Ref.8 Ref.13 Ref.7 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ubiquitinated, and this requires FZR1/CDH1. Ref.10
Sequence similarities	Contains 1 PH domain.

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	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	cytokinesis Ref.1 Inferred from direct assay. Source: MGI mitosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of exit from mitosis Ref.1 Traceable author statement. Source: ProtInc septin ring assembly Ref.1 Traceable author statement. Source: ProtInc
Cellular component	contractile ring Ref.1 Inferred from direct assay. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Ref.1 Inferred from direct assay. Source: MGI
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.19
	Modified residue	72	1	Phosphoserine Ref.19
	Modified residue	97	1	Phosphoserine Ref.18
	Modified residue	99	1	Phosphoserine Ref.7 Ref.19
	Modified residue	102	1	Phosphoserine Ref.18 Ref.19
	Modified residue	172	1	Phosphoserine Ref.19
	Modified residue	182	1	Phosphoserine Ref.17
	Modified residue	194	1	Phosphothreonine Ref.16 Ref.17
	Modified residue	320	1	Phosphothreonine Ref.16 Ref.19
	Modified residue	323	1	Phosphoserine Ref.7 Ref.16 Ref.19
	Modified residue	362	1	Phosphoserine Ref.17
	Modified residue	364	1	Phosphothreonine Ref.19
	Modified residue	368	1	Phosphothreonine Ref.17
	Modified residue	393	1	Phosphothreonine Ref.19
	Modified residue	397	1	Phosphothreonine Ref.19
	Modified residue	401	1	Phosphothreonine Ref.16 Ref.19
	Modified residue	449	1	Phosphoserine Ref.16 Ref.17 Ref.19
	Modified residue	485	1	Phosphoserine Ref.7 Ref.16 Ref.19
	Modified residue	515	1	Phosphothreonine By similarity
	Modified residue	518	1	Phosphoserine Ref.19
	Modified residue	553	1	Phosphoserine Ref.19
	Modified residue	637	1	Phosphoserine Ref.15
	Modified residue	642	1	Phosphoserine By similarity
	Modified residue	658	1	Phosphoserine Ref.19
	Modified residue	661	1	Phosphoserine Ref.18 Ref.19
	Modified residue	664	1	Phosphoserine Ref.19
	Modified residue	792	1	Phosphoserine Ref.19
	Modified residue	927	1	Phosphoserine Ref.17 Ref.19
Natural variations
	Alternative sequence	508 – 544	37	Missing in isoform 2.		VSP_017617
	Natural variant	65	1	S → W: dbSNP rs3735400.		VAR_025661
	Natural variant	185	1	R → K: dbSNP rs197367. Ref.1		VAR_025662
Experimental info
	Mutagenesis	32	1	R → A: Abrogates interaction with CD2AP. Ref.13
	Mutagenesis	41	1	R → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-44. Ref.10
	Mutagenesis	44	1	L → A: Abrogates ubiquitin-mediated proteolysis; when associated with A-41. Ref.10
	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

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. 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: 10931866] [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: 15489334] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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: 14702039] [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: 12479805] [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: 12637748] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-323 AND SER-485, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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: 16357138] [Abstract] Cited for: FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION, OVEREXPRESSION IN LUNG CANCER, DEVELOPMENTAL STAGE, PHOSPHORYLATION.
[9]	"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: 16203764] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, OVEREXPRESSION IN CANCERS.
[10]	"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: 16040610] [Abstract] Cited for: FUNCTION, INTERACTION WITH FZR1, DEVELOPMENTAL STAGE, UBIQUITINATION, MUTAGENESIS OF ARG-41 AND LEU-44.
[11]	"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: 15496454] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"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: 15616196] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"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: 15800069] [Abstract] Cited for: INTERACTION WITH CD2AP, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, MUTAGENESIS OF ARG-32.
[14]	"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: 16129829] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; THR-320; SER-323; THR-401; SER-449 AND SER-485, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; THR-194; SER-362; THR-368; SER-449 AND SER-927, MASS SPECTROMETRY. Tissue: Epithelium.
[18]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-102 AND SER-661, MASS SPECTROMETRY.
[19]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-72; SER-99; SER-102; SER-172; THR-320; SER-323; THR-364; THR-393; THR-397; THR-401; SER-449; SER-485; SER-518; SER-553; SER-658; SER-661; SER-664; SER-792 AND SER-927, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. IPI00657687.
RefSeq	NP_061155.2.
UniGene	Hs.62180
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q9NQW6.
Proteomic databases
PRIDE	Q9NQW6.
Genome annotation databases
Ensembl	ENSG00000011426. Homo sapiens. [Contig view]
GeneID	54443.
KEGG	hsa:54443.
Organism-specific databases
GeneCards	GC07P036395.
H-InvDB	HIX0006603.
HGNC	HGNC:14082. ANLN.
PharmGKB	PA24809.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9NQW6.
HOVERGEN	Q9NQW6.
OMA	Q9NQW6. SEEQEDA.
Gene expression databases
ArrayExpress	Q9NQW6.
Bgee	Q9NQW6.
CleanEx	HS_ANLN.
GermOnline	ENSG00000011426. Homo sapiens.
Family and domain databases
InterPro	IPR011993. PH_type. IPR001849. Pleckstrin_homology. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
Pfam	PF00169. PH. 1 hit. [Graphical view]
SMART	SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)