ID DJC12_HUMAN Reviewed; 198 AA. AC Q9UKB3; Q5JVQ1; Q9UKB2; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 28-JAN-2026, entry version 172. DE RecName: Full=DnaJ homolog subfamily C member 12; DE AltName: Full=J domain-containing protein 1; GN Name=DNAJC12; Synonyms=JDP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). RX PubMed=10760603; DOI=10.1016/s0167-4781(00)00047-6; RA Lee J., Hahn Y., Yun J.H., Mita K., Chung J.H.; RT "Characterization of JDP genes, an evolutionarily conserved J domain-only RT protein family, from human and moths."; RL Biochim. Biophys. Acta 1491:355-363(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP 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 [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., Buerckstuemmer T., RA 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 [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [9] RP SUBCELLULAR LOCATION, INDUCTION BY ER STRESS, AND INTERACTION WITH HSPA8. RX PubMed=24122553; DOI=10.1007/s12192-013-0471-6; RA Choi J., Djebbar S., Fournier A., Labrie C.; RT "The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic RT reticulum stress."; RL Cell Stress Chaperones 19:439-446(2014). RN [10] RP STRUCTURE BY NMR OF 1-100. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of J-domain from human DnaJ subfamily C member 12."; RL Submitted (NOV-2005) to the PDB data bank. RN [11] RP VARIANT HPANBH4 PRO-72, INVOLVEMENT IN HPANBH4, CHARACTERIZATION OF VARIANT RP HPANBH4 PRO-72, AND FUNCTION. RX PubMed=28132689; DOI=10.1016/j.ajhg.2017.01.002; RA Anikster Y., Haack T.B., Vilboux T., Pode-Shakked B., Thoeny B., Shen N., RA Guarani V., Meissner T., Mayatepek E., Trefz F.K., Marek-Yagel D., RA Martinez A., Huttlin E.L., Paulo J.A., Berutti R., Benoist J.F., Imbard A., RA Dorboz I., Heimer G., Landau Y., Ziv-Strasser L., Malicdan M.C., RA Gemperle-Britschgi C., Cremer K., Engels H., Meili D., Keller I., RA Bruggmann R., Strom T.M., Meitinger T., Mullikin J.C., Schwartz G., RA Ben-Zeev B., Gahl W.A., Harper J.W., Blau N., Hoffmann G.F., Prokisch H., RA Opladen T., Schiff M.; RT "Biallelic mutations in DNAJC12 cause hyperphenylalaninemia, dystonia, and RT intellectual disability."; RL Am. J. Hum. Genet. 100:257-266(2017). RN [12] RP VARIANT HPANBH4 72-ARG--ILE-198 DEL, AND INVOLVEMENT IN HPANBH4. RX PubMed=28794131; DOI=10.1136/jmedgenet-2017-104875; RA van Spronsen F.J., Himmelreich N., Ruefenacht V., Shen N., Vliet D.V., RA Al-Owain M., Ramzan K., Alkhalifi S.M., Lunsing R.J., Heiner-Fokkema R.M., RA Rassi A., Gemperle-Britschgi C., Hoffmann G.F., Blau N., Thoeny B.; RT "Heterogeneous clinical spectrum of DNAJC12-deficient RT hyperphenylalaninemia: from attention deficit to severe dystonia and RT intellectual disability."; RL J. Med. Genet. 0:0-0(2017). RN [13] RP INVOLVEMENT IN HPANBH4. RX PubMed=30139987; DOI=10.1038/s41431-018-0237-9; RA Veenma D., Cordeiro D., Sondheimer N., Mercimek-Andrews S.; RT "DNAJC12-associated developmental delay, movement disorder, and mild RT hyperphenylalaninemia identified by whole-exome sequencing re-analysis."; RL Eur. J. Hum. Genet. 26:1867-1870(2018). RN [14] RP INVOLVEMENT IN HPANBH4. RX PubMed=29380259; DOI=10.1007/8904_2017_86; RA de Sain-van der Velden M.G.M., Kuper W.F.E., Kuijper M.A., van Kats L.A.T., RA Prinsen H.C.M.T., Balemans A.C.J., Visser G., van Gassen K.L.I., RA van Hasselt P.M.; RT "Beneficial Effect of BH4 Treatment in a 15-Year-Old Boy with Biallelic RT Mutations in DNAJC12."; RL JIMD Rep. 42:99-103(2018). RN [15] RP INVOLVEMENT IN HPANBH4. RX PubMed=30179615; DOI=10.1016/j.cca.2018.09.002; RA Feng Y., Liu S., Tang C., Jiang X., Tang F., Li B., Jia X., Chen Q., RA Liu J., Huang Y.; RT "Identification of an inherited pathogenic DNAJC12 variant in a patient RT with hyperphenylalalinemia."; RL Clin. Chim. Acta 490:172-175(2019). RN [16] RP VARIANTS HPANBH4 CYS-103 AND 175-TRP--ILE-198 DEL, INVOLVEMENT IN HPANBH4, RP AND CHARACTERIZATION OF VARIANT HPANBH4 175-TRP--ILE-198 DEL. RX PubMed=32333439; DOI=10.1002/humu.24026; RA Gallego D., Leal F., Gamez A., Castro M., Navarrete R., RA Sanchez-Lijarcio O., Vitoria I., Bueno-Delgado M., Belanger-Quintana A., RA Morais A., Pedron-Giner C., Garcia I., Campistol J., Artuch R., Alcaide C., RA Cornejo V., Gil D., Yahyaoui R., Desviat L.R., Ugarte M., Martinez A., RA Perez B.; RT "Pathogenic variants of DNAJC12 and evaluation of the encoded cochaperone RT as a genetic modifier of hyperphenylalaninemia."; RL Hum. Mutat. 41:1329-1338(2020). RN [17] RP VARIANT HPANBH4 GLN-102, INVOLVEMENT IN HPANBH4, AND FUNCTION. RX PubMed=32519510; DOI=10.1002/mgg3.1303; RA Li M., Yang Q., Yi S., Qin Z., Luo J., Fan X.; RT "Two novel mutations in DNAJC12 identified by whole-exome sequencing in a RT patient with mild hyperphenylalaninemia."; RL Mol. Genet. Genomic Med. 8:e1303-e1303(2020). RN [18] RP VARIANT HPANBH4 79-ARG--ILE-198 DEL, AND INVOLVEMENT IN HPANBH4. RX PubMed=38248634; DOI=10.3390/ijns10010007; RA Donnelly C., Estrella L., Ginevic I., Ganesh J.; RT "A Case of DNAJC12-Deficient Hyperphenylalaninemia Detected on Newborn RT Screening: Clinical Outcomes from Early Detection."; RL Int. J. Neonatal Screen. 10:0-0(2024). RN [19] RP VARIANTS HPANBH4 GLU-62 AND 72-ARG--ILE-198 DEL, AND INVOLVEMENT IN RP HPANBH4. RX PubMed=39584997; DOI=10.3390/ijns10040074; RA Wong T.S., Wong S.S.N., Kwok A.M.K., Wu H., Law H.F., Lam S., Yeung M.C.W., RA Chan T.C.H., Leung G., Mak C.M., Belaramani K.M., Fung C.W.; RT "DNAJC12 Deficiency, an Emerging Condition Picked Up by Newborn Screening: RT A Case Illustration and a Novel Variant Identified."; RL Int. J. Neonatal Screen. 10:0-0(2024). CC -!- FUNCTION: Probable co-chaperone that participates in the proper folding CC of biopterin-dependent aromatic amino acid hydroxylases, which include CC phenylalanine-4-hydroxylase (PAH), tyrosine 3-monooxygenase (TH) and CC peripheral and neuronal tryptophan hydroxylases (TPH1 and TPH2). CC {ECO:0000269|PubMed:28132689, ECO:0000269|PubMed:32333439}. CC -!- SUBUNIT: Interacts with HSPA8 (PubMed:24122553). Interacts with TPH1 CC (By similarity). Interacts with TPH2 (By similarity). CC {ECO:0000250|UniProtKB:Q9R022, ECO:0000269|PubMed:24122553}. CC -!- INTERACTION: CC Q9UKB3; P17752: TPH1; NbExp=3; IntAct=EBI-2689937, EBI-3956833; CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm CC {ECO:0000269|PubMed:24122553}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=a; Synonyms=JDP1a; CC IsoId=Q9UKB3-1; Sequence=Displayed; CC Name=B; Synonyms=JDP1b; CC IsoId=Q9UKB3-2; Sequence=VSP_001295, VSP_001296; CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, heart, and CC testis, and at reduced levels in kidney and stomach. CC -!- INDUCTION: Up-regulated by ER stress. {ECO:0000269|PubMed:24122553}. CC -!- DISEASE: Hyperphenylalaninemia, mild, non-BH4-deficient (HPANBH4) CC [MIM:617384]: An autosomal recessive disorder characterized by CC increased serum phenylalanine, normal BH4 metabolism, and highly CC variable neurologic defects, including movement abnormalities and CC intellectual disability. {ECO:0000269|PubMed:28132689, CC ECO:0000269|PubMed:28794131, ECO:0000269|PubMed:29380259, CC ECO:0000269|PubMed:30139987, ECO:0000269|PubMed:32333439, CC ECO:0000269|PubMed:32519510, ECO:0000269|PubMed:38248634, CC ECO:0000269|PubMed:39584997}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF176012; AAD52650.1; -; mRNA. DR EMBL; AF176013; AAD52651.1; -; mRNA. DR EMBL; AL133551; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54257.1; -; Genomic_DNA. DR EMBL; BC017018; AAH17018.1; -; mRNA. DR CCDS; CCDS7271.1; -. [Q9UKB3-1] DR CCDS; CCDS7272.1; -. [Q9UKB3-2] DR RefSeq; NP_068572.1; NM_021800.3. [Q9UKB3-1] DR RefSeq; NP_957714.1; NM_201262.2. [Q9UKB3-2] DR PDB; 2CTQ; NMR; -; A=1-99. DR PDBsum; 2CTQ; -. DR AlphaFoldDB; Q9UKB3; -. DR EMDB; EMD-18058; -. DR EMDB; EMD-18289; -. DR SMR; Q9UKB3; -. DR BioGRID; 121150; 61. DR FunCoup; Q9UKB3; 884. DR IntAct; Q9UKB3; 34. DR STRING; 9606.ENSP00000225171; -. DR GlyGen; Q9UKB3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9UKB3; -. DR PhosphoSitePlus; Q9UKB3; -. DR BioMuta; DNAJC12; -. DR DMDM; 28201819; -. DR jPOST; Q9UKB3; -. DR MassIVE; Q9UKB3; -. DR PaxDb; 9606-ENSP00000225171; -. DR PeptideAtlas; Q9UKB3; -. DR ProteomicsDB; 84763; -. [Q9UKB3-1] DR ProteomicsDB; 84764; -. [Q9UKB3-2] DR Pumba; Q9UKB3; -. DR Antibodypedia; 28382; 87 antibodies from 23 providers. DR DNASU; 56521; -. DR Ensembl; ENST00000225171.7; ENSP00000225171.2; ENSG00000108176.16. [Q9UKB3-1] DR Ensembl; ENST00000339758.7; ENSP00000343575.6; ENSG00000108176.16. [Q9UKB3-2] DR GeneID; 56521; -. DR KEGG; hsa:56521; -. DR MANE-Select; ENST00000225171.7; ENSP00000225171.2; NM_021800.3; NP_068572.1. DR UCSC; uc001jnb.4; human. [Q9UKB3-1] DR AGR; HGNC:28908; -. DR ClinPGx; PA134931354; -. DR CTD; 56521; -. DR DisGeNET; 56521; -. DR GeneCards; DNAJC12; -. DR HGNC; HGNC:28908; DNAJC12. DR HPA; ENSG00000108176; Tissue enhanced (adrenal gland, brain, liver). DR MalaCards; DNAJC12; -. DR MIM; 606060; gene. DR MIM; 617384; phenotype. DR OpenTargets; ENSG00000108176; -. DR Orphanet; 508523; Hyperphenylalaninemia due to DNAJC12 deficiency. DR VEuPathDB; HostDB:ENSG00000108176; -. DR eggNOG; KOG0691; Eukaryota. DR GeneTree; ENSGT00940000159378; -. DR HOGENOM; CLU_2313030_0_0_1; -. DR InParanoid; Q9UKB3; -. DR OrthoDB; 436519at2759; -. DR PAN-GO; Q9UKB3; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9UKB3; -. DR PathwayCommons; Q9UKB3; -. DR SignaLink; Q9UKB3; -. DR Agora; ENSG00000108176; -. DR BioGRID-ORCS; 56521; 9 hits in 1155 CRISPR screens. DR ChiTaRS; DNAJC12; human. DR EvolutionaryTrace; Q9UKB3; -. DR GenomeRNAi; 56521; -. DR Pharos; Q9UKB3; Tbio. DR PRO; PR:Q9UKB3; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q9UKB3; protein. DR Bgee; ENSG00000108176; Expressed in islet of Langerhans and 167 other cell types or tissues. DR ExpressionAtlas; Q9UKB3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR FunFam; 1.10.287.110:FF:000049; DnaJ homolog subfamily C member 12; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR029827; JDP1-like. DR PANTHER; PTHR44500; DNAJ HOMOLOG SUBFAMILY C MEMBER 12; 1. DR PANTHER; PTHR44500:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 12; 1. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. DR SMART; SM00271; DnaJ; 1. DR SUPFAM; SSF46565; Chaperone J-domain; 1. DR PROSITE; PS50076; DNAJ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm; KW Disease variant; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..198 FT /note="DnaJ homolog subfamily C member 12" FT /id="PRO_0000071066" FT DOMAIN 14..79 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT REGION 114..169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 114..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 166 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R022" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9R022" FT VAR_SEQ 100..107 FT /note="SMHWVVRG -> VGFSLGAT (in isoform B)" FT /evidence="ECO:0000303|PubMed:10760603" FT /id="VSP_001295" FT VAR_SEQ 108..198 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:10760603" FT /id="VSP_001296" FT VARIANT 62 FT /note="A -> E (in HPANBH4; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:39584997" FT /id="VAR_090211" FT VARIANT 72..198 FT /note="Missing (in HPANBH4; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:28794131, FT ECO:0000269|PubMed:39584997" FT /id="VAR_090212" FT VARIANT 72 FT /note="R -> P (in HPANBH4; uncertain significance; FT decreased protein levels in homozygous patient cells; FT probably affects PAH stability; PAH activity is reduced in FT homozygous patient cells; dbSNP:rs1035794099)" FT /evidence="ECO:0000269|PubMed:28132689" FT /id="VAR_078797" FT VARIANT 79..198 FT /note="Missing (in HPANBH4; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:38248634" FT /id="VAR_090213" FT VARIANT 102 FT /note="H -> Q (in HPANBH4; uncertain significance; FT dbSNP:rs1373961824)" FT /evidence="ECO:0000269|PubMed:32519510" FT /id="VAR_090214" FT VARIANT 103 FT /note="W -> C (in HPANBH4; likely pathogenic; FT dbSNP:rs1841794635)" FT /evidence="ECO:0000269|PubMed:32333439" FT /id="VAR_090215" FT VARIANT 124 FT /note="M -> I (in dbSNP:rs35690028)" FT /id="VAR_048913" FT VARIANT 129 FT /note="C -> W (in dbSNP:rs36099123)" FT /id="VAR_048914" FT VARIANT 175..198 FT /note="Missing (in HPANBH4; likely pathogenic; decreased FT mRNA and protein levels in homozygous patient cells; FT probably affects PAH stability; PAH levels and activity are FT severely reduced in homozygous patient cells)" FT /evidence="ECO:0000269|PubMed:32333439" FT /id="VAR_090216" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:2CTQ" FT HELIX 27..39 FT /evidence="ECO:0007829|PDB:2CTQ" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:2CTQ" FT HELIX 52..67 FT /evidence="ECO:0007829|PDB:2CTQ" FT HELIX 69..81 FT /evidence="ECO:0007829|PDB:2CTQ" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:2CTQ" SQ SEQUENCE 198 AA; 23415 MW; 03429472C61413EB CRC64; MDAILNYRSE DTEDYYTLLG CDELSSVEQI LAEFKVRALE CHPDKHPENP KAVETFQKLQ KAKEILTNEE SRARYDHWRR SQMSMPFQQW EALNDSVKTS MHWVVRGKKD LMLEESDKTH TTKMENEECN EQRERKKEEL ASTAEKTEQK EPKPLEKSVS PQNSDSSGFA DVNGWHLRFR WSKDAPSELL RKFRNYEI //