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CHCH9_HUMAN
ID   CHCH9_HUMAN             Reviewed;         151 AA.
AC   Q5T1J5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial;
DE   AltName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing 2 pseudogene 9;
DE   Flags: Precursor;
GN   Name=CHCHD2P9; Synonyms=C9orf49, CHCHD9;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC   -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR   EMBL; AL450243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5T1J5; -.
DR   SMR; Q5T1J5; -.
DR   IntAct; Q5T1J5; 20.
DR   MINT; Q5T1J5; -.
DR   GlyGen; Q5T1J5; 1 site, 1 O-linked glycan (1 site).
DR   BioMuta; HGNC:23676; -.
DR   DMDM; 74744476; -.
DR   EPD; Q5T1J5; -.
DR   jPOST; Q5T1J5; -.
DR   MassIVE; Q5T1J5; -.
DR   MaxQB; Q5T1J5; -.
DR   PeptideAtlas; Q5T1J5; -.
DR   PRIDE; Q5T1J5; -.
DR   TopDownProteomics; Q5T1J5; -.
DR   GeneCards; CHCHD2P9; -.
DR   HGNC; HGNC:23676; CHCHD2P9.
DR   neXtProt; NX_Q5T1J5; -.
DR   InParanoid; Q5T1J5; -.
DR   PhylomeDB; Q5T1J5; -.
DR   PathwayCommons; Q5T1J5; -.
DR   SignaLink; Q5T1J5; -.
DR   ChiTaRS; CHCHD2P9; human.
DR   Pharos; Q5T1J5; Tdark.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q5T1J5; protein.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   PROSITE; PS51808; CHCH; 1.
PE   5: Uncertain;
KW   Disulfide bond; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..9
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           10..151
FT                   /note="Putative coiled-coil-helix-coiled-coil-helix domain-
FT                   containing protein CHCHD2P9, mitochondrial"
FT                   /id="PRO_0000314910"
FT   DOMAIN          111..151
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           114..124
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           134..144
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        114..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        124..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   151 AA;  15490 MW;  1D157DDD5B459844 CRC64;
     MPRGSRSRTS RMAPPASRAP QMRAAPRPAP VAQPPAAAPP SAVGSSAAAP RQPGLMAQMA
     TTAAGVAVGS AVGHTQGHAV TGGFSGGSNA EPARPDIAYQ EPQGTQPAQQ QQPCFYGIKQ
     FLECAQNQGD IKLCEDFSKV LKQCRLAKGL A
 
 
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