PHTF1_HUMAN
ID PHTF1_HUMAN Reviewed; 762 AA.
AC Q9UMS5; Q5VWP7; Q5VWP8; Q9BUP2; Q9H1X8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein PHTF1 {ECO:0000305};
GN Name=PHTF1 {ECO:0000303|PubMed:10729229, ECO:0000312|HGNC:HGNC:8939};
GN Synonyms=PHTF {ECO:0000303|PubMed:10395808};
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] (ISOFORM 1).
RC TISSUE=Erythroleukemia;
RX PubMed=10395808; DOI=10.1006/geno.1999.5836;
RA Raich N., Mattei M.-G., Romeo P.-H., Beaupain D.;
RT "PHTF, a novel atypical homeobox gene on chromosome 1p13, is evolutionarily
RT conserved.";
RL Genomics 59:108-109(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=10729229; DOI=10.1006/geno.1999.6079;
RA Manuel A., Beaupain D., Romeo P.-H., Raich N.;
RT "Molecular characterization of a novel gene family (PHTF) conserved from
RT Drosophila to mammals.";
RL Genomics 64:216-220(2000).
CC -!- SUBUNIT: Interacts with FEM1B. {ECO:0000250|UniProtKB:Q9QZ09}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:F1M8G0}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:F1M8G0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UMS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UMS5-2; Sequence=VSP_002144, VSP_002145;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis.
CC {ECO:0000269|PubMed:10729229}.
CC -!- CAUTION: The PHTF domain was initially defined as an atypical
CC homeodomain, suggesting that this protein could act as a transcription
CC regulator (PubMed:10395808). However, the protein is not found in the
CC nucleus and mainly localizes in the endoplasmic reticulum membrane,
CC suggesting that it does not act as a transcription factor (By
CC similarity). {ECO:0000250|UniProtKB:F1M8G0,
CC ECO:0000303|PubMed:10395808}.
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DR EMBL; AJ011863; CAB51572.1; -; mRNA.
DR EMBL; AL365321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002447; AAH02447.1; -; mRNA.
DR CCDS; CCDS81359.1; -. [Q9UMS5-2]
DR CCDS; CCDS861.1; -. [Q9UMS5-1]
DR RefSeq; NP_001309970.1; NM_001323041.1. [Q9UMS5-1]
DR RefSeq; NP_001309971.1; NM_001323042.1. [Q9UMS5-1]
DR RefSeq; NP_001309972.1; NM_001323043.1. [Q9UMS5-1]
DR RefSeq; NP_001309976.1; NM_001323047.1. [Q9UMS5-2]
DR RefSeq; NP_001309977.1; NM_001323048.1. [Q9UMS5-2]
DR RefSeq; NP_001309978.1; NM_001323049.1. [Q9UMS5-2]
DR RefSeq; NP_006599.2; NM_006608.2. [Q9UMS5-1]
DR AlphaFoldDB; Q9UMS5; -.
DR SMR; Q9UMS5; -.
DR BioGRID; 115968; 9.
DR IntAct; Q9UMS5; 6.
DR MINT; Q9UMS5; -.
DR STRING; 9606.ENSP00000358617; -.
DR GlyGen; Q9UMS5; 6 sites.
DR iPTMnet; Q9UMS5; -.
DR PhosphoSitePlus; Q9UMS5; -.
DR BioMuta; PHTF1; -.
DR DMDM; 71152973; -.
DR EPD; Q9UMS5; -.
DR MassIVE; Q9UMS5; -.
DR MaxQB; Q9UMS5; -.
DR PaxDb; Q9UMS5; -.
DR PeptideAtlas; Q9UMS5; -.
DR PRIDE; Q9UMS5; -.
DR ProteomicsDB; 85208; -. [Q9UMS5-1]
DR ProteomicsDB; 85209; -. [Q9UMS5-2]
DR Antibodypedia; 20143; 28 antibodies from 12 providers.
DR DNASU; 10745; -.
DR Ensembl; ENST00000357783.6; ENSP00000350428.2; ENSG00000116793.16. [Q9UMS5-2]
DR Ensembl; ENST00000369604.6; ENSP00000358617.1; ENSG00000116793.16. [Q9UMS5-1]
DR Ensembl; ENST00000393357.6; ENSP00000377025.2; ENSG00000116793.16. [Q9UMS5-1]
DR GeneID; 10745; -.
DR KEGG; hsa:10745; -.
DR MANE-Select; ENST00000369604.6; ENSP00000358617.1; NM_001323043.2; NP_001309972.1.
DR UCSC; uc001edn.4; human. [Q9UMS5-1]
DR CTD; 10745; -.
DR DisGeNET; 10745; -.
DR GeneCards; PHTF1; -.
DR HGNC; HGNC:8939; PHTF1.
DR HPA; ENSG00000116793; Low tissue specificity.
DR MIM; 604950; gene.
DR neXtProt; NX_Q9UMS5; -.
DR OpenTargets; ENSG00000116793; -.
DR PharmGKB; PA33278; -.
DR VEuPathDB; HostDB:ENSG00000116793; -.
DR eggNOG; ENOG502QQGQ; Eukaryota.
DR GeneTree; ENSGT00390000011648; -.
DR InParanoid; Q9UMS5; -.
DR OMA; LYFMIPV; -.
DR OrthoDB; 710715at2759; -.
DR PhylomeDB; Q9UMS5; -.
DR TreeFam; TF323570; -.
DR PathwayCommons; Q9UMS5; -.
DR SignaLink; Q9UMS5; -.
DR BioGRID-ORCS; 10745; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; PHTF1; human.
DR GenomeRNAi; 10745; -.
DR Pharos; Q9UMS5; Tdark.
DR PRO; PR:Q9UMS5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UMS5; protein.
DR Bgee; ENSG00000116793; Expressed in right hemisphere of cerebellum and 145 other tissues.
DR ExpressionAtlas; Q9UMS5; baseline and differential.
DR Genevisible; Q9UMS5; HS.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR039775; PHTF1/2.
DR InterPro; IPR021980; PHTF1/2_N.
DR PANTHER; PTHR12680; PTHR12680; 1.
DR Pfam; PF12129; Phtf-FEM1B_bdg; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..762
FT /note="Protein PHTF1"
FT /id="PRO_0000127423"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 6..150
FT /note="PHTF"
FT /evidence="ECO:0000255"
FT REGION 152..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZ09"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 632..637
FT /note="LQGHKT -> KVSHLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002144"
FT VAR_SEQ 638..762
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_002145"
FT CONFLICT 245
FT /note="W -> C (in Ref. 1; CAB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="A -> P (in Ref. 1; CAB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="C -> G (in Ref. 1; CAB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="L -> W (in Ref. 1; CAB51572)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="F -> S (in Ref. 1; CAB51572)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 762 AA; 87252 MW; 0813B7A668262DD9 CRC64;
MASNERDAIS WYQKKIGAYD QQIWEKSIEQ TQIKGLKNKP KKMGHIKPDL IDVDLIRGST
FAKAKPEIPW TSLTRKGLVR VVFFPLFSNW WIQVTSLRIF VWLLLLYFMQ VIAIVLYLMM
PIVNISEVLG PLCLMLLMGT VHCQIVSTQI TRPSGNNGNR RRRKLRKTVN GDGSRENGNN
SSDKVRGIET LESVPIIGGF WETIFGNRIK RVKLISNKGT ETDNDPSCVH PIIKRRQCRP
EIRMWQTREK AKFSDGEKCR REAFRRLGNG VSDDLSSEED GEARTQMILL RRSVEGASSD
NGCEVKNRKS ILSRHLNSQV KKTTTRWCHI VRDSDSLAES EFESAAFSQG SRSGVSGGSR
SLNMSRRDSE STRHDSETED MLWDDLLHGP ECRSSVTSDS EGAHVNTLHS GTKRDPKEDV
FQQNHLFWLQ NSSPSSDRVS AIIWEGNECK KMDMSVLEIS GIIMSRVNAY QQGVGYQMLG
NVVTIGLAFF PFLHRLFREK SLDQLKSISA EEILTLFCGA PPVTPIIVLS IINFFERLCL
TWMFFFMMCV AERTYKQRFL FAKLFSHITS ARKARKYEIP HFRLKKVENI KIWLSLRSYL
KRRGPQRSVD VVVSSVFLLT LSIAFICCAQ VLQGHKTFLN DAYNWEFLIW ETALLLFLLR
LASLGSETNK KYSNVSILLT EQINLYLKME KKPNKKEQLT LVNNVLKLST KLLKELDTPF
RLYGLTMNPL IYNITRVVIL SAVSGVISDL LGFNIRLWKI KS
