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Protein

MICOS complex subunit MIC19

Gene

CHCHD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. Has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Plays an important role in the maintenance of the MICOS complex stability and the mitochondrial cristae morphology (PubMed:25781180).2 Publications

GO - Molecular functioni

GO - Biological processi

  • cristae formation Source: UniProtKB
  • inner mitochondrial membrane organization Source: UniProtKB
  • mitochondrial fusion Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
MICOS complex subunit MIC19
Alternative name(s):
Coiled-coil-helix-coiled-coil-helix domain-containing protein 3
Gene namesi
Name:CHCHD3
Synonyms:MIC19, MINOS3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:21906. CHCHD3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • MICOS complex Source: UniProtKB
  • mitochondrial inner membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134983108.

Polymorphism and mutation databases

BioMutaiCHCHD3.
DMDMi62510520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 227226MICOS complex subunit MIC19PRO_0000129163Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei29 – 291PhosphoserineBy similarity
Modified residuei49 – 491PhosphotyrosineCombined sources
Modified residuei50 – 501PhosphoserineCombined sources
Modified residuei56 – 561PhosphoserineBy similarity
Modified residuei142 – 1421N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

EPDiQ9NX63.
MaxQBiQ9NX63.
PaxDbiQ9NX63.
PeptideAtlasiQ9NX63.
PRIDEiQ9NX63.
TopDownProteomicsiQ9NX63.

2D gel databases

REPRODUCTION-2DPAGEIPI00015833.
UCD-2DPAGEQ9NX63.

PTM databases

iPTMnetiQ9NX63.
PhosphoSiteiQ9NX63.
SwissPalmiQ9NX63.

Expressioni

Tissue specificityi

Detected at low levels in brain, placenta, lung, liver, kidney and pancreas with increased levels in heart and skeletal muscle. Higher expression in primary lung cancers than in normal lung tissue.1 Publication

Gene expression databases

BgeeiQ9NX63.
CleanExiHS_CHCHD3.
ExpressionAtlasiQ9NX63. baseline and differential.
GenevisibleiQ9NX63. HS.

Organism-specific databases

HPAiHPA042935.

Interactioni

Subunit structurei

Component of the mitochondrial contact site and cristae organizing system (MICOS) complex, composed of at least MINOS1/MIC10, CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26 and QIL1/MIC13 (PubMed:21081504, PubMed:22114354, PubMed:22228767, PubMed:25997101). This complex was also known under the names MINOS or MitOS complex. The MICOS complex associates with mitochondrial outer membrane proteins SAMM50, MTX1, MTX2 and DNAJC11, mitochondrial inner membrane protein TMEM11 and with HSPA9 (PubMed:21081504, PubMed:22114354, PubMed:22228767, PubMed:25997101). Found in a complex with IMMT/MIC60 and SAMM50 termed mitochondrial intermembrane space bridging (MIB) complex. Interacts with HSPA1A/HSPA1B and OPA1, preferentially with the soluble OPA1 form (By similarity). Interacts with IMMT/MIC60.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BLZF1Q9H2G93EBI-743375,EBI-2548012
CALCOCO2Q131373EBI-743375,EBI-739580
CCDC85BQ158342EBI-743375,EBI-739674
FANCLQ9NW383EBI-743375,EBI-2339898
GMCL1P1Q8NEA93EBI-743375,EBI-745707
GOLGA2Q083793EBI-743375,EBI-618309
KRT40Q6A1623EBI-743375,EBI-10171697
LZTS2Q9BRK43EBI-743375,EBI-741037
NOTCH2NLQ7Z3S93EBI-743375,EBI-945833
PDE4DIPQ5VU433EBI-743375,EBI-1105124
PPP1CAP621362EBI-743375,EBI-357253
RAB3IPQ96QF03EBI-743375,EBI-747844
RPGRIP1Q96KN73EBI-743375,EBI-1050213
SAMM50Q9Y5123EBI-743375,EBI-748409
SPAG5Q96R063EBI-743375,EBI-413317
SPERTQ8NA613EBI-743375,EBI-741724
SSX2IPQ9Y2D83EBI-743375,EBI-2212028
TRAF1Q130773EBI-743375,EBI-359224
TRIM27P143733EBI-743375,EBI-719493

GO - Molecular functioni

  • phosphatase binding Source: UniProtKB
  • protein complex scaffold Source: UniProtKB

Protein-protein interaction databases

BioGridi120267. 72 interactions.
IntActiQ9NX63. 58 interactions.
MINTiMINT-1477668.
STRINGi9606.ENSP00000262570.

Structurei

3D structure databases

ProteinModelPortaliQ9NX63.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini176 – 21742CHCHAdd
BLAST

Sequence similaritiesi

Contains 1 CHCH domain.Curated

Phylogenomic databases

eggNOGiKOG4083. Eukaryota.
ENOG41126BR. LUCA.
GeneTreeiENSGT00390000000903.
HOGENOMiHOG000252969.
HOVERGENiHBG050936.
InParanoidiQ9NX63.
KOiK17563.
OrthoDBiEOG7NW6C3.
PhylomeDBiQ9NX63.
TreeFamiTF326279.

Family and domain databases

InterProiIPR007964. DUF737.
[Graphical view]
PfamiPF05300. DUF737. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9NX63-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGGTTSTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS
60 70 80 90 100
GAYGASVSDE ELKRRVAEEL ALEQAKKESE DQKRLKQAKE LDRERAAANE
110 120 130 140 150
QLTRAILRER ICSEEERAKA KHLARQLEEK DRVLKKQDAF YKEQLARLEE
160 170 180 190 200
RSSEFYRVTT EQYQKAAEEV EAKFKRYESH PVCADLQAKI LQCYRENTHQ
210 220
TLKCSALATQ YMHCVNHAKQ SMLEKGG
Length:227
Mass (Da):26,152
Last modified:October 1, 2000 - v1
Checksum:i569E405EB7C801D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000427 mRNA. Translation: BAA91157.1.
BC011596 mRNA. Translation: AAH11596.1.
BC014839 mRNA. Translation: AAH14839.1.
CCDSiCCDS5828.1.
RefSeqiNP_001304106.1. NM_001317177.1.
NP_060282.1. NM_017812.3.
UniGeneiHs.655010.

Genome annotation databases

EnsembliENST00000262570; ENSP00000262570; ENSG00000106554.
GeneIDi54927.
KEGGihsa:54927.
UCSCiuc003vre.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000427 mRNA. Translation: BAA91157.1.
BC011596 mRNA. Translation: AAH11596.1.
BC014839 mRNA. Translation: AAH14839.1.
CCDSiCCDS5828.1.
RefSeqiNP_001304106.1. NM_001317177.1.
NP_060282.1. NM_017812.3.
UniGeneiHs.655010.

3D structure databases

ProteinModelPortaliQ9NX63.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120267. 72 interactions.
IntActiQ9NX63. 58 interactions.
MINTiMINT-1477668.
STRINGi9606.ENSP00000262570.

PTM databases

iPTMnetiQ9NX63.
PhosphoSiteiQ9NX63.
SwissPalmiQ9NX63.

Polymorphism and mutation databases

BioMutaiCHCHD3.
DMDMi62510520.

2D gel databases

REPRODUCTION-2DPAGEIPI00015833.
UCD-2DPAGEQ9NX63.

Proteomic databases

EPDiQ9NX63.
MaxQBiQ9NX63.
PaxDbiQ9NX63.
PeptideAtlasiQ9NX63.
PRIDEiQ9NX63.
TopDownProteomicsiQ9NX63.

Protocols and materials databases

DNASUi54927.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262570; ENSP00000262570; ENSG00000106554.
GeneIDi54927.
KEGGihsa:54927.
UCSCiuc003vre.4. human.

Organism-specific databases

CTDi54927.
GeneCardsiCHCHD3.
HGNCiHGNC:21906. CHCHD3.
HPAiHPA042935.
MIMi613748. gene.
neXtProtiNX_Q9NX63.
PharmGKBiPA134983108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4083. Eukaryota.
ENOG41126BR. LUCA.
GeneTreeiENSGT00390000000903.
HOGENOMiHOG000252969.
HOVERGENiHBG050936.
InParanoidiQ9NX63.
KOiK17563.
OrthoDBiEOG7NW6C3.
PhylomeDBiQ9NX63.
TreeFamiTF326279.

Miscellaneous databases

ChiTaRSiCHCHD3. human.
GenomeRNAii54927.
NextBioi58019.
PROiQ9NX63.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NX63.
CleanExiHS_CHCHD3.
ExpressionAtlasiQ9NX63. baseline and differential.
GenevisibleiQ9NX63. HS.

Family and domain databases

InterProiIPR007964. DUF737.
[Graphical view]
PfamiPF05300. DUF737. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix and Skin.
  3. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-49 AND SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function."
    Darshi M., Mendiola V.L., Mackey M.R., Murphy A.N., Koller A., Perkins G.A., Ellisman M.H., Taylor S.S.
    J. Biol. Chem. 286:2918-2932(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IMMT AND SAMM50.
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization."
    Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O., Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.
    Mol. Biol. Cell 23:247-257(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MICOS COMPLEX.
  12. "CHCM1/CHCHD6, a novel mitochondrial protein linked to regulation of mitofilin and mitochondrial cristae morphology."
    An J., Shi J., He Q., Lui K., Liu Y., Huang Y., Sheikh M.S.
    J. Biol. Chem. 287:7411-7426(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHCHD6.
  13. "Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes."
    Ott C., Ross K., Straub S., Thiede B., Gotz M., Goosmann C., Krischke M., Mueller M.J., Krohne G., Rudel T., Kozjak-Pavlovic V.
    Mol. Cell. Biol. 32:1173-1188(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MICOS COMPLEX.
  14. "Cloning and functional analysis of FLJ20420: a novel transcription factor for the BAG-1 promoter."
    Liu H., Li Y., Li Y., Liu B., Wu H., Wang J., Wang Y., Wang M., Tang S.C., Zhou Q., Chen J.
    PLoS ONE 7:E34832-E34832(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. Cited for: NOMENCLATURE.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Global profiling of co- and post-translationally N-myristoylated proteomes in human cells."
    Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.
    Nat. Commun. 5:4919-4919(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology."
    Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F., Gygi S.P., Van Vactor D., Harper J.W.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MIB AND MICOS COMPLEX, INTERACTION WITH IMMT, SUBCELLULAR LOCATION.
  19. "Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits."
    Ott C., Dorsch E., Fraunholz M., Straub S., Kozjak-Pavlovic V.
    PLoS ONE 10:E0120213-E0120213(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MICOS COMPLEX, FUNCTION, SUBCELLULAR LOCATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMIC19_HUMAN
AccessioniPrimary (citable) accession number: Q9NX63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: October 1, 2000
Last modified: April 13, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.