Full text data of ARHGAP4
ARHGAP4
(KIAA0131, RGC1, RHOGAP4)
[Confidence: low (only semi-automatic identification from reviews)]
Rho GTPase-activating protein 4 (Rho-GAP hematopoietic protein C1; Rho-type GTPase-activating protein 4; p115)
Rho GTPase-activating protein 4 (Rho-GAP hematopoietic protein C1; Rho-type GTPase-activating protein 4; p115)
UniProt
P98171
ID RHG04_HUMAN Reviewed; 946 AA.
AC P98171; Q14144; Q86UY3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Rho GTPase-activating protein 4;
DE AltName: Full=Rho-GAP hematopoietic protein C1;
DE AltName: Full=Rho-type GTPase-activating protein 4;
DE AltName: Full=p115;
GN Name=ARHGAP4; Synonyms=KIAA0131, RGC1, RHOGAP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=8570618; DOI=10.1073/pnas.93.2.695;
RA Tribioli C., Droetto S., Bione S., Cesareni G., Torrisi M.R.,
RA Lotti L.V., Lanfrancone L., Toniolo D., Pelicci P.-G.;
RT "An X chromosome-linked gene encoding a protein with characteristics
RT of a rhoGAP predominantly expressed in hematopoietic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:695-699(1996).
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-946 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=7981673; DOI=10.1093/hmg/3.7.1061;
RA Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C.,
RA Torri G., Toniolo D.;
RT "Isolation of new genes in distal Xq28: transcriptional map and
RT identification of a human homologue of the ARD1 N-acetyl transferase
RT of Saccharomyces cerevisiae.";
RL Hum. Mol. Genet. 3:1061-1068(1994).
RN [7]
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP STRUCTURE BY NMR OF 746-814.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domain in Rho-GTPase-activating protein
RT 4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Inhibitory effect on stress fiber organization. May
CC down-regulate Rho-like GTPase in hematopoietic cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Just below the plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98171-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98171-2; Sequence=VSP_042902;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly in hematopoietic cells (spleen,
CC thymus and leukocytes); low levels in placenta, lung and various
CC fetal tissues.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
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DR EMBL; X78817; CAA55394.1; -; mRNA.
DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72778.1; -; Genomic_DNA.
DR EMBL; BC052303; AAH52303.1; -; mRNA.
DR EMBL; D50921; BAA09480.1; -; mRNA.
DR PIR; I38100; I38100.
DR RefSeq; NP_001158213.1; NM_001164741.1.
DR RefSeq; NP_001657.3; NM_001666.4.
DR UniGene; Hs.701324; -.
DR PDB; 2EPD; NMR; -; A=746-814.
DR PDBsum; 2EPD; -.
DR ProteinModelPortal; P98171; -.
DR SMR; P98171; 502-695, 751-848.
DR IntAct; P98171; 3.
DR MINT; MINT-4717773; -.
DR STRING; 9606.ENSP00000203786; -.
DR PhosphoSite; P98171; -.
DR DMDM; 116242759; -.
DR PaxDb; P98171; -.
DR PRIDE; P98171; -.
DR DNASU; 393; -.
DR Ensembl; ENST00000350060; ENSP00000203786; ENSG00000089820.
DR Ensembl; ENST00000370028; ENSP00000359045; ENSG00000089820.
DR Ensembl; ENST00000596481; ENSP00000469103; ENSG00000268876.
DR Ensembl; ENST00000602200; ENSP00000472759; ENSG00000268876.
DR GeneID; 393; -.
DR KEGG; hsa:393; -.
DR UCSC; uc004fjk.2; human.
DR CTD; 393; -.
DR GeneCards; GC0XM153172; -.
DR HGNC; HGNC:674; ARHGAP4.
DR HPA; HPA001012; -.
DR HPA; HPA001083; -.
DR MIM; 300023; gene.
DR neXtProt; NX_P98171; -.
DR PharmGKB; PA24958; -.
DR eggNOG; NOG264793; -.
DR HOGENOM; HOG000039980; -.
DR HOVERGEN; HBG051637; -.
DR OMA; WTQYTQR; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; P98171; -.
DR GeneWiki; ARHGAP4; -.
DR GenomeRNAi; 393; -.
DR NextBio; 1639; -.
DR PMAP-CutDB; P98171; -.
DR PRO; PR:P98171; -.
DR ArrayExpress; P98171; -.
DR Bgee; P98171; -.
DR CleanEx; HS_ARHGAP4; -.
DR Genevestigator; P98171; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005100; F:Rho GTPase activator activity; TAS:ProtInc.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; GTPase activation; Polymorphism; Reference proteome;
KW SH3 domain.
FT CHAIN 1 946 Rho GTPase-activating protein 4.
FT /FTId=PRO_0000056701.
FT DOMAIN 15 88 FCH.
FT DOMAIN 507 695 Rho-GAP.
FT DOMAIN 746 805 SH3.
FT COILED 128 195 Potential.
FT VAR_SEQ 227 227 K -> KLWPPQRPVAASSCAPVCWLQAGFLVHPPWWGAMCA
FT PSTHQ (in isoform 2).
FT /FTId=VSP_042902.
FT VARIANT 104 104 A -> V (in dbSNP:rs5987182).
FT /FTId=VAR_028413.
FT CONFLICT 609 609 A -> D (in Ref. 1; CAA55394).
FT CONFLICT 731 731 E -> D (in Ref. 1; CAA55394).
FT STRAND 749 755
FT STRAND 772 780
FT STRAND 783 788
FT STRAND 791 801
SQ SEQUENCE 946 AA; 105026 MW; ED3D48C5DAA24969 CRC64;
MAAHGKLRRE RGLQAEYETQ VKEMRWQLSE QLRCLELQGE LRRELLQELA EFMRRRAEVE
LEYSRGLEKL AERFSSRGGR LGSSREHQSF RKEPSLLSPL HCWAVLLQHT RQQSRESAAL
SEVLAGPLAQ RLSHIAEDVG RLVKKSRDLE QQLQDELLEV VSELQTAKKT YQAYHMESVN
AEAKLREAER QEEKRAGRSV PTTTAGATEA GPLRKSSLKK GGRLVEKRQA KFMEHKLKCT
KARNEYLLSL ASVNAAVSNY YLHDVLDLMD CCDTGFHLAL GQVLRSYTAA ESRTQASQVQ
GLGSLEEAVE ALDPPGDKAK VLEVHATVFC PPLRFDYHPH DGDEVAEICV EMELRDEILP
RAQNIQSRLD RQTIETEEVN KTLKATLQAL LEVVASDDGD VLDSFQTSPS TESLKSTSSD
PGSRQAGRRR GQQQETETFY LTKLQEYLSG RSILAKLQAK HEKLQEALQR GDKEEQEVSW
TQYTQRKFQK SRQPRPSSQY NQRLFGGDME KFIQSSGQPV PLVVESCIRF INLNGLQHEG
IFRVSGAQLR VSEIRDAFER GEDPLVEGCT AHDLDSVAGV LKLYFRSLEP PLFPPDLFGE
LLASSELEAT AERVEHVSRL LWRLPAPVLV VLRYLFTFLN HLAQYSDENM MDPYNLAVCF
GPTLLPVPAG QDPVALQGRV NQLVQTLIVQ PDRVFPPLTS LPGPVYEKCM APPSASCLGD
AQLESLGADN EPELEAEMPA QEDDLEGVVE AVACFAYTGR TAQELSFRRG DVLRLHERAS
SDWWRGEHNG MRGLIPHKYI TLPAGTEKQV VGAGLQTAGE SGSSPEGLLA SELVHRPEPC
TSPEAMGPSG HRRRCLVPAS PEQHVEVDKA VAQNMDSVFK ELLGKTSVRQ GLGPASTTSP
SPGPRSPKAP PSSRLGRNKG FSRGPGAPAS PSASHPQGLD TTPKPH
//
ID RHG04_HUMAN Reviewed; 946 AA.
AC P98171; Q14144; Q86UY3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 17-OCT-2006, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Rho GTPase-activating protein 4;
DE AltName: Full=Rho-GAP hematopoietic protein C1;
DE AltName: Full=Rho-type GTPase-activating protein 4;
DE AltName: Full=p115;
GN Name=ARHGAP4; Synonyms=KIAA0131, RGC1, RHOGAP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=8570618; DOI=10.1073/pnas.93.2.695;
RA Tribioli C., Droetto S., Bione S., Cesareni G., Torrisi M.R.,
RA Lotti L.V., Lanfrancone L., Toniolo D., Pelicci P.-G.;
RT "An X chromosome-linked gene encoding a protein with characteristics
RT of a rhoGAP predominantly expressed in hematopoietic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:695-699(1996).
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-946 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-103 (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=7981673; DOI=10.1093/hmg/3.7.1061;
RA Tribioli C., Mancini M., Plassart E., Bione S., Rivella S., Sala C.,
RA Torri G., Toniolo D.;
RT "Isolation of new genes in distal Xq28: transcriptional map and
RT identification of a human homologue of the ARD1 N-acetyl transferase
RT of Saccharomyces cerevisiae.";
RL Hum. Mol. Genet. 3:1061-1068(1994).
RN [7]
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP STRUCTURE BY NMR OF 746-814.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of SH3 domain in Rho-GTPase-activating protein
RT 4.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Inhibitory effect on stress fiber organization. May
CC down-regulate Rho-like GTPase in hematopoietic cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Just below the plasma
CC membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98171-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98171-2; Sequence=VSP_042902;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Predominantly in hematopoietic cells (spleen,
CC thymus and leukocytes); low levels in placenta, lung and various
CC fetal tissues.
CC -!- SIMILARITY: Contains 1 FCH domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -----------------------------------------------------------------------
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DR EMBL; X78817; CAA55394.1; -; mRNA.
DR EMBL; U52112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72778.1; -; Genomic_DNA.
DR EMBL; BC052303; AAH52303.1; -; mRNA.
DR EMBL; D50921; BAA09480.1; -; mRNA.
DR PIR; I38100; I38100.
DR RefSeq; NP_001158213.1; NM_001164741.1.
DR RefSeq; NP_001657.3; NM_001666.4.
DR UniGene; Hs.701324; -.
DR PDB; 2EPD; NMR; -; A=746-814.
DR PDBsum; 2EPD; -.
DR ProteinModelPortal; P98171; -.
DR SMR; P98171; 502-695, 751-848.
DR IntAct; P98171; 3.
DR MINT; MINT-4717773; -.
DR STRING; 9606.ENSP00000203786; -.
DR PhosphoSite; P98171; -.
DR DMDM; 116242759; -.
DR PaxDb; P98171; -.
DR PRIDE; P98171; -.
DR DNASU; 393; -.
DR Ensembl; ENST00000350060; ENSP00000203786; ENSG00000089820.
DR Ensembl; ENST00000370028; ENSP00000359045; ENSG00000089820.
DR Ensembl; ENST00000596481; ENSP00000469103; ENSG00000268876.
DR Ensembl; ENST00000602200; ENSP00000472759; ENSG00000268876.
DR GeneID; 393; -.
DR KEGG; hsa:393; -.
DR UCSC; uc004fjk.2; human.
DR CTD; 393; -.
DR GeneCards; GC0XM153172; -.
DR HGNC; HGNC:674; ARHGAP4.
DR HPA; HPA001012; -.
DR HPA; HPA001083; -.
DR MIM; 300023; gene.
DR neXtProt; NX_P98171; -.
DR PharmGKB; PA24958; -.
DR eggNOG; NOG264793; -.
DR HOGENOM; HOG000039980; -.
DR HOVERGEN; HBG051637; -.
DR OMA; WTQYTQR; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; P98171; -.
DR GeneWiki; ARHGAP4; -.
DR GenomeRNAi; 393; -.
DR NextBio; 1639; -.
DR PMAP-CutDB; P98171; -.
DR PRO; PR:P98171; -.
DR ArrayExpress; P98171; -.
DR Bgee; P98171; -.
DR CleanEx; HS_ARHGAP4; -.
DR Genevestigator; P98171; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005100; F:Rho GTPase activator activity; TAS:ProtInc.
DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
DR GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50133; FCH; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; GTPase activation; Polymorphism; Reference proteome;
KW SH3 domain.
FT CHAIN 1 946 Rho GTPase-activating protein 4.
FT /FTId=PRO_0000056701.
FT DOMAIN 15 88 FCH.
FT DOMAIN 507 695 Rho-GAP.
FT DOMAIN 746 805 SH3.
FT COILED 128 195 Potential.
FT VAR_SEQ 227 227 K -> KLWPPQRPVAASSCAPVCWLQAGFLVHPPWWGAMCA
FT PSTHQ (in isoform 2).
FT /FTId=VSP_042902.
FT VARIANT 104 104 A -> V (in dbSNP:rs5987182).
FT /FTId=VAR_028413.
FT CONFLICT 609 609 A -> D (in Ref. 1; CAA55394).
FT CONFLICT 731 731 E -> D (in Ref. 1; CAA55394).
FT STRAND 749 755
FT STRAND 772 780
FT STRAND 783 788
FT STRAND 791 801
SQ SEQUENCE 946 AA; 105026 MW; ED3D48C5DAA24969 CRC64;
MAAHGKLRRE RGLQAEYETQ VKEMRWQLSE QLRCLELQGE LRRELLQELA EFMRRRAEVE
LEYSRGLEKL AERFSSRGGR LGSSREHQSF RKEPSLLSPL HCWAVLLQHT RQQSRESAAL
SEVLAGPLAQ RLSHIAEDVG RLVKKSRDLE QQLQDELLEV VSELQTAKKT YQAYHMESVN
AEAKLREAER QEEKRAGRSV PTTTAGATEA GPLRKSSLKK GGRLVEKRQA KFMEHKLKCT
KARNEYLLSL ASVNAAVSNY YLHDVLDLMD CCDTGFHLAL GQVLRSYTAA ESRTQASQVQ
GLGSLEEAVE ALDPPGDKAK VLEVHATVFC PPLRFDYHPH DGDEVAEICV EMELRDEILP
RAQNIQSRLD RQTIETEEVN KTLKATLQAL LEVVASDDGD VLDSFQTSPS TESLKSTSSD
PGSRQAGRRR GQQQETETFY LTKLQEYLSG RSILAKLQAK HEKLQEALQR GDKEEQEVSW
TQYTQRKFQK SRQPRPSSQY NQRLFGGDME KFIQSSGQPV PLVVESCIRF INLNGLQHEG
IFRVSGAQLR VSEIRDAFER GEDPLVEGCT AHDLDSVAGV LKLYFRSLEP PLFPPDLFGE
LLASSELEAT AERVEHVSRL LWRLPAPVLV VLRYLFTFLN HLAQYSDENM MDPYNLAVCF
GPTLLPVPAG QDPVALQGRV NQLVQTLIVQ PDRVFPPLTS LPGPVYEKCM APPSASCLGD
AQLESLGADN EPELEAEMPA QEDDLEGVVE AVACFAYTGR TAQELSFRRG DVLRLHERAS
SDWWRGEHNG MRGLIPHKYI TLPAGTEKQV VGAGLQTAGE SGSSPEGLLA SELVHRPEPC
TSPEAMGPSG HRRRCLVPAS PEQHVEVDKA VAQNMDSVFK ELLGKTSVRQ GLGPASTTSP
SPGPRSPKAP PSSRLGRNKG FSRGPGAPAS PSASHPQGLD TTPKPH
//
MIM
300023
*RECORD*
*FIELD* NO
300023
*FIELD* TI
*300023 RHO GTPase-ACTIVATING PROTEIN 4; ARHGAP4
;;RHO GAP HEMATOPOIETIC PROTEIN C1; RGC1;;
read moreGTPase-ACTIVATING PROTEIN, RHO, 4; RHOGAP4
*FIELD* TX
CLONING
By constructing a detailed transcription map of the region of 2 Mb in
distal Xq28, Tribioli et al. (1996) identified a large number of novel
genes, including ARHGAP4, which they designated RGC1. RGC1 encodes a
cytoplasmic protein of 115 kD preferentially expressed in hematopoietic
cells and containing SH3 and GAP homologous regions. It appears to be a
member of the group of signaling proteins involved in regulation of the
small GTP-binding proteins of the RAS superfamily. Its localization in a
narrow cytoplasmic region just below the plasma membrane (as indicated
by immunocytochemistry on human cell lines using a polyclonal antibody)
and its inhibitory effect on stress fiber organization indicated to the
authors that the protein may downregulate RHO-like GTPase in
hematopoietic cells. The gene is approximately 20 kb long and encodes an
mRNA of 3.5 kb. The protein contains 946 amino acids.
CYTOGENETICS
Schoneberg et al. (1999) described a 16-year-old male with nephrogenic
diabetes insipidus (NDI; 304800) diagnosed at 8 months of age who had a
21.5-kb deletion encompassing the entire AVPR2 gene (300538) and most of
the RGC1 gene. Besides the symptoms of NDI, the patient had no major
morphologic abnormalities as determined by physical examination,
radiography, ultrasound, and CT scan. Blood chemical, enzyme, and
hormone values over a period of 16 years showed no deviations from
normal ranges. Close attention was paid to hematopoietic and immunologic
abnormalities because of the predominant expression pattern of the RGC1
gene in hematopoietic cells, but no abnormalities were observed.
Schoneberg et al. (1999) postulated that the loss of RGC1 function is
most likely compensated for by other members of the GAP family.
Demura et al. (2002) reported 2 novel types of contiguous gene deletion
of both the AVPR2 gene and the ARHGAP4 gene in unrelated Japanese
kindreds with NDI. They discussed the mechanism of each of the
deletions, which were 21.3 and 26.3 kb, respectively. Both patients,
despite lacking ARHGAP4, had no morphologic, clinical, or laboratory
abnormalities except for those usually found in patients with NDI.
Huang et al. (2012) reported 2 male dizygotic twins with a 17.9-kb
deletion of Xq28 encompassing the entire AVPR2 gene and extending into
intron 7 of the ARHGAP4 gene. The mother was a carrier of the deletion.
The boys showed significant failure to thrive in infancy and were
diagnosed with nephrogenic diabetes insipidus at 27 months of age. Both
showed delayed psychomotor development. At age 11 years, they had
intellectual impairment (IQ in the fifties), short stature, and some
mild but inconsistent dysmorphic features, such as pes planus, cupped
ears, and undescended testes. Neither patient had signs of an
immunodeficiency. Huang et al. (2012) hypothesized that the ARHGAP4 gene
plays a role in brain function.
*FIELD* RF
1. Demura, M.; Takeda, Y.; Yoneda, T.; Furukawa, K.; Usukura, M.;
Itoh, Y.; Mabuchi, H.: Two novel types of contiguous gene deletion
of the AVPR2 and ARHGAP4 genes in unrelated Japanese kindreds with
nephrogenic diabetes insipidus. Hum. Mutat. 19: 23-29, 2002.
2. Huang, L.; Poke, G.; Gecz, J.; Gibson, K.: A novel contiguous
gene deletion of AVPR2 and ARHGAP4 genes in male dizygotic twins with
nephrogenic diabetes insipidus and intellectual disability. Am. J.
Med. Genet. 158A: 2511-2518, 2012.
3. Schoneberg, T.; Pasel, K.; von Baehr, V.; Schulz, A.; Volk, H.-D.;
Gudermann, T.; Filler, G.: Compound deletion of the rhoGAP C1 and
V2 vasopressin receptor genes in a patient with nephrogenic diabetes
insipidus. Hum. Mutat. 14: 163-174, 1999.
4. Tribioli, C.; Droetto, S.; Bione, S.; Cesareni, G.; Torrisi, M.
R.; Lotti, L. V.; Lanfrancone, L.; Toniolo, D.; Pelicci, P.: An X
chromosome-linked gene encoding a protein with characteristics of
a rhoGAP predominantly expressed in hematopoietic cells. Proc. Nat.
Acad. Sci. 93: 695-699, 1996.
*FIELD* CN
Cassandra L. Kniffin - updated: 12/17/2013
Victor A. McKusick - updated: 1/15/2002
Ada Hamosh - updated: 9/20/1999
*FIELD* CD
Victor A. McKusick: 2/9/1996
*FIELD* ED
carol: 12/18/2013
ckniffin: 12/17/2013
wwang: 8/17/2010
carol: 10/16/2006
ckniffin: 8/3/2005
carol: 3/27/2002
carol: 1/19/2002
mcapotos: 1/17/2002
terry: 1/15/2002
psherman: 12/6/1999
carol: 9/23/1999
carol: 9/21/1999
terry: 9/20/1999
alopez: 5/18/1998
terry: 5/24/1996
mark: 2/9/1996
*RECORD*
*FIELD* NO
300023
*FIELD* TI
*300023 RHO GTPase-ACTIVATING PROTEIN 4; ARHGAP4
;;RHO GAP HEMATOPOIETIC PROTEIN C1; RGC1;;
read moreGTPase-ACTIVATING PROTEIN, RHO, 4; RHOGAP4
*FIELD* TX
CLONING
By constructing a detailed transcription map of the region of 2 Mb in
distal Xq28, Tribioli et al. (1996) identified a large number of novel
genes, including ARHGAP4, which they designated RGC1. RGC1 encodes a
cytoplasmic protein of 115 kD preferentially expressed in hematopoietic
cells and containing SH3 and GAP homologous regions. It appears to be a
member of the group of signaling proteins involved in regulation of the
small GTP-binding proteins of the RAS superfamily. Its localization in a
narrow cytoplasmic region just below the plasma membrane (as indicated
by immunocytochemistry on human cell lines using a polyclonal antibody)
and its inhibitory effect on stress fiber organization indicated to the
authors that the protein may downregulate RHO-like GTPase in
hematopoietic cells. The gene is approximately 20 kb long and encodes an
mRNA of 3.5 kb. The protein contains 946 amino acids.
CYTOGENETICS
Schoneberg et al. (1999) described a 16-year-old male with nephrogenic
diabetes insipidus (NDI; 304800) diagnosed at 8 months of age who had a
21.5-kb deletion encompassing the entire AVPR2 gene (300538) and most of
the RGC1 gene. Besides the symptoms of NDI, the patient had no major
morphologic abnormalities as determined by physical examination,
radiography, ultrasound, and CT scan. Blood chemical, enzyme, and
hormone values over a period of 16 years showed no deviations from
normal ranges. Close attention was paid to hematopoietic and immunologic
abnormalities because of the predominant expression pattern of the RGC1
gene in hematopoietic cells, but no abnormalities were observed.
Schoneberg et al. (1999) postulated that the loss of RGC1 function is
most likely compensated for by other members of the GAP family.
Demura et al. (2002) reported 2 novel types of contiguous gene deletion
of both the AVPR2 gene and the ARHGAP4 gene in unrelated Japanese
kindreds with NDI. They discussed the mechanism of each of the
deletions, which were 21.3 and 26.3 kb, respectively. Both patients,
despite lacking ARHGAP4, had no morphologic, clinical, or laboratory
abnormalities except for those usually found in patients with NDI.
Huang et al. (2012) reported 2 male dizygotic twins with a 17.9-kb
deletion of Xq28 encompassing the entire AVPR2 gene and extending into
intron 7 of the ARHGAP4 gene. The mother was a carrier of the deletion.
The boys showed significant failure to thrive in infancy and were
diagnosed with nephrogenic diabetes insipidus at 27 months of age. Both
showed delayed psychomotor development. At age 11 years, they had
intellectual impairment (IQ in the fifties), short stature, and some
mild but inconsistent dysmorphic features, such as pes planus, cupped
ears, and undescended testes. Neither patient had signs of an
immunodeficiency. Huang et al. (2012) hypothesized that the ARHGAP4 gene
plays a role in brain function.
*FIELD* RF
1. Demura, M.; Takeda, Y.; Yoneda, T.; Furukawa, K.; Usukura, M.;
Itoh, Y.; Mabuchi, H.: Two novel types of contiguous gene deletion
of the AVPR2 and ARHGAP4 genes in unrelated Japanese kindreds with
nephrogenic diabetes insipidus. Hum. Mutat. 19: 23-29, 2002.
2. Huang, L.; Poke, G.; Gecz, J.; Gibson, K.: A novel contiguous
gene deletion of AVPR2 and ARHGAP4 genes in male dizygotic twins with
nephrogenic diabetes insipidus and intellectual disability. Am. J.
Med. Genet. 158A: 2511-2518, 2012.
3. Schoneberg, T.; Pasel, K.; von Baehr, V.; Schulz, A.; Volk, H.-D.;
Gudermann, T.; Filler, G.: Compound deletion of the rhoGAP C1 and
V2 vasopressin receptor genes in a patient with nephrogenic diabetes
insipidus. Hum. Mutat. 14: 163-174, 1999.
4. Tribioli, C.; Droetto, S.; Bione, S.; Cesareni, G.; Torrisi, M.
R.; Lotti, L. V.; Lanfrancone, L.; Toniolo, D.; Pelicci, P.: An X
chromosome-linked gene encoding a protein with characteristics of
a rhoGAP predominantly expressed in hematopoietic cells. Proc. Nat.
Acad. Sci. 93: 695-699, 1996.
*FIELD* CN
Cassandra L. Kniffin - updated: 12/17/2013
Victor A. McKusick - updated: 1/15/2002
Ada Hamosh - updated: 9/20/1999
*FIELD* CD
Victor A. McKusick: 2/9/1996
*FIELD* ED
carol: 12/18/2013
ckniffin: 12/17/2013
wwang: 8/17/2010
carol: 10/16/2006
ckniffin: 8/3/2005
carol: 3/27/2002
carol: 1/19/2002
mcapotos: 1/17/2002
terry: 1/15/2002
psherman: 12/6/1999
carol: 9/23/1999
carol: 9/21/1999
terry: 9/20/1999
alopez: 5/18/1998
terry: 5/24/1996
mark: 2/9/1996