Full text data of ANKFY1
ANKFY1
(ANKHZN, KIAA1255)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ankyrin repeat and FYVE domain-containing protein 1 (Ankyrin repeats hooked to a zinc finger motif)
Ankyrin repeat and FYVE domain-containing protein 1 (Ankyrin repeats hooked to a zinc finger motif)
UniProt
Q9P2R3
ID ANFY1_HUMAN Reviewed; 1169 AA.
AC Q9P2R3; A8KA65; Q5RKV4; Q9ULG5;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Ankyrin repeat and FYVE domain-containing protein 1;
DE AltName: Full=Ankyrin repeats hooked to a zinc finger motif;
GN Name=ANKFY1; Synonyms=ANKHZN, KIAA1255;
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), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10940552; DOI=10.1016/S0378-1119(00)00247-X;
RA Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K.,
RA Gejyo F., Arakawa M., Shimizu N., Kuwano R.;
RT "Characterization and chromosomal mapping of a novel human gene,
RT ANKHZN.";
RL Gene 253:151-160(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-458 (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [8]
RP PROTEIN SEQUENCE OF 2-11; 145-151 AND 924-931, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
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).
CC -!- INTERACTION:
CC P60520:GABARAPL2; NbExp=2; IntAct=EBI-2513908, EBI-720116;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein. Note=Also associated with endosomal membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2R3-2; Sequence=VSP_035607;
CC Name=4;
CC IsoId=Q9P2R3-4; Sequence=VSP_041447;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: High expression in whole adult brain and
CC intermediate expression in all other tissues and specific brain
CC regions examined, including fetal brain.
CC -!- SIMILARITY: Contains 21 ANK repeats.
CC -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52308.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=BAA86569.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB037360; BAA90300.1; -; mRNA.
DR EMBL; AB033081; BAA86569.2; ALT_INIT; mRNA.
DR EMBL; AK292930; BAF85619.1; -; mRNA.
DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90448.1; -; Genomic_DNA.
DR EMBL; BC052308; AAH52308.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001244928.1; NM_001257999.1.
DR RefSeq; NP_057460.3; NM_016376.3.
DR RefSeq; XP_005256736.1; XM_005256679.1.
DR UniGene; Hs.696087; -.
DR ProteinModelPortal; Q9P2R3; -.
DR SMR; Q9P2R3; 53-193, 219-1074, 1100-1163.
DR DIP; DIP-46068N; -.
DR IntAct; Q9P2R3; 13.
DR STRING; 9606.ENSP00000343362; -.
DR PhosphoSite; Q9P2R3; -.
DR DMDM; 33514905; -.
DR PaxDb; Q9P2R3; -.
DR PRIDE; Q9P2R3; -.
DR DNASU; 51479; -.
DR Ensembl; ENST00000341657; ENSP00000343362; ENSG00000185722.
DR Ensembl; ENST00000433651; ENSP00000416005; ENSG00000185722.
DR Ensembl; ENST00000570535; ENSP00000459943; ENSG00000185722.
DR Ensembl; ENST00000574367; ENSP00000459775; ENSG00000185722.
DR GeneID; 51479; -.
DR KEGG; hsa:51479; -.
DR UCSC; uc002fxq.1; human.
DR CTD; 51479; -.
DR GeneCards; GC17M004013; -.
DR H-InvDB; HIX0013439; -.
DR H-InvDB; HIX0173682; -.
DR HGNC; HGNC:20763; ANKFY1.
DR HPA; HPA024513; -.
DR HPA; HPA024522; -.
DR MIM; 607927; gene.
DR neXtProt; NX_Q9P2R3; -.
DR PharmGKB; PA134984226; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000022583; -.
DR HOVERGEN; HBG050501; -.
DR InParanoid; Q9P2R3; -.
DR OMA; WSLLHKA; -.
DR OrthoDB; EOG7327MZ; -.
DR ChiTaRS; ANKFY1; human.
DR GeneWiki; ANKFY1; -.
DR GenomeRNAi; 51479; -.
DR NextBio; 55128; -.
DR PRO; PR:Q9P2R3; -.
DR ArrayExpress; Q9P2R3; -.
DR Bgee; Q9P2R3; -.
DR CleanEx; HS_ANKFY1; -.
DR Genevestigator; Q9P2R3; -.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR000210; BTB/POZ-like.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR013069; BTB_POZ.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01363; FYVE; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 21.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF48403; SSF48403; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endosome; Membrane;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1169 Ankyrin repeat and FYVE domain-containing
FT protein 1.
FT /FTId=PRO_0000066890.
FT DOMAIN 68 130 BTB.
FT REPEAT 217 247 ANK 1.
FT REPEAT 255 284 ANK 2.
FT REPEAT 288 317 ANK 3.
FT REPEAT 322 362 ANK 4.
FT REPEAT 366 396 ANK 5.
FT REPEAT 490 519 ANK 6.
FT REPEAT 542 572 ANK 7.
FT REPEAT 588 617 ANK 8.
FT REPEAT 621 650 ANK 9.
FT REPEAT 654 683 ANK 10.
FT REPEAT 687 716 ANK 11.
FT REPEAT 724 753 ANK 12.
FT REPEAT 769 798 ANK 13.
FT REPEAT 802 832 ANK 14.
FT REPEAT 836 865 ANK 15.
FT REPEAT 870 899 ANK 16.
FT REPEAT 905 934 ANK 17.
FT REPEAT 938 967 ANK 18.
FT REPEAT 971 1001 ANK 19.
FT REPEAT 1005 1037 ANK 20.
FT REPEAT 1043 1072 ANK 21.
FT ZN_FING 1104 1164 FYVE-type.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 4 MAEE -> MPTPRDCGRLRSRAGRSRAGAACSRGAPRAARE
FT ALDCRRCRDAGGK (in isoform 4).
FT /FTId=VSP_041447.
FT VAR_SEQ 650 650 V -> VS (in isoform 2).
FT /FTId=VSP_035607.
FT CONFLICT 48 48 E -> K (in Ref. 1; BAA90300).
FT CONFLICT 115 115 M -> V (in Ref. 1; BAA90300).
FT CONFLICT 207 207 A -> P (in Ref. 1; BAA90300).
FT CONFLICT 235 235 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 270 270 S -> N (in Ref. 1; BAA90300).
FT CONFLICT 283 291 DMVDKSGWS -> AWWPRVLE (in Ref. 1;
FT BAA90300).
FT CONFLICT 299 300 RG -> E (in Ref. 1; BAA90300).
FT CONFLICT 322 322 A -> C (in Ref. 1; BAA90300).
FT CONFLICT 336 337 KK -> RN (in Ref. 1; BAA90300).
FT CONFLICT 379 379 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 385 385 Q -> H (in Ref. 1; BAA90300).
FT CONFLICT 645 645 Q -> R (in Ref. 1; BAA90300).
FT CONFLICT 652 654 TQD -> PQA (in Ref. 1; BAA90300).
FT CONFLICT 687 687 K -> E (in Ref. 1; BAA90300).
FT CONFLICT 713 713 D -> G (in Ref. 1; BAA90300).
FT CONFLICT 784 784 Missing (in Ref. 1; BAA90300).
FT CONFLICT 795 795 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 798 798 A -> P (in Ref. 1; BAA90300).
FT CONFLICT 807 807 I -> C (in Ref. 1; BAA90300).
FT CONFLICT 827 829 DIH -> ISS (in Ref. 1; BAA90300).
FT CONFLICT 835 835 R -> K (in Ref. 1; BAA90300).
FT CONFLICT 849 849 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 860 860 E -> G (in Ref. 1; BAA90300).
FT CONFLICT 874 874 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 889 889 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 901 901 V -> A (in Ref. 1; BAA90300).
FT CONFLICT 905 905 S -> P (in Ref. 1; BAA90300).
FT CONFLICT 913 913 A -> V (in Ref. 1; BAA90300).
FT CONFLICT 916 916 A -> E (in Ref. 1; BAA90300).
FT CONFLICT 933 933 N -> T (in Ref. 1; BAA90300).
FT CONFLICT 940 940 Q -> K (in Ref. 1; BAA90300).
FT CONFLICT 949 949 Q -> E (in Ref. 1; BAA90300).
FT CONFLICT 962 962 G -> A (in Ref. 1; BAA90300).
FT CONFLICT 1120 1120 T -> A (in Ref. 1; BAA90300).
FT CONFLICT 1157 1157 N -> T (in Ref. 1; BAA90300).
SQ SEQUENCE 1169 AA; 128399 MW; 589297CA4ACDDB56 CRC64;
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD
LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW
IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG
DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP
NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV
NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN
GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS
VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG
PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW
GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP
FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN
AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI
FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK
EIPIIKFDLN KPVRVCNICF DVLTLGGVS
//
ID ANFY1_HUMAN Reviewed; 1169 AA.
AC Q9P2R3; A8KA65; Q5RKV4; Q9ULG5;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 04-AUG-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Ankyrin repeat and FYVE domain-containing protein 1;
DE AltName: Full=Ankyrin repeats hooked to a zinc finger motif;
GN Name=ANKFY1; Synonyms=ANKHZN, KIAA1255;
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), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=10940552; DOI=10.1016/S0378-1119(00)00247-X;
RA Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K.,
RA Gejyo F., Arakawa M., Shimizu N., Kuwano R.;
RT "Characterization and chromosomal mapping of a novel human gene,
RT ANKHZN.";
RL Gene 253:151-160(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-458 (ISOFORM 1).
RC TISSUE=Mammary gland;
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 [8]
RP PROTEIN SEQUENCE OF 2-11; 145-151 AND 924-931, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [9]
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).
CC -!- INTERACTION:
CC P60520:GABARAPL2; NbExp=2; IntAct=EBI-2513908, EBI-720116;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC membrane protein. Note=Also associated with endosomal membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9P2R3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2R3-2; Sequence=VSP_035607;
CC Name=4;
CC IsoId=Q9P2R3-4; Sequence=VSP_041447;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: High expression in whole adult brain and
CC intermediate expression in all other tissues and specific brain
CC regions examined, including fetal brain.
CC -!- SIMILARITY: Contains 21 ANK repeats.
CC -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52308.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC Sequence=BAA86569.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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; AB037360; BAA90300.1; -; mRNA.
DR EMBL; AB033081; BAA86569.2; ALT_INIT; mRNA.
DR EMBL; AK292930; BAF85619.1; -; mRNA.
DR EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90448.1; -; Genomic_DNA.
DR EMBL; BC052308; AAH52308.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001244928.1; NM_001257999.1.
DR RefSeq; NP_057460.3; NM_016376.3.
DR RefSeq; XP_005256736.1; XM_005256679.1.
DR UniGene; Hs.696087; -.
DR ProteinModelPortal; Q9P2R3; -.
DR SMR; Q9P2R3; 53-193, 219-1074, 1100-1163.
DR DIP; DIP-46068N; -.
DR IntAct; Q9P2R3; 13.
DR STRING; 9606.ENSP00000343362; -.
DR PhosphoSite; Q9P2R3; -.
DR DMDM; 33514905; -.
DR PaxDb; Q9P2R3; -.
DR PRIDE; Q9P2R3; -.
DR DNASU; 51479; -.
DR Ensembl; ENST00000341657; ENSP00000343362; ENSG00000185722.
DR Ensembl; ENST00000433651; ENSP00000416005; ENSG00000185722.
DR Ensembl; ENST00000570535; ENSP00000459943; ENSG00000185722.
DR Ensembl; ENST00000574367; ENSP00000459775; ENSG00000185722.
DR GeneID; 51479; -.
DR KEGG; hsa:51479; -.
DR UCSC; uc002fxq.1; human.
DR CTD; 51479; -.
DR GeneCards; GC17M004013; -.
DR H-InvDB; HIX0013439; -.
DR H-InvDB; HIX0173682; -.
DR HGNC; HGNC:20763; ANKFY1.
DR HPA; HPA024513; -.
DR HPA; HPA024522; -.
DR MIM; 607927; gene.
DR neXtProt; NX_Q9P2R3; -.
DR PharmGKB; PA134984226; -.
DR eggNOG; COG0666; -.
DR HOGENOM; HOG000022583; -.
DR HOVERGEN; HBG050501; -.
DR InParanoid; Q9P2R3; -.
DR OMA; WSLLHKA; -.
DR OrthoDB; EOG7327MZ; -.
DR ChiTaRS; ANKFY1; human.
DR GeneWiki; ANKFY1; -.
DR GenomeRNAi; 51479; -.
DR NextBio; 55128; -.
DR PRO; PR:Q9P2R3; -.
DR ArrayExpress; Q9P2R3; -.
DR Bgee; Q9P2R3; -.
DR CleanEx; HS_ANKFY1; -.
DR Genevestigator; Q9P2R3; -.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 3.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR InterPro; IPR000210; BTB/POZ-like.
DR InterPro; IPR011333; BTB/POZ_fold.
DR InterPro; IPR013069; BTB_POZ.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01363; FYVE; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 21.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF48403; SSF48403; 4.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Endosome; Membrane;
KW Metal-binding; Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1169 Ankyrin repeat and FYVE domain-containing
FT protein 1.
FT /FTId=PRO_0000066890.
FT DOMAIN 68 130 BTB.
FT REPEAT 217 247 ANK 1.
FT REPEAT 255 284 ANK 2.
FT REPEAT 288 317 ANK 3.
FT REPEAT 322 362 ANK 4.
FT REPEAT 366 396 ANK 5.
FT REPEAT 490 519 ANK 6.
FT REPEAT 542 572 ANK 7.
FT REPEAT 588 617 ANK 8.
FT REPEAT 621 650 ANK 9.
FT REPEAT 654 683 ANK 10.
FT REPEAT 687 716 ANK 11.
FT REPEAT 724 753 ANK 12.
FT REPEAT 769 798 ANK 13.
FT REPEAT 802 832 ANK 14.
FT REPEAT 836 865 ANK 15.
FT REPEAT 870 899 ANK 16.
FT REPEAT 905 934 ANK 17.
FT REPEAT 938 967 ANK 18.
FT REPEAT 971 1001 ANK 19.
FT REPEAT 1005 1037 ANK 20.
FT REPEAT 1043 1072 ANK 21.
FT ZN_FING 1104 1164 FYVE-type.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 4 MAEE -> MPTPRDCGRLRSRAGRSRAGAACSRGAPRAARE
FT ALDCRRCRDAGGK (in isoform 4).
FT /FTId=VSP_041447.
FT VAR_SEQ 650 650 V -> VS (in isoform 2).
FT /FTId=VSP_035607.
FT CONFLICT 48 48 E -> K (in Ref. 1; BAA90300).
FT CONFLICT 115 115 M -> V (in Ref. 1; BAA90300).
FT CONFLICT 207 207 A -> P (in Ref. 1; BAA90300).
FT CONFLICT 235 235 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 270 270 S -> N (in Ref. 1; BAA90300).
FT CONFLICT 283 291 DMVDKSGWS -> AWWPRVLE (in Ref. 1;
FT BAA90300).
FT CONFLICT 299 300 RG -> E (in Ref. 1; BAA90300).
FT CONFLICT 322 322 A -> C (in Ref. 1; BAA90300).
FT CONFLICT 336 337 KK -> RN (in Ref. 1; BAA90300).
FT CONFLICT 379 379 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 385 385 Q -> H (in Ref. 1; BAA90300).
FT CONFLICT 645 645 Q -> R (in Ref. 1; BAA90300).
FT CONFLICT 652 654 TQD -> PQA (in Ref. 1; BAA90300).
FT CONFLICT 687 687 K -> E (in Ref. 1; BAA90300).
FT CONFLICT 713 713 D -> G (in Ref. 1; BAA90300).
FT CONFLICT 784 784 Missing (in Ref. 1; BAA90300).
FT CONFLICT 795 795 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 798 798 A -> P (in Ref. 1; BAA90300).
FT CONFLICT 807 807 I -> C (in Ref. 1; BAA90300).
FT CONFLICT 827 829 DIH -> ISS (in Ref. 1; BAA90300).
FT CONFLICT 835 835 R -> K (in Ref. 1; BAA90300).
FT CONFLICT 849 849 N -> D (in Ref. 1; BAA90300).
FT CONFLICT 860 860 E -> G (in Ref. 1; BAA90300).
FT CONFLICT 874 874 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 889 889 F -> S (in Ref. 1; BAA90300).
FT CONFLICT 901 901 V -> A (in Ref. 1; BAA90300).
FT CONFLICT 905 905 S -> P (in Ref. 1; BAA90300).
FT CONFLICT 913 913 A -> V (in Ref. 1; BAA90300).
FT CONFLICT 916 916 A -> E (in Ref. 1; BAA90300).
FT CONFLICT 933 933 N -> T (in Ref. 1; BAA90300).
FT CONFLICT 940 940 Q -> K (in Ref. 1; BAA90300).
FT CONFLICT 949 949 Q -> E (in Ref. 1; BAA90300).
FT CONFLICT 962 962 G -> A (in Ref. 1; BAA90300).
FT CONFLICT 1120 1120 T -> A (in Ref. 1; BAA90300).
FT CONFLICT 1157 1157 N -> T (in Ref. 1; BAA90300).
SQ SEQUENCE 1169 AA; 128399 MW; 589297CA4ACDDB56 CRC64;
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD
LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW
IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG
DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP
NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV
NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN
GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS
VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG
PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW
GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP
FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN
AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI
FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK
EIPIIKFDLN KPVRVCNICF DVLTLGGVS
//
MIM
607927
*RECORD*
*FIELD* NO
607927
*FIELD* TI
*607927 ANKYRIN REPEATS- AND FYVE DOMAIN-CONTAINING PROTEIN 1; ANKFY1
;;ANKYRIN REPEATS HOOKED TO A ZINC FINGER MOTIF; ANKHZN;;
read moreKIAA1255
*FIELD* TX
DESCRIPTION
ANKFY1 contains several protein-interacting domains and shares
significant identity with a number of S. cerevisiae proteins involved in
vesicular trafficking (Kuriyama et al., 2000).
CLONING
Ito et al. (1999) cloned mouse Ankfy1, which they designated Ankhzn. The
deduced 1,184-amino acid protein has an apparent molecular mass of 130
kD. Ankhzn contains an N-terminal coiled-coil domain, a BTB/POZ domain,
17 ankyrin repeats, and a C-terminal zinc finger motif. The ankyrin
repeats are separated into a group of 4 repeats in the N-terminal half
and a group of 13 repeats in the C-terminal half. Ito et al. (1999)
determined that there is a soluble form of Ankhzn and a form that
associates with endosomes.
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned ANKFY1, which they designated
KIAA1255. The deduced protein shares 88% identity with mouse Ankhzn.
RT-PCR ELISA detected high expression in whole adult brain and
intermediate expression in all other tissues and specific brain regions
examined, including fetal brain.
By searching databases for sequences sharing homology with mouse Ankhzn,
followed by PCR, Kuriyama et al. (2000) cloned ANKHZN from a fetal brain
cDNA library. The deduced 1,166 amino acid protein has a calculated
molecular mass of about 128 kD. ANKHZN shares 85% identity with mouse
Ankhzn, and the 2 proteins have the same domain structure. Kuriyama et
al. (2000) noted that the C-terminal zinc finger (FYVE) domain, which
contains 8 potential Zn(2+)-coordinating cysteine residues that bind 2
Zn(2+) ions, is well conserved among proteins related to intracellular
trafficking. Northern blot analysis detected a 7-kb transcript in both
human and mouse brain. RT-PCR detected expression in all tissues
examined. Subcellular fractionation of human kidney recovered ANKHZN in
both the soluble and membrane fractions.
GENE STRUCTURE
Kuriyama et al. (2000) determined that the ANKFY1 gene contains 25
exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (1999) mapped the ANKFY1
gene to chromosome 17. By radiation hybrid analysis and FISH, Kuriyama
et al. (2000) mapped the ANKFY1 gene to chromosome 17p13. Southern blot
analysis indicated that ANKFY1 is a single-copy gene.
*FIELD* RF
1. Ito, K.; Ishii, N.; Miyashita, A.; Tominaga, K.; Kuriyama, H.;
Maruyama, H.; Shirai, M.; Naito, M.; Arakawa, M.; Kuwano, R.: Molecular
cloning of a novel 130-kDa cytoplasmic protein, Ankhzn, containing
ankyrin repeats hooked to a zinc finger motif. Biochem. Biophys.
Res. Commun. 257: 206-213, 1999.
2. Kuriyama, H.; Asakawa, S.; Minoshima, S.; Maruyama, H.; Ishii,
N.; Ito, K.; Gejyo, F.; Arakawa, M.; Shimizu, N.; Kuwano, R.: Characterization
and chromosomal mapping of a novel human gene, ANKHZN. Gene 253:
151-160, 2000.
3. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
*FIELD* CD
Patricia A. Hartz: 6/27/2003
*FIELD* ED
mgross: 06/27/2003
*RECORD*
*FIELD* NO
607927
*FIELD* TI
*607927 ANKYRIN REPEATS- AND FYVE DOMAIN-CONTAINING PROTEIN 1; ANKFY1
;;ANKYRIN REPEATS HOOKED TO A ZINC FINGER MOTIF; ANKHZN;;
read moreKIAA1255
*FIELD* TX
DESCRIPTION
ANKFY1 contains several protein-interacting domains and shares
significant identity with a number of S. cerevisiae proteins involved in
vesicular trafficking (Kuriyama et al., 2000).
CLONING
Ito et al. (1999) cloned mouse Ankfy1, which they designated Ankhzn. The
deduced 1,184-amino acid protein has an apparent molecular mass of 130
kD. Ankhzn contains an N-terminal coiled-coil domain, a BTB/POZ domain,
17 ankyrin repeats, and a C-terminal zinc finger motif. The ankyrin
repeats are separated into a group of 4 repeats in the N-terminal half
and a group of 13 repeats in the C-terminal half. Ito et al. (1999)
determined that there is a soluble form of Ankhzn and a form that
associates with endosomes.
By sequencing clones obtained from a size-fractionated adult brain cDNA
library, Nagase et al. (1999) cloned ANKFY1, which they designated
KIAA1255. The deduced protein shares 88% identity with mouse Ankhzn.
RT-PCR ELISA detected high expression in whole adult brain and
intermediate expression in all other tissues and specific brain regions
examined, including fetal brain.
By searching databases for sequences sharing homology with mouse Ankhzn,
followed by PCR, Kuriyama et al. (2000) cloned ANKHZN from a fetal brain
cDNA library. The deduced 1,166 amino acid protein has a calculated
molecular mass of about 128 kD. ANKHZN shares 85% identity with mouse
Ankhzn, and the 2 proteins have the same domain structure. Kuriyama et
al. (2000) noted that the C-terminal zinc finger (FYVE) domain, which
contains 8 potential Zn(2+)-coordinating cysteine residues that bind 2
Zn(2+) ions, is well conserved among proteins related to intracellular
trafficking. Northern blot analysis detected a 7-kb transcript in both
human and mouse brain. RT-PCR detected expression in all tissues
examined. Subcellular fractionation of human kidney recovered ANKHZN in
both the soluble and membrane fractions.
GENE STRUCTURE
Kuriyama et al. (2000) determined that the ANKFY1 gene contains 25
exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (1999) mapped the ANKFY1
gene to chromosome 17. By radiation hybrid analysis and FISH, Kuriyama
et al. (2000) mapped the ANKFY1 gene to chromosome 17p13. Southern blot
analysis indicated that ANKFY1 is a single-copy gene.
*FIELD* RF
1. Ito, K.; Ishii, N.; Miyashita, A.; Tominaga, K.; Kuriyama, H.;
Maruyama, H.; Shirai, M.; Naito, M.; Arakawa, M.; Kuwano, R.: Molecular
cloning of a novel 130-kDa cytoplasmic protein, Ankhzn, containing
ankyrin repeats hooked to a zinc finger motif. Biochem. Biophys.
Res. Commun. 257: 206-213, 1999.
2. Kuriyama, H.; Asakawa, S.; Minoshima, S.; Maruyama, H.; Ishii,
N.; Ito, K.; Gejyo, F.; Arakawa, M.; Shimizu, N.; Kuwano, R.: Characterization
and chromosomal mapping of a novel human gene, ANKHZN. Gene 253:
151-160, 2000.
3. Nagase, T.; Ishikawa, K.; Kikuno, R.; Hirosawa, M.; Nomura, N.;
Ohara, O.: Prediction of the coding sequences of unidentified human
genes. XV. The complete sequences of 100 new cDNA clones from brain
which code for large proteins in vitro. DNA Res. 6: 337-345, 1999.
*FIELD* CD
Patricia A. Hartz: 6/27/2003
*FIELD* ED
mgross: 06/27/2003