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DNA-directed primase/polymerase protein (hPrimpol1) (EC 2.7.7.-) (Coiled-coil domain-containing protein 111)

 PRIPO_HUMAN             Reviewed;         560 AA.
Q96LW4; D3DP55; D6RDM1; Q5HYJ9;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
27-SEP-2017, entry version 112.
RecName: Full=DNA-directed primase/polymerase protein;
Short=hPrimpol1;
EC=2.7.7.-;
AltName: Full=Coiled-coil domain-containing protein 111;
Name=PRIMPOL; Synonyms=CCDC111;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-168.
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ARG-168.
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-168.
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-168.
TISSUE=Uterus;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[7]
FUNCTION, INTERACTION WITH RPA1, AND MUTAGENESIS OF ASP-114; HIS-169
AND HIS-426.
PubMed=24126761; DOI=10.1038/embor.2013.159;
Wan L., Lou J., Xia Y., Su B., Liu T., Cui J., Sun Y., Lou H.,
Huang J.;
"hPrimpol1/CCDC111 is a human DNA primase-polymerase required for the
maintenance of genome integrity.";
EMBO Rep. 14:1104-1112(2013).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[9]
FUNCTION, SUBCELLULAR LOCATION, COFACTOR, AND MUTAGENESIS OF
114-ASP--GLU-116.
PubMed=24207056; DOI=10.1016/j.molcel.2013.09.025;
Garcia-Gomez S., Reyes A., Martinez-Jimenez M.I., Chocron E.S.,
Mouron S., Terrados G., Powell C., Salido E., Mendez J., Holt I.J.,
Blanco L.;
"PrimPol, an archaic primase/polymerase operating in human cells.";
Mol. Cell 52:541-553(2013).
[10]
FUNCTION, AND MUTAGENESIS OF 114-ASP--GLU-116.
PubMed=24267451; DOI=10.1016/j.molcel.2013.10.035;
Bianchi J., Rudd S.G., Jozwiakowski S.K., Bailey L.J., Soura V.,
Taylor E., Stevanovic I., Green A.J., Stracker T.H., Lindsay H.D.,
Doherty A.J.;
"PrimPol bypasses UV photoproducts during eukaryotic chromosomal DNA
replication.";
Mol. Cell 52:566-573(2013).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-419 AND
HIS-426.
PubMed=24240614; DOI=10.1038/nsmb.2719;
Mouron S., Rodriguez-Acebes S., Martinez-Jimenez M.I.,
Garcia-Gomez S., Chocron S., Blanco L., Mendez J.;
"Repriming of DNA synthesis at stalled replication forks by human
PrimPol.";
Nat. Struct. Mol. Biol. 20:1383-1389(2013).
[12]
VARIANT MYP22 ASP-89.
PubMed=23579484; DOI=10.1007/s00439-013-1303-6;
Zhao F., Wu J., Xue A., Su Y., Wang X., Lu X., Zhou Z., Qu J.,
Zhou X.;
"Exome sequencing reveals CCDC111 mutation associated with high
myopia.";
Hum. Genet. 132:913-921(2013).
-!- FUNCTION: DNA primase and DNA polymerase able to initiate de novo
DNA synthesis using dNTPs. Shows a high capacity to tolerate DNA
damage lesions such as 8oxoG and abasic sites in DNA. Involved in
translesion synthesis via its primase activity by mediating
uninterrupted fork progression after programmed or damage-induced
fork arrest and by reinitiating DNA synthesis after dNTP
depletion. Required for mitochondrial DNA (mtDNA) synthesis,
suggesting it may be involved in DNA tolerance during the
replication of mitochondrial DNA. Has non-overlapping function
with POLH. {ECO:0000269|PubMed:24126761,
ECO:0000269|PubMed:24207056, ECO:0000269|PubMed:24240614,
ECO:0000269|PubMed:24267451}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000305|PubMed:24207056};
-!- SUBUNIT: Interacts with RPA1. {ECO:0000269|PubMed:24126761}.
-!- INTERACTION:
Q8NEY1-3:NAV1; NbExp=4; IntAct=EBI-10044038, EBI-11953718;
P27694:RPA1; NbExp=7; IntAct=EBI-10044038, EBI-621389;
-!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion matrix. Note=Present
in the nucleus, but a larger fraction is localized inside
mitochondria. Associates with nuclear chromatin during the G1 and
S phases of unperturbed cell cycles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96LW4-1; Sequence=Displayed;
Name=2;
IsoId=Q96LW4-2; Sequence=VSP_053600;
Note=No experimental confirmation available.;
-!- DISEASE: Myopia 22, autosomal dominant (MYP22) [MIM:615420]: A
refractive error of the eye, in which parallel rays from a distant
object come to focus in front of the retina, vision being better
for near objects than for far. {ECO:0000269|PubMed:23579484}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
family. {ECO:0000305}.
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EMBL; AK057729; BAB71553.1; -; mRNA.
EMBL; BX647575; CAI46079.1; -; mRNA.
EMBL; AC079257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471056; EAX04669.1; -; Genomic_DNA.
EMBL; CH471056; EAX04670.1; -; Genomic_DNA.
EMBL; BC064600; AAH64600.1; -; mRNA.
CCDS; CCDS3837.1; -. [Q96LW4-1]
CCDS; CCDS75211.1; -. [Q96LW4-2]
RefSeq; NP_001287696.1; NM_001300767.1.
RefSeq; NP_001287697.1; NM_001300768.1.
RefSeq; NP_001332824.1; NM_001345895.1.
RefSeq; NP_689896.1; NM_152683.3.
UniGene; Hs.481307; -.
PDB; 5L2X; X-ray; 2.20 A; A/B=1-353.
PDB; 5N85; X-ray; 2.00 A; B=514-528.
PDB; 5N8A; X-ray; 1.28 A; X=480-560.
PDBsum; 5L2X; -.
PDBsum; 5N85; -.
PDBsum; 5N8A; -.
ProteinModelPortal; Q96LW4; -.
SMR; Q96LW4; -.
BioGrid; 128410; 6.
IntAct; Q96LW4; 12.
STRING; 9606.ENSP00000313816; -.
iPTMnet; Q96LW4; -.
PhosphoSitePlus; Q96LW4; -.
BioMuta; CCDC111; -.
DMDM; 296434425; -.
MaxQB; Q96LW4; -.
PaxDb; Q96LW4; -.
PeptideAtlas; Q96LW4; -.
PRIDE; Q96LW4; -.
Ensembl; ENST00000314970; ENSP00000313816; ENSG00000164306.
Ensembl; ENST00000503752; ENSP00000420860; ENSG00000164306.
GeneID; 201973; -.
KEGG; hsa:201973; -.
UCSC; uc003iwk.3; human. [Q96LW4-1]
CTD; 201973; -.
DisGeNET; 201973; -.
EuPathDB; HostDB:ENSG00000164306.10; -.
GeneCards; PRIMPOL; -.
HGNC; HGNC:26575; PRIMPOL.
HPA; HPA054372; -.
MalaCards; PRIMPOL; -.
MIM; 615420; phenotype.
MIM; 615421; gene.
neXtProt; NX_Q96LW4; -.
PharmGKB; PA145008751; -.
eggNOG; ENOG410IIJT; Eukaryota.
eggNOG; ENOG410XP31; LUCA.
HOGENOM; HOG000111379; -.
HOVERGEN; HBG081027; -.
InParanoid; Q96LW4; -.
OrthoDB; EOG091G0C75; -.
PhylomeDB; Q96LW4; -.
TreeFam; TF328961; -.
ChiTaRS; PRIMPOL; human.
GenomeRNAi; 201973; -.
PRO; PR:Q96LW4; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164306; -.
CleanEx; HS_CCDC111; -.
ExpressionAtlas; Q96LW4; baseline and differential.
Genevisible; Q96LW4; HS.
GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003896; F:DNA primase activity; IDA:UniProtKB.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; TAS:UniProtKB.
GO; GO:0006264; P:mitochondrial DNA replication; IMP:UniProtKB.
GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
1: Evidence at protein level;
3D-structure; Alternative splicing; Coiled coil; Complete proteome;
Disease mutation; DNA damage; DNA repair; DNA-directed DNA polymerase;
DNA-directed RNA polymerase; Manganese; Mitochondrion;
Nucleotidyltransferase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transferase.
CHAIN 1 560 DNA-directed primase/polymerase protein.
/FTId=PRO_0000279395.
REGION 481 560 Interaction with RPA1.
{ECO:0000269|PubMed:24126761}.
COILED 1 22 {ECO:0000255}.
MOTIF 419 452 Zinc knuckle motif.
ACT_SITE 114 114 {ECO:0000255}.
ACT_SITE 116 116 {ECO:0000255}.
MOD_RES 255 255 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 366 366 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_053600.
VARIANT 89 89 Y -> D (in MYP22).
{ECO:0000269|PubMed:23579484}.
/FTId=VAR_070120.
VARIANT 168 168 Q -> R (in dbSNP:rs2463447).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|Ref.4}.
/FTId=VAR_030878.
VARIANT 505 505 T -> K (in dbSNP:rs14969).
/FTId=VAR_030879.
MUTAGEN 114 116 DLE->ALA: Abolishes DNA primase and
polymerase activities.
{ECO:0000269|PubMed:24207056,
ECO:0000269|PubMed:24267451}.
MUTAGEN 114 114 D->A: Abolishes DNA primase and
polymerase activities.
{ECO:0000269|PubMed:24126761}.
MUTAGEN 169 169 H->N: Abolishes DNA primase and
polymerase activities.
{ECO:0000269|PubMed:24126761}.
MUTAGEN 419 419 C->G: In mutant CH; abolished DNA primase
activity and impaired ability to restart
stalled forks; when associated with Y-
426. {ECO:0000269|PubMed:24240614}.
MUTAGEN 426 426 H->D: Abolishes DNA primase activity,
while it increases DNA polymerase
activity. {ECO:0000269|PubMed:24126761,
ECO:0000269|PubMed:24240614}.
MUTAGEN 426 426 H->Y: In mutant CH; abolished DNA primase
activity and impaired ability to restart
stalled forks; when associated with G-
419. {ECO:0000269|PubMed:24126761,
ECO:0000269|PubMed:24240614}.
CONFLICT 322 322 D -> G (in Ref. 2; CAI46079).
{ECO:0000305}.
HELIX 2 16 {ECO:0000244|PDB:5L2X}.
STRAND 43 47 {ECO:0000244|PDB:5L2X}.
HELIX 48 56 {ECO:0000244|PDB:5L2X}.
STRAND 63 68 {ECO:0000244|PDB:5L2X}.
STRAND 70 73 {ECO:0000244|PDB:5L2X}.
STRAND 76 81 {ECO:0000244|PDB:5L2X}.
HELIX 83 90 {ECO:0000244|PDB:5L2X}.
STRAND 93 95 {ECO:0000244|PDB:5L2X}.
STRAND 98 102 {ECO:0000244|PDB:5L2X}.
STRAND 112 118 {ECO:0000244|PDB:5L2X}.
TURN 119 121 {ECO:0000244|PDB:5L2X}.
HELIX 127 146 {ECO:0000244|PDB:5L2X}.
HELIX 152 154 {ECO:0000244|PDB:5L2X}.
STRAND 155 159 {ECO:0000244|PDB:5L2X}.
STRAND 163 172 {ECO:0000244|PDB:5L2X}.
STRAND 177 180 {ECO:0000244|PDB:5L2X}.
HELIX 182 192 {ECO:0000244|PDB:5L2X}.
HELIX 194 198 {ECO:0000244|PDB:5L2X}.
HELIX 264 266 {ECO:0000244|PDB:5L2X}.
STRAND 267 269 {ECO:0000244|PDB:5L2X}.
STRAND 275 279 {ECO:0000244|PDB:5L2X}.
HELIX 281 283 {ECO:0000244|PDB:5L2X}.
STRAND 289 291 {ECO:0000244|PDB:5L2X}.
STRAND 303 306 {ECO:0000244|PDB:5L2X}.
HELIX 322 330 {ECO:0000244|PDB:5L2X}.
STRAND 342 344 {ECO:0000244|PDB:5L2X}.
SEQUENCE 560 AA; 64383 MW; C7E75FC7EFAEEF13 CRC64;
MNRKWEAKLK QIEERASHYE RKPLSSVYRP RLSKPEEPPS IWRLFHRQAQ AFNFVKSCKE
DVHVFALECK VGDGQRIYLV TTYAEFWFYY KSRKNLLHCY EVIPENAVCK LYFDLEFNKP
ANPGADGKKM VALLIEYVCK ALQELYGVNC SAEDVLNLDS STDEKFSQHL IFQLHDVAFK
DNIHVGNFLR KILQPALDLL GSEDDDSAPE TTGHGFPHFS EAPARQGFSF NKMFTEKATE
ESWTSNSKKL ERLGSAEQSS PDLSFLVVKN NMGEKHLFVD LGVYTRNRNF RLYKSSKIGK
RVALEVTEDN KFFPIQSKDV SDEYQYFLSS LVSNVRFSDT LRILTCEPSQ NKQKGVGYFN
SIGTSVETIE GFQCSPYPEV DHFVLSLVNK DGIKGGIRRW NYFFPEELLV YDICKYRWCE
NIGRAHKSNN IMILVDLKNE VWYQKCHDPV CKAENFKSDC FPLPAEVCLL FLFKEEEEFT
TDEADETRSN ETQNPHKPSP SRLSTGASAD AVWDNGIDDA YFLEATEDAE LAEAAENSLL
SYNSEVDEIP DELIIEVLQE


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EIAAB07113 C10orf34,CHCHD1,Coiled-coil-helix-coiled-coil-helix domain-containing protein 1,Homo sapiens,Human,Nuclear protein C2360
EIAAB07111 C22orf16,CHCHD10,Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial,Homo sapiens,Human,Protein N27C7-4
EIAAB11295 Ccd1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,Dixdc1,Dixin,Kiaa1735,Mouse,Mus musculus
EIAAB11294 Ccd1,Coiled-coil protein DIX1,Coiled-coil-DIX1,DIX domain-containing protein 1,Dixdc1,Dixin,Rat,Rattus norvegicus
10-288-22341F Coiled-coil-helix-coiled-coil-helix domain-containing protein 2 - HCV NS2 trans-regulated protein; NS2TP 0.05 mg
10-288-22341F Coiled-coil-helix-coiled-coil-helix domain-containing protein 2 - HCV NS2 trans-regulated protein; NS2TP 0.1 mg
CSB-EL005324HU Human Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial(CHCHD9) ELISA kit SpeciesHuman 96T
CHC10_HUMAN ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 10, mitochondrial; organism: Human; gene name: CHCHD10 96T
G5255 Putative coiled-coil-helix-coiled-coil-helix domain-containing protein CHCHD2P9, mitochondrial (CHCHD9), Human, ELISA Kit 96T
CHCH3_MOUSE ELISA Kit FOR Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial; organism: Mouse; gene name: Chchd3 96T


 

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