ID FGD1_HUMAN Reviewed; 961 AA.
AC P98174; Q5H999; Q8N4D9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 24-JAN-2024, entry version 208.
DE RecName: Full=FYVE, RhoGEF and PH domain-containing protein 1;
DE AltName: Full=Faciogenital dysplasia 1 protein;
DE AltName: Full=Rho/Rac guanine nucleotide exchange factor FGD1;
DE Short=Rho/Rac GEF;
DE AltName: Full=Zinc finger FYVE domain-containing protein 3;
GN Name=FGD1; Synonyms=FGDY, ZFYVE3;
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].
RC TISSUE=Craniofacial;
RX PubMed=7954831; DOI=10.1016/0092-8674(94)90552-5;
RA Pasteris N.G., Cadle A., Logie L.J., Porteous M.E.M., Schwartz C.E.,
RA Stevenson R.E., Glover T.W., Wilroy R.S., Gorski J.L.;
RT "Isolation and characterization of the faciogenital dysplasia (Aarskog-
RT Scott syndrome) gene: a putative Rho/Rac guanine nucleotide exchange
RT factor.";
RL Cell 79:669-678(1994).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.
RX PubMed=8969170; DOI=10.1074/jbc.271.52.33169;
RA Zheng Y., Fischer D.J., Santos M.F., Tigyi G., Pasteris N.G., Gorski J.L.,
RA Xu Y.;
RT "The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-
RT specific guanine-nucleotide exchange factor.";
RL J. Biol. Chem. 271:33169-33172(1996).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-205; THR-711 AND
RP SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY 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 IDENTIFICATION BY 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).
RN [9]
RP VARIANT AAS HIS-522.
RX PubMed=11093277; DOI=10.1038/sj.ejhg.5200553;
RA Schwartz C.E., Gillessen-Kaesbach G., May M., Cappa M., Gorski J.L.,
RA Steindl K., Neri G.;
RT "Two novel mutations confirm FGD1 is responsible for the Aarskog
RT syndrome.";
RL Eur. J. Hum. Genet. 8:869-874(2000).
RN [10]
RP VARIANT AAS GLN-610.
RX PubMed=10930571; DOI=10.1016/s0014-5793(00)01857-3;
RA Orrico A., Galli L., Falciani M., Bracci M., Cavaliere M.L., Rinaldi M.M.,
RA Musacchio A., Sorrentino V.;
RT "A mutation in the pleckstrin homology (PH) domain of the FGD1 gene in an
RT Italian family with faciogenital dysplasia (Aarskog-Scott syndrome).";
RL FEBS Lett. 478:216-220(2000).
RN [11]
RP VARIANT LEU-312.
RX PubMed=11940089; DOI=10.1034/j.1399-0004.2002.610209.x;
RA Lebel R.R., May M., Pouls S., Lubs H.A., Stevenson R.E., Schwartz C.E.;
RT "Non-syndromic X-linked mental retardation associated with a missense
RT mutation (P312L) in the FGD1 gene.";
RL Clin. Genet. 61:139-145(2002).
RN [12]
RP VARIANTS AAS ILE-205; ALA-380 AND HIS-443.
RX PubMed=14560308; DOI=10.1038/sj.ejhg.5201081;
RA Orrico A., Galli L., Cavaliere M.L., Garavelli L., Fryns J.-P.,
RA Crushell E., Rinaldi M.M., Medeira A., Sorrentino V.;
RT "Phenotypic and molecular characterisation of the Aarskog-Scott syndrome: a
RT survey of the clinical variability in light of FGD1 mutation analysis in 46
RT patients.";
RL Eur. J. Hum. Genet. 12:16-23(2004).
CC -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho- and
CC Rac proteins, by exchanging bound GDP for free GTP. Plays a role in
CC regulating the actin cytoskeleton and cell shape.
CC {ECO:0000269|PubMed:8969170}.
CC -!- SUBUNIT: Interacts with DBNL/ABP1 and CTTN. May interact with CCPG1 (By
CC similarity). Binds CDC42. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
CC lamellipodium {ECO:0000250}. Cell projection, ruffle {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated with membrane
CC ruffles and lamellipodia. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal heart, brain, lung, kidney and
CC placenta. Less expressed in liver; adult heart, brain, lung, pancreas
CC and skeletal muscle.
CC -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC {ECO:0000250}.
CC -!- DISEASE: Aarskog-Scott syndrome (AAS) [MIM:305400]: An X-linked
CC recessive, rare multisystemic disorder characterized by
CC disproportionately short stature, and by facial, skeletal and
CC urogenital anomalies. Some patients manifest intellectual disability,
CC attention deficit disorder and hyperactivity.
CC {ECO:0000269|PubMed:10930571, ECO:0000269|PubMed:11093277,
CC ECO:0000269|PubMed:14560308}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; U11690; AAA57004.1; -; mRNA.
DR EMBL; Z85987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471154; EAW93179.1; -; Genomic_DNA.
DR EMBL; BC034530; AAH34530.1; -; mRNA.
DR CCDS; CCDS14359.1; -.
DR PIR; A55380; A55380.
DR RefSeq; NP_004454.2; NM_004463.2.
DR AlphaFoldDB; P98174; -.
DR SMR; P98174; -.
DR BioGRID; 108536; 42.
DR ELM; P98174; -.
DR IntAct; P98174; 23.
DR STRING; 9606.ENSP00000364277; -.
DR BindingDB; P98174; -.
DR ChEMBL; CHEMBL2862; -.
DR iPTMnet; P98174; -.
DR PhosphoSitePlus; P98174; -.
DR BioMuta; FGD1; -.
DR DMDM; 28202247; -.
DR EPD; P98174; -.
DR jPOST; P98174; -.
DR MassIVE; P98174; -.
DR MaxQB; P98174; -.
DR PaxDb; 9606-ENSP00000364277; -.
DR PeptideAtlas; P98174; -.
DR ProteomicsDB; 57809; -.
DR Pumba; P98174; -.
DR Antibodypedia; 376; 85 antibodies from 21 providers.
DR DNASU; 2245; -.
DR Ensembl; ENST00000375135.4; ENSP00000364277.3; ENSG00000102302.8.
DR GeneID; 2245; -.
DR KEGG; hsa:2245; -.
DR MANE-Select; ENST00000375135.4; ENSP00000364277.3; NM_004463.3; NP_004454.2.
DR UCSC; uc004dtg.3; human.
DR AGR; HGNC:3663; -.
DR CTD; 2245; -.
DR DisGeNET; 2245; -.
DR GeneCards; FGD1; -.
DR HGNC; HGNC:3663; FGD1.
DR HPA; ENSG00000102302; Low tissue specificity.
DR MalaCards; FGD1; -.
DR MIM; 300546; gene.
DR MIM; 305400; phenotype.
DR neXtProt; NX_P98174; -.
DR OpenTargets; ENSG00000102302; -.
DR Orphanet; 915; Aarskog-Scott syndrome.
DR PharmGKB; PA28102; -.
DR VEuPathDB; HostDB:ENSG00000102302; -.
DR eggNOG; KOG4424; Eukaryota.
DR GeneTree; ENSGT00940000159438; -.
DR HOGENOM; CLU_011755_1_1_1; -.
DR InParanoid; P98174; -.
DR OMA; QQRWMAV; -.
DR OrthoDB; 5385125at2759; -.
DR PhylomeDB; P98174; -.
DR TreeFam; TF316247; -.
DR PathwayCommons; P98174; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR SignaLink; P98174; -.
DR SIGNOR; P98174; -.
DR BioGRID-ORCS; 2245; 14 hits in 774 CRISPR screens.
DR ChiTaRS; FGD1; human.
DR GeneWiki; FGD1; -.
DR GenomeRNAi; 2245; -.
DR Pharos; P98174; Tbio.
DR PRO; PR:P98174; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P98174; Protein.
DR Bgee; ENSG00000102302; Expressed in cortical plate and 119 other cell types or tissues.
DR ExpressionAtlas; P98174; baseline and differential.
DR Genevisible; P98174; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; IDA:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd15741; FYVE_FGD1_2_4; 1.
DR CDD; cd01219; PH1_FGD1; 1.
DR CDD; cd13236; PH2_FGD1-4; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR035941; FGD1-4_PH2.
DR InterPro; IPR035939; FGD1_PH1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF79; FYVE, RHOGEF AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Cytoskeleton; Disease variant;
KW Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..961
FT /note="FYVE, RhoGEF and PH domain-containing protein 1"
FT /id="PRO_0000080940"
FT DOMAIN 373..561
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 590..689
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 821..921
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 730..790
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 1..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 171..187
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 141..190
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..352
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 736
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 739
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 756
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 761
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 782
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 711
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 205
FT /note="S -> I (in AAS)"
FT /evidence="ECO:0000269|PubMed:14560308"
FT /id="VAR_019268"
FT VARIANT 312
FT /note="P -> L (in dbSNP:rs28935498)"
FT /evidence="ECO:0000269|PubMed:11940089"
FT /id="VAR_019269"
FT VARIANT 380
FT /note="E -> A (in AAS)"
FT /evidence="ECO:0000269|PubMed:14560308"
FT /id="VAR_019270"
FT VARIANT 443
FT /note="R -> H (in AAS; dbSNP:rs137853266)"
FT /evidence="ECO:0000269|PubMed:14560308"
FT /id="VAR_019271"
FT VARIANT 522
FT /note="R -> H (in AAS; dbSNP:rs137853264)"
FT /evidence="ECO:0000269|PubMed:11093277"
FT /id="VAR_015236"
FT VARIANT 610
FT /note="R -> Q (in AAS; dbSNP:rs28935497)"
FT /evidence="ECO:0000269|PubMed:10930571"
FT /id="VAR_015237"
FT CONFLICT 10..23
FT /note="AGPSEPEHPATNPP -> RRAFGARTPGHEPA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> G (in Ref. 1; AAA57004)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 106561 MW; 30963F7B9931E45C CRC64;
MHGHRAPGGA GPSEPEHPAT NPPGAAPPAC ADSDPGASEP GLLARRGSGS ALGGPLDPQF
VGPSDTSLGA APGHRVLPCG PSPQHHRALR FSYHLEGSQP RPGLHQGNRI LVKSLSLDPG
QSLEPHPEGP QRLRSDPGPP TETPSQRPSP LKRAPGPKPQ VPPKPSYLQM PRMPPPLEPI
PPPPSRPLPA DPRVAKGLAP RAEASPSSAA VSSLIEKFER EPVIVASDRP VPGPSPGPPE
PVMLPQPTSQ PPVPQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
SDDGPPSHSL CPGPPALASV PVALADPHRP GSQEVDSDLE EEDDEEEEEE KDREIPVPLM
ERQESVELTV QQKVFHIANE LLQTEKAYVS RLHLLDQVFC ARLLEEARNR SSFPADVVHG
IFSNICSIYC FHQQFLLPEL EKRMEEWDRY PRIGDILQKL APFLKMYGEY VKNFDRAVEL
VNTWTERSTQ FKVIIHEVQK EEACGNLTLQ HHMLEPVQRI PRYELLLKDY LLKLPHGSPD
SKDAQKSLEL IATAAEHSNA AIRKMERMHK LLKVYELLGG EEDIVSPTKE LIKEGHILKL
SAKNGTTQDR YLILFNDRLL YCVPRLRLLG QKFSVRARID VDGMELKESS NLNLPRTFLV
SGKQRSLELQ ARTEEEKKDW VQAINSTLLK HEQTLETFKL LNSTNREDED TPPNSPNVDL
GKRAPTPIRE KEVTMCMRCQ EPFNSITKRR HHCKACGHVV CGKCSEFRAR LVYDNNRSNR
VCTDCYVALH GVPGSSPACS QHTPQRRRSI LEKQASVAAE NSVICSFLHY MEKGGKGWHK
AWFVVPENEP LVLYIYGAPQ DVKAQRSLPL IGFEVGPPEA GERPDRRHVF KITQSHLSWY
FSPETEELQR RWMAVLGRAG RGDTFCPGPT LSEDREMEEA PVAALGATAE PPESPQTRDK
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