Full text data of F8A1
F8A1
(F8A)
[Confidence: low (only semi-automatic identification from reviews)]
Factor VIII intron 22 protein (CpG island protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Factor VIII intron 22 protein (CpG island protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P23610
ID F8I2_HUMAN Reviewed; 371 AA.
AC P23610; Q5HY66; Q8IXP3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-NOV-2004, sequence version 2.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Factor VIII intron 22 protein;
DE AltName: Full=CpG island protein;
GN Name=F8A1; Synonyms=F8A;
GN and
GN Name=F8A2; Synonyms=F8A;
GN and
GN Name=F8A3; Synonyms=F8A;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2110545; DOI=10.1016/0888-7543(90)90512-S;
RA Levinson B., Kenwrick S., Lakich D., Hammonds G. Jr., Gitschier J.;
RT "A transcribed gene in an intron of the human factor VIII gene.";
RL Genomics 7:1-11(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bagnall R.D., Green P.M., Giannelli F.;
RT "Gene conversion and evolution of Xq28 duplicons involved in recurring
RT inversions causing severe haemophilia A.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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.,
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Not known. Possible housekeeping role.
CC -!- TISSUE SPECIFICITY: Produced abundantly in a wide variety of cell
CC types.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35713.1; Type=Frameshift; Positions=231, 257, 367;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M34677; AAA35713.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY619999; AAT44606.1; -; Genomic_DNA.
DR EMBL; AY620000; AAT44607.1; -; Genomic_DNA.
DR EMBL; AY620001; AAT44608.1; -; Genomic_DNA.
DR EMBL; BX276110; CAH71439.1; -; Genomic_DNA.
DR EMBL; BX682237; CAI41333.1; -; Genomic_DNA.
DR EMBL; BX842559; CAI41669.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72648.1; -; Genomic_DNA.
DR EMBL; BC039693; AAH39693.1; -; mRNA.
DR EMBL; BC071963; AAH71963.1; -; mRNA.
DR PIR; B42832; B42832.
DR RefSeq; NP_001007524.1; NM_001007523.1.
DR RefSeq; NP_001007525.1; NM_001007524.1.
DR RefSeq; NP_036283.2; NM_012151.3.
DR UniGene; Hs.533543; -.
DR UniGene; Hs.731793; -.
DR ProteinModelPortal; P23610; -.
DR SMR; P23610; 146-171.
DR IntAct; P23610; 1.
DR MINT; MINT-4720691; -.
DR PhosphoSite; P23610; -.
DR PaxDb; P23610; -.
DR PRIDE; P23610; -.
DR DNASU; 474384; -.
DR DNASU; 8263; -.
DR Ensembl; ENST00000369445; ENSP00000358454; ENSG00000185990.
DR Ensembl; ENST00000369446; ENSP00000358456; ENSG00000197932.
DR Ensembl; ENST00000369505; ENSP00000358518; ENSG00000198444.
DR Ensembl; ENST00000597478; ENSP00000470422; ENSG00000268835.
DR Ensembl; ENST00000598873; ENSP00000469849; ENSG00000268720.
DR Ensembl; ENST00000599403; ENSP00000470549; ENSG00000268464.
DR GeneID; 474383; -.
DR GeneID; 474384; -.
DR GeneID; 8263; -.
DR KEGG; hsa:474383; -.
DR KEGG; hsa:474384; -.
DR KEGG; hsa:8263; -.
DR UCSC; uc004fmv.3; human.
DR CTD; 474383; -.
DR CTD; 474384; -.
DR CTD; 8263; -.
DR GeneCards; GC0XM154686; -.
DR GeneCards; GC0XP154114; -.
DR GeneCards; GC0XP154611; -.
DR HGNC; HGNC:3547; F8A1.
DR HGNC; HGNC:31849; F8A2.
DR HGNC; HGNC:31850; F8A3.
DR HPA; HPA046960; -.
DR MIM; 305423; gene.
DR neXtProt; NX_P23610; -.
DR PharmGKB; PA27953; -.
DR eggNOG; NOG41279; -.
DR HOGENOM; HOG000232189; -.
DR HOVERGEN; HBG005629; -.
DR InParanoid; P23610; -.
DR OMA; QRLVCPA; -.
DR OrthoDB; EOG7HTHHH; -.
DR ChiTaRS; F8A3; human.
DR GeneWiki; F8A1; -.
DR NextBio; 111709; -.
DR Bgee; P23610; -.
DR CleanEx; HS_F8A1; -.
DR CleanEx; HS_F8A2; -.
DR Genevestigator; P23610; -.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 371 Factor VIII intron 22 protein.
FT /FTId=PRO_0000087159.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 105 107 RQR -> PA (in Ref. 1; AAA35713).
SQ SEQUENCE 371 AA; 39103 MW; 0E230A1978FAB59D CRC64;
MAAAAAGLGG GGAGPGPEAG DFLARYRLVS NKLKKRFLRK PNVAEAGEQF GQLGRELRAQ
ECLPYAAWCQ LAVARCQQAL FHGPGEALAL TEAARLFLRQ ERDARQRLVC PAAYGEPLQA
AASALGAAVR LHLELGQPAA AAALCLELAA ALRDLGQPAA AAGHFQRAAQ LQLPQLPLAA
LQALGEAASC QLLARDYTGA LAVFTRMQRL AREHGSHPVQ SLPPPPPPAP QPGPGATPAL
PAALLPPNSG SAAPSPAALG AFSDVLVRCE VSRVLLLLLL QPPPAKLLPE HAQTLEKYSW
EAFDSHGQES SGQLPEELFL LLQSLVMATH EKDTEAIKSL QVEMWPLLTA EQNHLLHLVL
QETISPSGQG V
//
ID F8I2_HUMAN Reviewed; 371 AA.
AC P23610; Q5HY66; Q8IXP3;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-NOV-2004, sequence version 2.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=Factor VIII intron 22 protein;
DE AltName: Full=CpG island protein;
GN Name=F8A1; Synonyms=F8A;
GN and
GN Name=F8A2; Synonyms=F8A;
GN and
GN Name=F8A3; Synonyms=F8A;
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 [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=2110545; DOI=10.1016/0888-7543(90)90512-S;
RA Levinson B., Kenwrick S., Lakich D., Hammonds G. Jr., Gitschier J.;
RT "A transcribed gene in an intron of the human factor VIII gene.";
RL Genomics 7:1-11(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bagnall R.D., Green P.M., Giannelli F.;
RT "Gene conversion and evolution of Xq28 duplicons involved in recurring
RT inversions causing severe haemophilia A.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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.,
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Not known. Possible housekeeping role.
CC -!- TISSUE SPECIFICITY: Produced abundantly in a wide variety of cell
CC types.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35713.1; Type=Frameshift; Positions=231, 257, 367;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M34677; AAA35713.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY619999; AAT44606.1; -; Genomic_DNA.
DR EMBL; AY620000; AAT44607.1; -; Genomic_DNA.
DR EMBL; AY620001; AAT44608.1; -; Genomic_DNA.
DR EMBL; BX276110; CAH71439.1; -; Genomic_DNA.
DR EMBL; BX682237; CAI41333.1; -; Genomic_DNA.
DR EMBL; BX842559; CAI41669.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72648.1; -; Genomic_DNA.
DR EMBL; BC039693; AAH39693.1; -; mRNA.
DR EMBL; BC071963; AAH71963.1; -; mRNA.
DR PIR; B42832; B42832.
DR RefSeq; NP_001007524.1; NM_001007523.1.
DR RefSeq; NP_001007525.1; NM_001007524.1.
DR RefSeq; NP_036283.2; NM_012151.3.
DR UniGene; Hs.533543; -.
DR UniGene; Hs.731793; -.
DR ProteinModelPortal; P23610; -.
DR SMR; P23610; 146-171.
DR IntAct; P23610; 1.
DR MINT; MINT-4720691; -.
DR PhosphoSite; P23610; -.
DR PaxDb; P23610; -.
DR PRIDE; P23610; -.
DR DNASU; 474384; -.
DR DNASU; 8263; -.
DR Ensembl; ENST00000369445; ENSP00000358454; ENSG00000185990.
DR Ensembl; ENST00000369446; ENSP00000358456; ENSG00000197932.
DR Ensembl; ENST00000369505; ENSP00000358518; ENSG00000198444.
DR Ensembl; ENST00000597478; ENSP00000470422; ENSG00000268835.
DR Ensembl; ENST00000598873; ENSP00000469849; ENSG00000268720.
DR Ensembl; ENST00000599403; ENSP00000470549; ENSG00000268464.
DR GeneID; 474383; -.
DR GeneID; 474384; -.
DR GeneID; 8263; -.
DR KEGG; hsa:474383; -.
DR KEGG; hsa:474384; -.
DR KEGG; hsa:8263; -.
DR UCSC; uc004fmv.3; human.
DR CTD; 474383; -.
DR CTD; 474384; -.
DR CTD; 8263; -.
DR GeneCards; GC0XM154686; -.
DR GeneCards; GC0XP154114; -.
DR GeneCards; GC0XP154611; -.
DR HGNC; HGNC:3547; F8A1.
DR HGNC; HGNC:31849; F8A2.
DR HGNC; HGNC:31850; F8A3.
DR HPA; HPA046960; -.
DR MIM; 305423; gene.
DR neXtProt; NX_P23610; -.
DR PharmGKB; PA27953; -.
DR eggNOG; NOG41279; -.
DR HOGENOM; HOG000232189; -.
DR HOVERGEN; HBG005629; -.
DR InParanoid; P23610; -.
DR OMA; QRLVCPA; -.
DR OrthoDB; EOG7HTHHH; -.
DR ChiTaRS; F8A3; human.
DR GeneWiki; F8A1; -.
DR NextBio; 111709; -.
DR Bgee; P23610; -.
DR CleanEx; HS_F8A1; -.
DR CleanEx; HS_F8A2; -.
DR Genevestigator; P23610; -.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR011990; TPR-like_helical.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 371 Factor VIII intron 22 protein.
FT /FTId=PRO_0000087159.
FT MOD_RES 2 2 N-acetylalanine.
FT CONFLICT 105 107 RQR -> PA (in Ref. 1; AAA35713).
SQ SEQUENCE 371 AA; 39103 MW; 0E230A1978FAB59D CRC64;
MAAAAAGLGG GGAGPGPEAG DFLARYRLVS NKLKKRFLRK PNVAEAGEQF GQLGRELRAQ
ECLPYAAWCQ LAVARCQQAL FHGPGEALAL TEAARLFLRQ ERDARQRLVC PAAYGEPLQA
AASALGAAVR LHLELGQPAA AAALCLELAA ALRDLGQPAA AAGHFQRAAQ LQLPQLPLAA
LQALGEAASC QLLARDYTGA LAVFTRMQRL AREHGSHPVQ SLPPPPPPAP QPGPGATPAL
PAALLPPNSG SAAPSPAALG AFSDVLVRCE VSRVLLLLLL QPPPAKLLPE HAQTLEKYSW
EAFDSHGQES SGQLPEELFL LLQSLVMATH EKDTEAIKSL QVEMWPLLTA EQNHLLHLVL
QETISPSGQG V
//
MIM
305423
*RECORD*
*FIELD* NO
305423
*FIELD* TI
*305423 FACTOR VIII-ASSOCIATED GENE 1; F8A
;;DXS522E;;
HAP40
*FIELD* TX
CLONING
Levinson et al. (1990) found a curious example of a gene within a gene.
read moreWhile looking for transcripts from the Xq28 region, they found one that
hybridized to a region in exon 22 of the factor VIII gene (F8; 300841).
The transcribed region was in reverse orientation to the F8 exons and
was contained entirely within intron 22. The gene is small (less than 2
kb), contains no introns, and is G-C rich. Computer analysis of the
sequence suggested that it codes for a protein, with the complication
that codon usage analysis suggested a frameshift halfway through the
gene. The transcript cDNA also bound to mouse, monkey, and rat genomic
DNA in a 'zoo blot.' Probably significantly, human intron 22 is
hypomethylated on the active X and methylated on the inactive X. Inaba
et al. (1990) described an MspI RFLP in intron 22 of the F8 gene.
Japanese showed 45% heterozygosity and Asian Indians showed 13%;
polymorphism was not found in American blacks or Caucasians. In the
mouse, Levinson et al. (1992) found that the F8a gene has no introns and
codes for 380 amino acids with 85% identity to the predicted human
sequence. The murine gene is linked to the factor VIII locus, although
physical mapping suggests that it lies outside the factor VIII gene.
Like the human gene, the mouse F8a gene is highly expressed in a wide
variety of tissues.
GENE FUNCTION
Peters and Ross (2001) showed that huntingtin (613004), the protein that
is mutant in Huntington disease (HD; 143100), copurifies with a single
novel 40-kD protein termed HAP40. They showed that HAP40 is encoded by
the open reading frame F8A gene located within intron 22 of the factor
VIII gene. Recombinant HAP40 is cytoplasmic in the presence of
huntingtin but is actively targeted to the nucleus in the absence of
huntingtin. These data indicated that HAP40 is likely to contribute to
the function of normal huntingtin and is a candidate for involvement in
the aberrant nuclear localization of mutant huntingtin found in
degenerating neurons in Huntington disease.
*FIELD* RF
1. Inaba, H.; Fujimaki, M.; Kazazian, H. H., Jr.; Antonarakis, S.
E.: MspI polymorphic site in intron 22 of the factor VIII gene in
the Japanese population. Hum. Genet. 84: 214-215, 1990.
2. Levinson, B.; Bermingham, J. R., Jr.; Metzenberg, A.; Kenwrick,
S.; Chapman, V.; Gitschier, J.: Sequence of the human factor VIII-associated
gene is conserved in mouse. Genomics 13: 862-865, 1992.
3. Levinson, B.; Kenwrick, S.; Lakich, D.; Hammonds, G.; Gitschier,
J.: A transcribed gene in an intron of the human factor VIII gene. Genomics 7:
1-11, 1990.
4. Peters, M. F.; Ross, C. A.: Isolation of a 40-kDa huntingtin-associated
protein. J. Biol. Chem. 276: 3188-3194, 2001.
*FIELD* CN
Victor A. McKusick - updated: 4/12/2001
*FIELD* CD
Victor A. McKusick: 7/2/1992
*FIELD* ED
carol: 04/07/2011
carol: 9/15/2009
alopez: 9/8/2006
mcapotos: 4/24/2001
mcapotos: 4/18/2001
terry: 4/12/2001
alopez: 1/18/2000
alopez: 1/17/2000
carol: 11/10/1992
carol: 8/31/1992
carol: 7/21/1992
carol: 7/2/1992
*RECORD*
*FIELD* NO
305423
*FIELD* TI
*305423 FACTOR VIII-ASSOCIATED GENE 1; F8A
;;DXS522E;;
HAP40
*FIELD* TX
CLONING
Levinson et al. (1990) found a curious example of a gene within a gene.
read moreWhile looking for transcripts from the Xq28 region, they found one that
hybridized to a region in exon 22 of the factor VIII gene (F8; 300841).
The transcribed region was in reverse orientation to the F8 exons and
was contained entirely within intron 22. The gene is small (less than 2
kb), contains no introns, and is G-C rich. Computer analysis of the
sequence suggested that it codes for a protein, with the complication
that codon usage analysis suggested a frameshift halfway through the
gene. The transcript cDNA also bound to mouse, monkey, and rat genomic
DNA in a 'zoo blot.' Probably significantly, human intron 22 is
hypomethylated on the active X and methylated on the inactive X. Inaba
et al. (1990) described an MspI RFLP in intron 22 of the F8 gene.
Japanese showed 45% heterozygosity and Asian Indians showed 13%;
polymorphism was not found in American blacks or Caucasians. In the
mouse, Levinson et al. (1992) found that the F8a gene has no introns and
codes for 380 amino acids with 85% identity to the predicted human
sequence. The murine gene is linked to the factor VIII locus, although
physical mapping suggests that it lies outside the factor VIII gene.
Like the human gene, the mouse F8a gene is highly expressed in a wide
variety of tissues.
GENE FUNCTION
Peters and Ross (2001) showed that huntingtin (613004), the protein that
is mutant in Huntington disease (HD; 143100), copurifies with a single
novel 40-kD protein termed HAP40. They showed that HAP40 is encoded by
the open reading frame F8A gene located within intron 22 of the factor
VIII gene. Recombinant HAP40 is cytoplasmic in the presence of
huntingtin but is actively targeted to the nucleus in the absence of
huntingtin. These data indicated that HAP40 is likely to contribute to
the function of normal huntingtin and is a candidate for involvement in
the aberrant nuclear localization of mutant huntingtin found in
degenerating neurons in Huntington disease.
*FIELD* RF
1. Inaba, H.; Fujimaki, M.; Kazazian, H. H., Jr.; Antonarakis, S.
E.: MspI polymorphic site in intron 22 of the factor VIII gene in
the Japanese population. Hum. Genet. 84: 214-215, 1990.
2. Levinson, B.; Bermingham, J. R., Jr.; Metzenberg, A.; Kenwrick,
S.; Chapman, V.; Gitschier, J.: Sequence of the human factor VIII-associated
gene is conserved in mouse. Genomics 13: 862-865, 1992.
3. Levinson, B.; Kenwrick, S.; Lakich, D.; Hammonds, G.; Gitschier,
J.: A transcribed gene in an intron of the human factor VIII gene. Genomics 7:
1-11, 1990.
4. Peters, M. F.; Ross, C. A.: Isolation of a 40-kDa huntingtin-associated
protein. J. Biol. Chem. 276: 3188-3194, 2001.
*FIELD* CN
Victor A. McKusick - updated: 4/12/2001
*FIELD* CD
Victor A. McKusick: 7/2/1992
*FIELD* ED
carol: 04/07/2011
carol: 9/15/2009
alopez: 9/8/2006
mcapotos: 4/24/2001
mcapotos: 4/18/2001
terry: 4/12/2001
alopez: 1/18/2000
alopez: 1/17/2000
carol: 11/10/1992
carol: 8/31/1992
carol: 7/21/1992
carol: 7/2/1992