Full text data of ALDH16A1
ALDH16A1
[Confidence: high (present in two of the MS resources)]
Aldehyde dehydrogenase family 16 member A1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Aldehyde dehydrogenase family 16 member A1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00217920
IPI00217920 Hypothetical protein MGC10204 oxidoreductase activity, metabolism, FLJ00209 protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00217920 Hypothetical protein MGC10204 oxidoreductase activity, metabolism, FLJ00209 protein soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q8IZ83
ID A16A1_HUMAN Reviewed; 802 AA.
AC Q8IZ83; B4DLQ1; C9JBH6; Q86YF0; Q8IYL4; Q8TEI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 2.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Aldehyde dehydrogenase family 16 member A1;
GN Name=ALDH16A1;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP VAL-227.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-227.
RC TISSUE=Lymph, Skin, and Uterus;
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 INTERACTION WITH SPG21.
RX PubMed=19184135; DOI=10.1007/s10048-009-0172-6;
RA Hanna M.C., Blackstone C.;
RT "Interaction of the SPG21 protein ACP33/maspardin with the aldehyde
RT dehydrogenase ALDH16A1.";
RL Neurogenetics 10:217-228(2009).
RN [6]
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 -!- SUBUNIT: Interacts with SPG21.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZ83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ83-2; Sequence=VSP_029982, VSP_029983;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8IZ83-3; Sequence=VSP_043280;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC -!- CAUTION: The active site cysteine and glutamate residues are not
CC conserved in this protein. Its activity is therefore unsure.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35641.1; Type=Erroneous initiation;
CC Sequence=BAB84962.1; Type=Erroneous translation; Note=Wrong choice of frame;
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; AK074136; BAB84962.1; ALT_SEQ; mRNA.
DR EMBL; AK297101; BAG59613.1; -; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014895; AAH14895.2; -; mRNA.
DR EMBL; BC035641; AAH35641.1; ALT_INIT; mRNA.
DR EMBL; BC042142; AAH42142.1; -; mRNA.
DR RefSeq; NP_001138868.1; NM_001145396.1.
DR RefSeq; NP_699160.2; NM_153329.3.
DR UniGene; Hs.719998; -.
DR ProteinModelPortal; Q8IZ83; -.
DR SMR; Q8IZ83; 17-494, 528-791.
DR IntAct; Q8IZ83; 7.
DR MINT; MINT-4999900; -.
DR STRING; 9606.ENSP00000293350; -.
DR PhosphoSite; Q8IZ83; -.
DR DMDM; 269849532; -.
DR PaxDb; Q8IZ83; -.
DR PRIDE; Q8IZ83; -.
DR Ensembl; ENST00000293350; ENSP00000293350; ENSG00000161618.
DR Ensembl; ENST00000455361; ENSP00000410142; ENSG00000161618.
DR GeneID; 126133; -.
DR KEGG; hsa:126133; -.
DR UCSC; uc002pnt.3; human.
DR CTD; 126133; -.
DR GeneCards; GC19P049958; -.
DR H-InvDB; HIX0202728; -.
DR HGNC; HGNC:28114; ALDH16A1.
DR MIM; 613358; gene.
DR neXtProt; NX_Q8IZ83; -.
DR PharmGKB; PA134903503; -.
DR eggNOG; COG1012; -.
DR HOGENOM; HOG000112558; -.
DR HOVERGEN; HBG069396; -.
DR InParanoid; Q8IZ83; -.
DR OMA; QESVWDE; -.
DR OrthoDB; EOG7Q2N4V; -.
DR PhylomeDB; Q8IZ83; -.
DR GeneWiki; ALDH16A1; -.
DR GenomeRNAi; 126133; -.
DR NextBio; 81700; -.
DR PRO; PR:Q8IZ83; -.
DR ArrayExpress; Q8IZ83; -.
DR Bgee; Q8IZ83; -.
DR CleanEx; HS_ALDH16A1; -.
DR Genevestigator; Q8IZ83; -.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 2.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR011408; Aldehyde_DH.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; SSF53720; 2.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Polymorphism;
KW Reference proteome.
FT CHAIN 1 802 Aldehyde dehydrogenase family 16 member
FT A1.
FT /FTId=PRO_0000312986.
FT VAR_SEQ 254 308 EGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGV
FT VDAAWSDRGPGGLR -> VPSGQGSWRNAAGGRKAPPAAEL
FT GGVPRKGVPFDGAWRESVRSWAWRWGRSRCCC (in
FT isoform 2).
FT /FTId=VSP_029982.
FT VAR_SEQ 254 304 Missing (in isoform 3).
FT /FTId=VSP_043280.
FT VAR_SEQ 309 802 Missing (in isoform 2).
FT /FTId=VSP_029983.
FT VARIANT 110 110 E -> K (in dbSNP:rs3745312).
FT /FTId=VAR_037638.
FT VARIANT 227 227 L -> V (in dbSNP:rs1320303).
FT /FTId=VAR_037639.
SQ SEQUENCE 802 AA; 85127 MW; 2820628CD0EF5823 CRC64;
MAATRAGPRA REIFTSLEYG PVPESHACAL AWLDTQDRCL GHYVNGKWLK PEHRNSVPCQ
DPITGENLAS CLQAQAEDVA AAVEAARMAF KGWSAHPGVV RAQHLTRLAE VIQKHQRLLW
TLESLVTGRA VREVRDGDVQ LAQQLLHYHA IQASTQEEAL AGWEPMGVIG LILPPTFSFL
EMMWRICPAL AVGCTVVALV PPASPAPLLL AQLAGELGPF PGILNVLSGP ASLVPILASQ
PGIRKVAFCG APEEGRALRR SLAGECAELG LALGTESLLL LTDTADVDSA VEGVVDAAWS
DRGPGGLRLL IQESVWDEAM RRLQERMGRL RSGRGLDGAV DMGARGAAAC DLVQRFVREA
QSQGAQVFQA GDVPSERPFY PPTLVSNLPP ASPCAQVEVP WPVVVASPFR TAKEALLVAN
GTPRGGSASV WSERLGQALE LGYGLQVGTV WINAHGLRDP SVPTGGCKES GCSWHGGPDG
LYEYLRPSGT PARLSCLSKN LNYDTFGLAV PSTLPAGPEI GPSPAPPYGL FVGGRFQAPG
ARSSRPIRDS SGNLHGYVAE GGAKDIRGAV EAAHQAFPGW AGQSPGARAA LLWALAAALE
RRKSTLASRL ERQGAELKAA EAEVELSARR LRAWGARVQA QGHTLQVAGL RGPVLRLREP
LGVLAVVCPD EWPLLAFVSL LAPALAYGNT VVMVPSAACP LLALEVCQDM ATVFPAGLAN
VVTGDRDHLT RCLALHQDVQ AMWYFGSAQG SQFVEWASAG NLKPVWASRG CPRAWDQEAE
GAGPELGLRV ARTKALWLPM GD
//
ID A16A1_HUMAN Reviewed; 802 AA.
AC Q8IZ83; B4DLQ1; C9JBH6; Q86YF0; Q8IYL4; Q8TEI8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-NOV-2009, sequence version 2.
DT 22-JAN-2014, entry version 90.
DE RecName: Full=Aldehyde dehydrogenase family 16 member A1;
GN Name=ALDH16A1;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP VAL-227.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP VAL-227.
RC TISSUE=Lymph, Skin, and Uterus;
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 INTERACTION WITH SPG21.
RX PubMed=19184135; DOI=10.1007/s10048-009-0172-6;
RA Hanna M.C., Blackstone C.;
RT "Interaction of the SPG21 protein ACP33/maspardin with the aldehyde
RT dehydrogenase ALDH16A1.";
RL Neurogenetics 10:217-228(2009).
RN [6]
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 -!- SUBUNIT: Interacts with SPG21.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IZ83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZ83-2; Sequence=VSP_029982, VSP_029983;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q8IZ83-3; Sequence=VSP_043280;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC -!- CAUTION: The active site cysteine and glutamate residues are not
CC conserved in this protein. Its activity is therefore unsure.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35641.1; Type=Erroneous initiation;
CC Sequence=BAB84962.1; Type=Erroneous translation; Note=Wrong choice of frame;
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; AK074136; BAB84962.1; ALT_SEQ; mRNA.
DR EMBL; AK297101; BAG59613.1; -; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014895; AAH14895.2; -; mRNA.
DR EMBL; BC035641; AAH35641.1; ALT_INIT; mRNA.
DR EMBL; BC042142; AAH42142.1; -; mRNA.
DR RefSeq; NP_001138868.1; NM_001145396.1.
DR RefSeq; NP_699160.2; NM_153329.3.
DR UniGene; Hs.719998; -.
DR ProteinModelPortal; Q8IZ83; -.
DR SMR; Q8IZ83; 17-494, 528-791.
DR IntAct; Q8IZ83; 7.
DR MINT; MINT-4999900; -.
DR STRING; 9606.ENSP00000293350; -.
DR PhosphoSite; Q8IZ83; -.
DR DMDM; 269849532; -.
DR PaxDb; Q8IZ83; -.
DR PRIDE; Q8IZ83; -.
DR Ensembl; ENST00000293350; ENSP00000293350; ENSG00000161618.
DR Ensembl; ENST00000455361; ENSP00000410142; ENSG00000161618.
DR GeneID; 126133; -.
DR KEGG; hsa:126133; -.
DR UCSC; uc002pnt.3; human.
DR CTD; 126133; -.
DR GeneCards; GC19P049958; -.
DR H-InvDB; HIX0202728; -.
DR HGNC; HGNC:28114; ALDH16A1.
DR MIM; 613358; gene.
DR neXtProt; NX_Q8IZ83; -.
DR PharmGKB; PA134903503; -.
DR eggNOG; COG1012; -.
DR HOGENOM; HOG000112558; -.
DR HOVERGEN; HBG069396; -.
DR InParanoid; Q8IZ83; -.
DR OMA; QESVWDE; -.
DR OrthoDB; EOG7Q2N4V; -.
DR PhylomeDB; Q8IZ83; -.
DR GeneWiki; ALDH16A1; -.
DR GenomeRNAi; 126133; -.
DR NextBio; 81700; -.
DR PRO; PR:Q8IZ83; -.
DR ArrayExpress; Q8IZ83; -.
DR Bgee; Q8IZ83; -.
DR CleanEx; HS_ALDH16A1; -.
DR Genevestigator; Q8IZ83; -.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 2.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR011408; Aldehyde_DH.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 2.
DR PIRSF; PIRSF036490; Aldedh_dupl; 1.
DR SUPFAM; SSF53720; SSF53720; 2.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Polymorphism;
KW Reference proteome.
FT CHAIN 1 802 Aldehyde dehydrogenase family 16 member
FT A1.
FT /FTId=PRO_0000312986.
FT VAR_SEQ 254 308 EGRALRRSLAGECAELGLALGTESLLLLTDTADVDSAVEGV
FT VDAAWSDRGPGGLR -> VPSGQGSWRNAAGGRKAPPAAEL
FT GGVPRKGVPFDGAWRESVRSWAWRWGRSRCCC (in
FT isoform 2).
FT /FTId=VSP_029982.
FT VAR_SEQ 254 304 Missing (in isoform 3).
FT /FTId=VSP_043280.
FT VAR_SEQ 309 802 Missing (in isoform 2).
FT /FTId=VSP_029983.
FT VARIANT 110 110 E -> K (in dbSNP:rs3745312).
FT /FTId=VAR_037638.
FT VARIANT 227 227 L -> V (in dbSNP:rs1320303).
FT /FTId=VAR_037639.
SQ SEQUENCE 802 AA; 85127 MW; 2820628CD0EF5823 CRC64;
MAATRAGPRA REIFTSLEYG PVPESHACAL AWLDTQDRCL GHYVNGKWLK PEHRNSVPCQ
DPITGENLAS CLQAQAEDVA AAVEAARMAF KGWSAHPGVV RAQHLTRLAE VIQKHQRLLW
TLESLVTGRA VREVRDGDVQ LAQQLLHYHA IQASTQEEAL AGWEPMGVIG LILPPTFSFL
EMMWRICPAL AVGCTVVALV PPASPAPLLL AQLAGELGPF PGILNVLSGP ASLVPILASQ
PGIRKVAFCG APEEGRALRR SLAGECAELG LALGTESLLL LTDTADVDSA VEGVVDAAWS
DRGPGGLRLL IQESVWDEAM RRLQERMGRL RSGRGLDGAV DMGARGAAAC DLVQRFVREA
QSQGAQVFQA GDVPSERPFY PPTLVSNLPP ASPCAQVEVP WPVVVASPFR TAKEALLVAN
GTPRGGSASV WSERLGQALE LGYGLQVGTV WINAHGLRDP SVPTGGCKES GCSWHGGPDG
LYEYLRPSGT PARLSCLSKN LNYDTFGLAV PSTLPAGPEI GPSPAPPYGL FVGGRFQAPG
ARSSRPIRDS SGNLHGYVAE GGAKDIRGAV EAAHQAFPGW AGQSPGARAA LLWALAAALE
RRKSTLASRL ERQGAELKAA EAEVELSARR LRAWGARVQA QGHTLQVAGL RGPVLRLREP
LGVLAVVCPD EWPLLAFVSL LAPALAYGNT VVMVPSAACP LLALEVCQDM ATVFPAGLAN
VVTGDRDHLT RCLALHQDVQ AMWYFGSAQG SQFVEWASAG NLKPVWASRG CPRAWDQEAE
GAGPELGLRV ARTKALWLPM GD
//
MIM
613358
*RECORD*
*FIELD* NO
613358
*FIELD* TI
*613358 ALDEHYDE DEHYDROGENASE 16 FAMILY, MEMBER A1; ALDH16A1
*FIELD* TX
CLONING
read moreUsing mass spectrometry to identify proteins that coimmunoprecipitated
with maspardin (ACP33; 608181) from HeLa cell lysates, followed by
database analysis, Hanna and Blackstone (2009) identified ALDH16A1.
Immunohistochemical analysis detected a punctate cytoplasmic ALDH16A1
distribution in HeLa cells. Western blot analysis showed that the
protein had an apparent molecular mass of 85 kD. RT-PCR detected
Aldh16a1 in mouse brain. In situ hybridization of cultured mouse
cortical neurons revealed prominent punctate Aldh16a1 staining in cell
bodies and growth cones.
GENE FUNCTION
Using coimmunoprecipitation analysis and protein pull-down assays, Hanna
and Blackstone (2009) showed that endogenous maspardin and ALDH16A1
interacted directly.
MAPPING
Hartz (2010) mapped the ALDH16A1 gene to chromosome 19q13.33 based on an
alignment of the ALDH16A1 sequence (GenBank GENBANK AY007096) with the
genomic sequence (GRCH37).
*FIELD* RF
1. Hanna, M. C.; Blackstone, C.: Interaction of the SPG21 protein
ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1. Neurogenetics 10:
217-228, 2009.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/15/2010.
*FIELD* CD
Patricia A. Hartz: 4/15/2010
*FIELD* ED
mgross: 04/15/2010
*RECORD*
*FIELD* NO
613358
*FIELD* TI
*613358 ALDEHYDE DEHYDROGENASE 16 FAMILY, MEMBER A1; ALDH16A1
*FIELD* TX
CLONING
read moreUsing mass spectrometry to identify proteins that coimmunoprecipitated
with maspardin (ACP33; 608181) from HeLa cell lysates, followed by
database analysis, Hanna and Blackstone (2009) identified ALDH16A1.
Immunohistochemical analysis detected a punctate cytoplasmic ALDH16A1
distribution in HeLa cells. Western blot analysis showed that the
protein had an apparent molecular mass of 85 kD. RT-PCR detected
Aldh16a1 in mouse brain. In situ hybridization of cultured mouse
cortical neurons revealed prominent punctate Aldh16a1 staining in cell
bodies and growth cones.
GENE FUNCTION
Using coimmunoprecipitation analysis and protein pull-down assays, Hanna
and Blackstone (2009) showed that endogenous maspardin and ALDH16A1
interacted directly.
MAPPING
Hartz (2010) mapped the ALDH16A1 gene to chromosome 19q13.33 based on an
alignment of the ALDH16A1 sequence (GenBank GENBANK AY007096) with the
genomic sequence (GRCH37).
*FIELD* RF
1. Hanna, M. C.; Blackstone, C.: Interaction of the SPG21 protein
ACP33/maspardin with the aldehyde dehydrogenase ALDH16A1. Neurogenetics 10:
217-228, 2009.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 4/15/2010.
*FIELD* CD
Patricia A. Hartz: 4/15/2010
*FIELD* ED
mgross: 04/15/2010