MAMD1_HUMAN
ID MAMD1_HUMAN Reviewed; 774 AA.
AC Q13495; B2RCQ4; B4DG93; B9EGA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Mastermind-like domain-containing protein 1;
DE AltName: Full=F18;
DE AltName: Full=Protein CG1;
GN Name=MAMLD1; Synonyms=CG1, CXorf6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8640223; DOI=10.1038/ng0696-175;
RA Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J.,
RA Klauck S.M., Poutska A., Dahl N.;
RT "A gene mutated in X-linked myotubular myopathy defines a new putative
RT tyrosine phosphatase family conserved in yeast.";
RL Nat. Genet. 13:175-182(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 23-774 (ISOFORM 1).
RC TISSUE=Amygdala, and Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY NR5A1, AND
RP MUTAGENESIS OF LEU-176.
RX PubMed=18162467; DOI=10.1074/jbc.m703289200;
RA Fukami M., Wada Y., Okada M., Kato F., Katsumata N., Baba T., Morohashi K.,
RA Laporte J., Kitagawa M., Ogata T.;
RT "Mastermind-like domain-containing 1 (MAMLD1 or CXorf6) transactivates the
RT Hes3 promoter, augments testosterone production, and contains the SF1
RT target sequence.";
RL J. Biol. Chem. 283:5525-5532(2008).
RN [6]
RP INVOLVEMENT IN HYSP2, AND VARIANTS SER-359; ARG-580 AND SER-662.
RX PubMed=17086185; DOI=10.1038/ng1900;
RA Fukami M., Wada Y., Miyabayashi K., Nishino I., Hasegawa T., Camerino G.,
RA Kretz C., Buj-Bello A., Laporte J., Yamada G., Morohashi K., Ogata T.;
RT "CXorf6 is a causative gene for hypospadias.";
RL Nat. Genet. 38:1369-1371(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Transactivates the HES3 promoter independently of NOTCH
CC proteins. HES3 is a non-canonical NOTCH target gene which lacks binding
CC sites for RBPJ. {ECO:0000269|PubMed:18162467}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18162467}.
CC Note=Punctate nuclear localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13495-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13495-3; Sequence=VSP_037654, VSP_037655;
CC Name=3;
CC IsoId=Q13495-4; Sequence=VSP_037654;
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain, fetal ovary and fetal
CC testis. Expressed in adult brain, ovary, skin, testis, uterus. Highly
CC expressed in skeletal muscle. {ECO:0000269|PubMed:18162467}.
CC -!- INDUCTION: By NR5A1. {ECO:0000269|PubMed:18162467}.
CC -!- DISEASE: Hypospadias 2, X-linked (HYSP2) [MIM:300758]: A common
CC malformation in which the urethra opens on the ventral side of the
CC penis, due to developmental arrest of urethral fusion. The opening can
CC be located glandular, penile, or even more posterior in the scrotum or
CC perineum. Hypospadias is a feature of several syndromic disorders,
CC including the androgen insensitivity syndrome and Opitz syndrome.
CC {ECO:0000269|PubMed:17086185}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the mastermind family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50551.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG37651.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U46023; AAC50551.1; ALT_FRAME; mRNA.
DR EMBL; AK294478; BAG57704.1; -; mRNA.
DR EMBL; AK315217; BAG37651.1; ALT_INIT; mRNA.
DR EMBL; AC109994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL034384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136324; AAI36325.1; -; mRNA.
DR CCDS; CCDS14693.2; -. [Q13495-1]
DR CCDS; CCDS55525.1; -. [Q13495-4]
DR CCDS; CCDS55526.1; -. [Q13495-3]
DR RefSeq; NP_001170936.1; NM_001177465.2. [Q13495-3]
DR RefSeq; NP_001170937.1; NM_001177466.2. [Q13495-4]
DR RefSeq; NP_005482.2; NM_005491.4. [Q13495-1]
DR RefSeq; XP_006724865.1; XM_006724802.3. [Q13495-1]
DR RefSeq; XP_006724866.1; XM_006724803.3. [Q13495-4]
DR RefSeq; XP_016884677.1; XM_017029188.1. [Q13495-4]
DR AlphaFoldDB; Q13495; -.
DR BioGRID; 115357; 2.
DR IntAct; Q13495; 4.
DR STRING; 9606.ENSP00000414517; -.
DR GlyGen; Q13495; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q13495; -.
DR PhosphoSitePlus; Q13495; -.
DR BioMuta; MAMLD1; -.
DR DMDM; 215274020; -.
DR EPD; Q13495; -.
DR jPOST; Q13495; -.
DR MassIVE; Q13495; -.
DR MaxQB; Q13495; -.
DR PaxDb; Q13495; -.
DR PeptideAtlas; Q13495; -.
DR PRIDE; Q13495; -.
DR ProteomicsDB; 59492; -. [Q13495-1]
DR ProteomicsDB; 59493; -. [Q13495-3]
DR ProteomicsDB; 59494; -. [Q13495-4]
DR Antibodypedia; 16946; 65 antibodies from 18 providers.
DR DNASU; 10046; -.
DR Ensembl; ENST00000370401.7; ENSP00000359428.2; ENSG00000013619.15. [Q13495-1]
DR Ensembl; ENST00000426613.5; ENSP00000397438.2; ENSG00000013619.15. [Q13495-4]
DR Ensembl; ENST00000432680.7; ENSP00000414517.2; ENSG00000013619.15. [Q13495-3]
DR Ensembl; ENST00000682253.1; ENSP00000506890.1; ENSG00000013619.15. [Q13495-1]
DR GeneID; 10046; -.
DR KEGG; hsa:10046; -.
DR MANE-Select; ENST00000370401.7; ENSP00000359428.2; NM_005491.5; NP_005482.2.
DR UCSC; uc004fee.2; human. [Q13495-1]
DR CTD; 10046; -.
DR DisGeNET; 10046; -.
DR GeneCards; MAMLD1; -.
DR HGNC; HGNC:2568; MAMLD1.
DR HPA; ENSG00000013619; Low tissue specificity.
DR MalaCards; MAMLD1; -.
DR MIM; 300120; gene.
DR MIM; 300758; phenotype.
DR neXtProt; NX_Q13495; -.
DR OpenTargets; ENSG00000013619; -.
DR Orphanet; 95706; Non-syndromic posterior hypospadias.
DR Orphanet; 456328; X-linked myotubular myopathy-abnormal genitalia syndrome.
DR PharmGKB; PA162394950; -.
DR VEuPathDB; HostDB:ENSG00000013619; -.
DR eggNOG; ENOG502QV1F; Eukaryota.
DR GeneTree; ENSGT00730000111366; -.
DR HOGENOM; CLU_298909_0_0_1; -.
DR InParanoid; Q13495; -.
DR OMA; YCPEKLS; -.
DR OrthoDB; 296734at2759; -.
DR PhylomeDB; Q13495; -.
DR TreeFam; TF332922; -.
DR PathwayCommons; Q13495; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR SignaLink; Q13495; -.
DR BioGRID-ORCS; 10046; 10 hits in 693 CRISPR screens.
DR ChiTaRS; MAMLD1; human.
DR GenomeRNAi; 10046; -.
DR Pharos; Q13495; Tbio.
DR PRO; PR:Q13495; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13495; protein.
DR Bgee; ENSG00000013619; Expressed in right ovary and 121 other tissues.
DR ExpressionAtlas; Q13495; baseline and differential.
DR Genevisible; Q13495; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR026131; MAMLD1.
DR PANTHER; PTHR15275; PTHR15275; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..774
FT /note="Mastermind-like domain-containing protein 1"
FT /id="PRO_0000089592"
FT REGION 257..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 33..57
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037654"
FT VAR_SEQ 640..774
FT /note="GCCHLFAWTSAASSVKPQHQHGNSFTSRQDPQPGDVSPSNITHVDKACKLGE
FT ARHPQVSLGRQPPSCQALGSESFLPGSSFAHELARVTSSYSTSEAAPWGSWDPKAWRQV
FT PAPLLPSCDATARGTEIRSYGNDP -> QEEQRSGLMAMTPERQNAYISQQMSPFEAVQ
FT EQVTSKCSRIKASPPSSKHLMPPRTGLLQNNLSPGMIPLTRHQSCEGMGVISPTLGKRQ
FT GIFTSSPQCPILSHSGQTPLGRLDSVCQHMQSPKATPPEVPLPGFCPSSLGTQSLSPHQ
FT LRRPSVPRMPTAFNNAAWVTAAAAVTTAVSGKTPLSQVDNSVQQHSPSGQACLQRPSDW
FT EAQVPAAMGTQVPLANNPSFSLLGSQSLRQSPVQGPVPVANTTKFLQQGMASFSPLSPI
FT QGIEPPSYVAAAATAAAASAVAASQFPGPFDRTDIPPELPPADFLRQPQPPLNDLISSP
FT DCNEVDFIEALLKGSCVSPDEDWVCNLRLIDDILEQHAAAQNATAQNSGQVTQDAGAL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037655"
FT VARIANT 359
FT /note="P -> S (in dbSNP:rs41313406)"
FT /evidence="ECO:0000269|PubMed:17086185"
FT /id="VAR_030024"
FT VARIANT 580
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:17086185"
FT /id="VAR_030025"
FT VARIANT 662
FT /note="N -> S (in dbSNP:rs2073043)"
FT /evidence="ECO:0000269|PubMed:17086185"
FT /id="VAR_020273"
FT MUTAGEN 176
FT /note="L->P: Reduces transcriptional activation of the HES3
FT promoter."
FT /evidence="ECO:0000269|PubMed:18162467"
FT CONFLICT 61
FT /note="K -> N (in Ref. 1; AAC50551)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Y -> S (in Ref. 1; AAC50551)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..347
FT /note="PH -> LQ (in Ref. 1; AAC50551)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="M -> T (in Ref. 2; BAG37651)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="G -> V (in Ref. 1; AAC50551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 83231 MW; F8CDD865CBD86AF7 CRC64;
MDDWKSRLVI KSMLPHFAMV GNRQEPRKLQ ESGKKPSWME EEDLSFLYKS SPGRKHQGTV
KRRQEEDHFQ FPDMADGGYP NKIKRPCLED VTLAMGPGAH PSTACAELQV PPLTINPSPA
AMGVAGQSLL LENNPMNGNI MGSPFVVPQT TEVGLKGPTV PYYEKINSVP AVDQELQELL
EELTKIQDPS PNELDLEKIL GTKPEEPLVL DHPQATLSTT PKPSVQMSHL ESLASSKEFA
SSCSQVTGMS LQIPSSSTGI SYSIPSTSKQ IVSPSSSMAQ SKSQVQAMLP VALPPLPVPQ
WHHAHQLKAL AASKQGSATK QQGPTPSWSG LPPPGLSPPY RPVPSPHPPP LPLPPPPPPF
SPQSLMVSCM SSNTLSGSTL RGSPNALLSS MTSSSNAALG PAMPYAPEKL PSPALTQQPQ
FGPQSSILAN LMSSTIKTPQ GHLMSALPAS NPGPSPPYRP EKLSSPGLPQ QSFTPQCSLI
RSLTPTSNLL SQQQQQQQQQ QQANVIFKPI SSNSSKTLSM IMQQGMASSS PGATEPFTFG
NTKPLSHFVS EPGPQKMPSM PTTSRQPSLL HYLQQPTPTQ ASSATASSTA TATLQLQQQQ
QQQQQQPDHS SFLLQQMMQQ PQRFQRSVAS DSMPALPRQG CCHLFAWTSA ASSVKPQHQH
GNSFTSRQDP QPGDVSPSNI THVDKACKLG EARHPQVSLG RQPPSCQALG SESFLPGSSF
AHELARVTSS YSTSEAAPWG SWDPKAWRQV PAPLLPSCDA TARGTEIRSY GNDP
