Details for: ANLN
Associated with
Other Information
Genular Protein ID: 75974136
Symbol: ANLN_HUMAN
Name: Anillin
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 10931866
Title: Functional analysis of a human homolog of the Drosophila actin binding protein anillin suggests a role in cytokinesis.
PubMed ID: 10931866
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 17974005
Title: The full-ORF clone resource of the German cDNA consortium.
PubMed ID: 17974005
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 12479805
Title: Self- and actin-templated assembly of mammalian septins.
PubMed ID: 12479805
PubMed ID: 12637748
Title: Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor.
PubMed ID: 12637748
PubMed ID: 16357138
Title: ANLN plays a critical role in human lung carcinogenesis through the activation of RHOA and by involvement in the phosphoinositide 3-kinase/AKT pathway.
PubMed ID: 16357138
PubMed ID: 16203764
Title: The septin-binding protein anillin is overexpressed in diverse human tumors.
PubMed ID: 16203764
PubMed ID: 16040610
Title: Anillin is a substrate of anaphase-promoting complex/cyclosome (APC/C) that controls spatial contractility of myosin during late cytokinesis.
PubMed ID: 16040610
PubMed ID: 15496454
Title: Anillin binds nonmuscle myosin II and regulates the contractile ring.
PubMed ID: 15496454
PubMed ID: 15616196
Title: 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.
PubMed ID: 15616196
PubMed ID: 15800069
Title: Clues to CD2-associated protein involvement in cytokinesis.
PubMed ID: 15800069
PubMed ID: 16129829
Title: MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis.
PubMed ID: 16129829
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17924679
Title: 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.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 22814378
Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
PubMed ID: 22814378
PubMed ID: 23870127
Title: Cortical dynein and asymmetric membrane elongation coordinately position the spindle in anaphase.
PubMed ID: 23870127
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24676636
Title: Mutations in the gene that encodes the F-actin binding protein anillin cause FSGS.
PubMed ID: 24676636
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
Sequence Information:
- Length: 1124
- Mass: 124199
- Checksum: 79A8CC25C950DB2D
- Sequence:
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV SKTQSLPVTE KVTENQIPAK NSSTEPKGFT ECEMTKSSPL KITLFLEEDK SLKVTSDPKV EQKIEVIREI EMSVDDDDIN SSKVINDLFS DVLEEGELDM EKSQEEMDQA LAESSEEQED ALNISSMSLL APLAQTVGVV SPESLVSTPR LELKDTSRSD ESPKPGKFQR TRVPRAESGD SLGSEDRDLL YSIDAYRSQR FKETERPSIK QVIVRKEDVT SKLDEKNNAF PCQVNIKQKM QELNNEINMQ QTVIYQASQA LNCCVDEEHG KGSLEEAEAE RLLLIATGKR TLLIDELNKL KNEGPQRKNK ASPQSEFMPS KGSVTLSEIR LPLKADFVCS TVQKPDAANY YYLIILKAGA ENMVATPLAS TSNSLNGDAL TFTTTFTLQD VSNDFEINIE VYSLVQKKDP SGLDKKKKTS KSKAITPKRL LTSITTKSNI HSSVMASPGG LSAVRTSNFA LVGSYTLSLS SVGNTKFVLD KVPFLSSLEG HIYLKIKCQV NSSVEERGFL TIFEDVSGFG AWHRRWCVLS GNCISYWTYP DDEKRKNPIG RINLANCTSR QIEPANREFC ARRNTFELIT VRPQREDDRE TLVSQCRDTL CVTKNWLSAD TKEERDLWMQ KLNQVLVDIR LWQPDACYKP IGKP
Genular Protein ID: 2153050722
Symbol: A8K5D9_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 1086
- Mass: 119899
- Checksum: 0CE2B8C9113066FD
- Sequence:
MDPFTEKLLE RTRARRENLQ RKMAERPTAA PRSMTHAKRA RQPLSEASNQ QPLSGGEEKS CTKPSPSKKR CSDNTEVEVS NLENKQPVES TSAKSCSPSP VSPQVQPQAA DTISDSVAVP ASLLGMRRGL NSRLEATAAS SVKTRMQKLA EQRRRWDNDD MTDDIPESSL FSPMPSEEKA ASPPRPLLSN ASATPVGRRG RLANLAATIC SWEDDVNHSF AKQNSVQEQP GTACLSKFSS ASGASARINS SSVKQEATFC SQRDGDASLN KALSSSADDA SLVNASISSS VKATSPVKST TSITDAKSCE GQNPELLPKT PISPLKTGVS KPIVKSTLSQ TVPSKGELSR EICLQSQSKD KSTTPGGTGI KPFLERFGER CQEHSKESPA RSTPHRTPII TPNTKAIQER LFKQDTSSST THLAQQLKQE RQKELACLRG RFDKGNIWSA EKGGNSKSKQ LETKQETHCQ STPLKKHQGV SKTQSLPVTE KVTENQIPAK NSSTEPKVIR EIEMSVDDDD INSSKVINDL FSDVLEEGEL DMEKSQEEMD QALAESSEEQ EDALNISSMS LLAPLAQTVG VVSPESLVST PRLELKDTSR SDESPKPGKF QRTRVPRAES GDSLGSEDRD LLYSIDAYRS QRFKETERPS IKQVIVRKED VTSKLDEKNN AFPCQVNIKQ KMQELNNEIN MQQTVIYQAS QALNCCVDEE HGKGSLEEAE AERLLLIATG KRTLLIDELN KLKNEGPQRK NKASPQSEFM PSKGSVTLSE IRLPLKADFV CSTVQKPDAA NYYYLIILKA GAENMVATPL ASTSNSLNGD ALTFITTFTL QDVSNDFEIN IEVYSLVQKK DPSGLDKKKK TSKSKAITPK RLLTSITTKS NIHSSVMASP GGLSAVRTSN FALVGSYTLS LSSVGNTKFV LDKVPFLSSL EGHIYLKIKC QVNSSVEERG FLTIFEDVSG FGAWHRRWCV LSGNCISYWT YPDDEKRKNP IGRINLANCT SRQIEPANRE FCARRNTFEL ITVRPQREDD RETLVSQCRD TLCVTKNWLS ADTKEERDLW MQKLNQVLVD IRLWQPDACY KPIGKP
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.