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2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1)

 DPH1_HUMAN              Reviewed;         443 AA.
Q9BZG8; D3DTI3; Q16439; Q4VBA2; Q9BTW7; Q9UCY0;
23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
20-JUN-2018, entry version 116.
RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
EC=2.5.1.108 {ECO:0000250|UniProtKB:Q5NCQ5};
AltName: Full=Diphthamide biosynthesis protein 1;
AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000305};
AltName: Full=Ovarian cancer-associated gene 1 protein;
AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000305};
Name=DPH1; Synonyms=DPH2L, DPH2L1, OVCA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8603384; DOI=10.1016/0304-3835(96)04169-9;
Phillips N.J., Zeigler M.R., Deaven L.L.;
"A cDNA from the ovarian cancer critical region of deletion on
chromosome 17p13.3.";
Cancer Lett. 102:85-90(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT ARG-226.
PubMed=8616839;
Schultz D.C., Vanderveer L., Berman D.B., Hamilton T.C., Wong A.J.,
Godwin A.K.;
"Identification of two candidate tumor suppressor genes on chromosome
17p13.3.";
Cancer Res. 56:1997-2002(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANTS BREAST AND
OVARIAN CANCER VAL-7; ASP-34; VAL-335 AND ARG-389, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=10519411;
Bruening W., Prowse A.H., Schultz D.C., Holgado-Madruga M., Wong A.,
Godwin A.K.;
"Expression of OVCA1, a candidate tumor suppressor, is reduced in
tumors and inhibits growth of ovarian cancer cells.";
Cancer Res. 59:4973-4983(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 8-443 (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-443 (ISOFORMS 1/2/3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH RBM8A.
PubMed=11013075; DOI=10.1006/geno.2000.6315;
Salicioni A.M., Xi M., Vanderveer L.A., Balsara B., Testa J.R.,
Dunbrack R.L. Jr., Godwin A.K.;
"Identification and structural analysis of human RBM8A and RBM8B: two
highly conserved RNA-binding motif proteins that interact with OVCA1,
a candidate tumor suppressor.";
Genomics 69:54-62(2000).
[9]
INVOLVEMENT IN DEDSSH, AND VARIANT DEDSSH PRO-234.
PubMed=25558065; DOI=10.1016/j.celrep.2014.12.015;
Alazami A.M., Patel N., Shamseldin H.E., Anazi S., Al-Dosari M.S.,
Alzahrani F., Hijazi H., Alshammari M., Aldahmesh M.A., Salih M.A.,
Faqeih E., Alhashem A., Bashiri F.A., Al-Owain M., Kentab A.Y.,
Sogaty S., Al Tala S., Temsah M.H., Tulbah M., Aljelaify R.F.,
Alshahwan S.A., Seidahmed M.Z., Alhadid A.A., Aldhalaan H.,
AlQallaf F., Kurdi W., Alfadhel M., Babay Z., Alsogheer M., Kaya N.,
Al-Hassnan Z.N., Abdel-Salam G.M., Al-Sannaa N., Al Mutairi F.,
El Khashab H.Y., Bohlega S., Jia X., Nguyen H.C., Hammami R., Adly N.,
Mohamed J.Y., Abdulwahab F., Ibrahim N., Naim E.A., Al-Younes B.,
Meyer B.F., Hashem M., Shaheen R., Xiong Y., Abouelhoda M.,
Aldeeri A.A., Monies D.M., Alkuraya F.S.;
"Accelerating novel candidate gene discovery in neurogenetic disorders
via whole-exome sequencing of prescreened multiplex consanguineous
families.";
Cell Rep. 10:148-161(2015).
[10]
INVOLVEMENT IN DEDSSH, AND VARIANT DEDSSH LYS-6.
PubMed=26220823; DOI=10.1002/humu.22843;
Loucks C.M., Parboosingh J.S., Shaheen R., Bernier F.P., McLeod D.R.,
Seidahmed M.Z., Puffenberger E.G., Ober C., Hegele R.A., Boycott K.M.,
Alkuraya F.S., Innes A.M.;
"Matching two independent cohorts validates DPH1 as a gene responsible
for autosomal recessive intellectual disability with short stature,
craniofacial, and ectodermal anomalies.";
Hum. Mutat. 36:1015-1019(2015).
-!- FUNCTION: Required for the first step in the synthesis of
diphthamide, a post-translational modification of histidine which
occurs in translation elongation factor 2 (EEF2). When
overexpressed, suppresses colony formation ability and growth rate
of ovarian cancer cells. Acts also as a tumor suppressor in lung
and breast cancers (By similarity). Plays a role in embryonic
growth, organogenesis and postnatal survival (By similarity).
{ECO:0000250|UniProtKB:Q5NCQ5, ECO:0000269|PubMed:10519411}.
-!- CATALYTIC ACTIVITY: L-histidine-[translation elongation factor 2]
+ S-adenosyl-L-methionine = 2-((3S)-3-amino-3-carboxypropyl)-L-
histidine-[translation elongation factor 2] + S-methyl-5'-
thioadenosine. {ECO:0000250|UniProtKB:Q5NCQ5}.
-!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
-!- SUBUNIT: Interacts with DPH2 (By similarity). Interacts with
RBM8A. {ECO:0000250|UniProtKB:Q5NCQ5,
ECO:0000269|PubMed:11013075}.
-!- INTERACTION:
Q12800:TFCP2; NbExp=3; IntAct=EBI-10303200, EBI-717422;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10519411}.
Cytoplasm {ECO:0000269|PubMed:10519411}. Note=Punctate, primarily
perinuclear localization.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BZG8-1; Sequence=Displayed;
Name=2;
IsoId=Q9BZG8-2; Sequence=VSP_028852;
Name=3;
IsoId=Q9BZG8-3; Sequence=VSP_028851;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
liver, skeletal muscle, kidney, pancreas, spleen, thymus, mammary
gland, colon, small intestine, testis and ovary. Reduced
expression in primary breast and ovarian tumors.
{ECO:0000269|PubMed:10519411, ECO:0000269|PubMed:8616839}.
-!- DISEASE: Developmental delay with short stature, dysmorphic
features, and sparse hair (DEDSSH) [MIM:616901]: An autosomal
recessive syndrome characterized by intellectual disability, short
stature, and craniofacial and ectodermal anomalies including
scaphocephaly with or without craniosynostosis, prominent
forehead, sparse eyebrows and hair, hypoplastic toenails and, in
some cases, dental anomalies. {ECO:0000269|PubMed:25558065,
ECO:0000269|PubMed:26220823}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S81752; AAB36297.1; -; mRNA.
EMBL; U34880; AAD10198.1; -; mRNA.
EMBL; AF321876; AAK13428.1; -; mRNA.
EMBL; AC099684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90567.1; -; Genomic_DNA.
EMBL; CH471108; EAW90569.1; -; Genomic_DNA.
EMBL; BC003099; AAH03099.2; -; mRNA.
EMBL; BC096088; AAH96088.1; -; mRNA.
EMBL; BT019878; AAV38681.1; -; mRNA.
CCDS; CCDS42228.1; -. [Q9BZG8-1]
RefSeq; NP_001333505.1; NM_001346576.1. [Q9BZG8-3]
RefSeq; NP_001374.3; NM_001383.4. [Q9BZG8-1]
UniGene; Hs.513856; -.
ProteinModelPortal; Q9BZG8; -.
SMR; Q9BZG8; -.
BioGrid; 108135; 41.
IntAct; Q9BZG8; 2.
STRING; 9606.ENSP00000263083; -.
iPTMnet; Q9BZG8; -.
PhosphoSitePlus; Q9BZG8; -.
BioMuta; DPH1; -.
DMDM; 269849559; -.
EPD; Q9BZG8; -.
MaxQB; Q9BZG8; -.
PaxDb; Q9BZG8; -.
PeptideAtlas; Q9BZG8; -.
PRIDE; Q9BZG8; -.
ProteomicsDB; 79843; -.
ProteomicsDB; 79844; -. [Q9BZG8-2]
ProteomicsDB; 79845; -. [Q9BZG8-3]
DNASU; 1801; -.
Ensembl; ENST00000263083; ENSP00000263083; ENSG00000108963. [Q9BZG8-1]
Ensembl; ENST00000570477; ENSP00000458726; ENSG00000108963. [Q9BZG8-2]
GeneID; 1801; -.
KEGG; hsa:1801; -.
UCSC; uc002fts.4; human. [Q9BZG8-1]
CTD; 1801; -.
DisGeNET; 1801; -.
EuPathDB; HostDB:ENSG00000108963.17; -.
GeneCards; DPH1; -.
H-InvDB; HIX0013414; -.
HGNC; HGNC:3003; DPH1.
HPA; HPA069750; -.
MalaCards; DPH1; -.
MIM; 603527; gene.
MIM; 616901; phenotype.
neXtProt; NX_Q9BZG8; -.
OpenTargets; ENSG00000108963; -.
PharmGKB; PA27461; -.
eggNOG; KOG2648; Eukaryota.
eggNOG; COG1736; LUCA.
GeneTree; ENSGT00550000075112; -.
HOGENOM; HOG000164743; -.
HOVERGEN; HBG107822; -.
InParanoid; Q9BZG8; -.
KO; K07561; -.
OMA; PGQVLGC; -.
OrthoDB; EOG091G08DQ; -.
PhylomeDB; Q9BZG8; -.
TreeFam; TF105746; -.
Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
UniPathway; UPA00559; -.
ChiTaRS; DPH1; human.
GeneWiki; DPH1; -.
GenomeRNAi; 1801; -.
PRO; PR:Q9BZG8; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108963; -.
CleanEx; HS_DPH1; -.
ExpressionAtlas; Q9BZG8; baseline and differential.
Genevisible; Q9BZG8; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central.
InterPro; IPR016435; DPH1/DPH2.
InterPro; IPR035435; DPH1/DPH2_euk_archaea.
PANTHER; PTHR10762; PTHR10762; 1.
Pfam; PF01866; Diphthamide_syn; 1.
PIRSF; PIRSF004967; DPH1; 1.
SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
TIGRFAMs; TIGR00322; diphth2_R; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Disease mutation;
Dwarfism; Ectodermal dysplasia; Hypotrichosis; Mental retardation;
Nucleus; Polymorphism; Reference proteome; S-adenosyl-L-methionine;
Transferase; Tumor suppressor.
CHAIN 1 443 2-(3-amino-3-carboxypropyl)histidine
synthase subunit 1.
/FTId=PRO_0000307882.
VAR_SEQ 1 140 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_028851.
VAR_SEQ 1 80 Missing (in isoform 2).
{ECO:0000303|PubMed:8603384}.
/FTId=VSP_028852.
VARIANT 6 6 M -> K (in DEDSSH; dbSNP:rs757167361).
{ECO:0000269|PubMed:26220823}.
/FTId=VAR_076412.
VARIANT 7 7 A -> V (in breast and ovarian cancer;
dbSNP:rs778705666).
{ECO:0000269|PubMed:10519411}.
/FTId=VAR_036702.
VARIANT 34 34 A -> D (in breast and ovarian cancer).
{ECO:0000269|PubMed:10519411}.
/FTId=VAR_036703.
VARIANT 51 51 I -> M (in dbSNP:rs8070453).
/FTId=VAR_059255.
VARIANT 226 226 K -> R (in dbSNP:rs1131600).
{ECO:0000269|PubMed:8616839}.
/FTId=VAR_055706.
VARIANT 234 234 L -> P (in DEDSSH; dbSNP:rs730882250).
{ECO:0000269|PubMed:25558065}.
/FTId=VAR_076413.
VARIANT 335 335 L -> V (in breast and ovarian cancer;
requires 2 nucleotide substitutions;
dbSNP:rs35394823).
{ECO:0000269|PubMed:10519411}.
/FTId=VAR_036704.
VARIANT 389 389 S -> R (in breast and ovarian cancer).
{ECO:0000269|PubMed:10519411}.
/FTId=VAR_036705.
CONFLICT 8 8 A -> V (in Ref. 3; AAK13428).
{ECO:0000305}.
CONFLICT 162 162 T -> I (in Ref. 6; AAH96088).
{ECO:0000305}.
CONFLICT 358 358 F -> S (in Ref. 1; AAD10198/AAB36297).
{ECO:0000305}.
SEQUENCE 443 AA; 48805 MW; 6AF0FD0D8EE35E2D CRC64;
MRRQVMAALV VSGAAEQGGR DGPGRGRAPR GRVANQIPPE ILKNPQLQAA IRVLPSNYNF
EIPKTIWRIQ QAQAKKVALQ MPEGLLLFAC TIVDILERFT EAEVMVMGDV TYGACCVDDF
TARALGADFL VHYGHSCLIP MDTSAQDFRV LYVFVDIRID TTHLLDSLRL TFPPATALAL
VSTIQFVSTL QAAAQELKAE YRVSVPQCKP LSPGEILGCT SPRLSKEVEA VVYLGDGRFH
LESVMIANPN VPAYRYDPYS KVLSREHYDH QRMQAARQEA IATARSAKSW GLILGTLGRQ
GSPKILEHLE SRLRALGLSF VRLLLSEIFP SKLSLLPEVD VWVQVACPRL SIDWGTAFPK
PLLTPYEAAV ALRDISWQQP YPMDFYAGSS LGPWTVNHGQ DRRPHAPGRP ARGKVQEGSA
RPPSAVACED CSCRDEKVAP LAP


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