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Protein

Sorting and assembly machinery component 50 homolog

Gene

Samm50

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex.By similarity

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting and assembly machinery component 50 homolog
Gene namesi
Name:Samm50
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1915903. Samm50.

Subcellular locationi

  • Mitochondrion outer membrane By similarity; Multi-pass membrane protein By similarity
  • Cytoplasm By similarity
  • Mitochondrion By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Sorting and assembly machinery component 50 homologPRO_0000286399Add
BLAST

Proteomic databases

EPDiQ8BGH2.
MaxQBiQ8BGH2.
PaxDbiQ8BGH2.
PRIDEiQ8BGH2.

2D gel databases

REPRODUCTION-2DPAGEQ8BGH2.

PTM databases

iPTMnetiQ8BGH2.
PhosphoSiteiQ8BGH2.
SwissPalmiQ8BGH2.

Expressioni

Gene expression databases

BgeeiQ8BGH2.
GenevisibleiQ8BGH2. MM.

Interactioni

Subunit structurei

Associates with 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. 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. Found in a complex with IMMT/MIC60 and CHCHD3/MIC19 termed mitochondrial intermembrane space bridging (MIB) complex. Interacts with IMMT/MIC60 (By similarity). Interacts with CHCHD3/MIC19.By similarity1 Publication

Protein-protein interaction databases

BioGridi212974. 51 interactions.
IntActiQ8BGH2. 52 interactions.
MINTiMINT-4110307.
STRINGi10090.ENSMUSP00000023071.

Structurei

3D structure databases

ProteinModelPortaliQ8BGH2.
SMRiQ8BGH2. Positions 47-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 12581POTRAPROSITE-ProRule annotationAdd
BLAST

Domaini

Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure.By similarity

Sequence similaritiesi

Belongs to the SAM50/omp85 family.Curated
Contains 1 POTRA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane beta strand

Phylogenomic databases

eggNOGiKOG2602. Eukaryota.
COG4775. LUCA.
GeneTreeiENSGT00390000011355.
HOGENOMiHOG000015411.
HOVERGENiHBG054614.
InParanoidiQ8BGH2.
KOiK07277.
OMAiWDQTSEV.
OrthoDBiEOG7VMP51.
PhylomeDBiQ8BGH2.
TreeFamiTF106126.

Family and domain databases

InterProiIPR000184. Bac_surfAg_D15.
[Graphical view]
PfamiPF01103. Bac_surface_Ag. 1 hit.
[Graphical view]
PROSITEiPS51779. POTRA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGH2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTVHARSLE PLPSSGTDFG ALGEEAEFVE VEPEAKQEIL ENKDVVVQHV
60 70 80 90 100
HFDGLGRTKD DIIICEIGEV FKAKNLIEVM RRSHEAREKL LRLGIFRQVD
110 120 130 140 150
VLIDTCHGED ALPNGLDVTF EVTELRRLTG SYNTMVGNNE GSMVLGLKLP
160 170 180 190 200
NLLGRAEKVT FQFSYGTKET SYGLSFFKPQ PGNFERNFSV NLYKVTGQFP
210 220 230 240 250
WSSLRETDRG VSAEYSFPLW KTSHTVKWEG VWRELGCLSR TASFAVRKES
260 270 280 290 300
GHSLKSSLSH AMVIDSRNSS ILPRRGALFK VNQELAGYTG GDVSFIKEDF
310 320 330 340 350
ELQLNKPLAL DSVFSTSLWG GMLVPIGDKP SSIADRFYLG GPTSVRGFSM
360 370 380 390 400
HSIGPQSEGD YLGGEAYWAG GLHLYTPLPF RPGQGGFGEL FRTHFFLNAG
410 420 430 440 450
NLCNLNYGEG PKAHIRKLAE CIRWSYGAGV VLRLGNIARL ELNYCIPMGV
460
QGGDRICDGV QFGAGIRFL
Length:469
Mass (Da):51,864
Last modified:March 1, 2003 - v1
Checksum:i9A9F99114CD01B31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421N → D in BAE36358 (PubMed:16141072).Curated
Sequence conflicti337 – 3371F → V in BAE35333 (PubMed:16141072).Curated
Sequence conflicti465 – 4651G → R in BAE39833 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039949 mRNA. Translation: BAC30484.1.
BC119180 mRNA. Translation: AAI19181.1.
BC119178 mRNA. Translation: AAI19179.1.
AK159740 mRNA. Translation: BAE35333.1.
AK161378 mRNA. Translation: BAE36358.1.
AK167806 mRNA. Translation: BAE39833.1.
AK169351 mRNA. Translation: BAE41101.1.
AK169066 mRNA. Translation: BAE40853.1.
AK168510 mRNA. Translation: BAE40393.1.
AK144975 mRNA. Translation: BAE26162.1.
AK084395 mRNA. Translation: BAC39174.1.
AK041783 mRNA. Translation: BAC31062.1.
CCDSiCCDS37166.1.
RefSeqiNP_848729.1. NM_178614.4.
UniGeneiMm.290725.

Genome annotation databases

EnsembliENSMUST00000023071; ENSMUSP00000023071; ENSMUSG00000022437.
GeneIDi68653.
KEGGimmu:68653.
UCSCiuc007xbx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039949 mRNA. Translation: BAC30484.1.
BC119180 mRNA. Translation: AAI19181.1.
BC119178 mRNA. Translation: AAI19179.1.
AK159740 mRNA. Translation: BAE35333.1.
AK161378 mRNA. Translation: BAE36358.1.
AK167806 mRNA. Translation: BAE39833.1.
AK169351 mRNA. Translation: BAE41101.1.
AK169066 mRNA. Translation: BAE40853.1.
AK168510 mRNA. Translation: BAE40393.1.
AK144975 mRNA. Translation: BAE26162.1.
AK084395 mRNA. Translation: BAC39174.1.
AK041783 mRNA. Translation: BAC31062.1.
CCDSiCCDS37166.1.
RefSeqiNP_848729.1. NM_178614.4.
UniGeneiMm.290725.

3D structure databases

ProteinModelPortaliQ8BGH2.
SMRiQ8BGH2. Positions 47-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212974. 51 interactions.
IntActiQ8BGH2. 52 interactions.
MINTiMINT-4110307.
STRINGi10090.ENSMUSP00000023071.

PTM databases

iPTMnetiQ8BGH2.
PhosphoSiteiQ8BGH2.
SwissPalmiQ8BGH2.

2D gel databases

REPRODUCTION-2DPAGEQ8BGH2.

Proteomic databases

EPDiQ8BGH2.
MaxQBiQ8BGH2.
PaxDbiQ8BGH2.
PRIDEiQ8BGH2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023071; ENSMUSP00000023071; ENSMUSG00000022437.
GeneIDi68653.
KEGGimmu:68653.
UCSCiuc007xbx.1. mouse.

Organism-specific databases

CTDi25813.
MGIiMGI:1915903. Samm50.

Phylogenomic databases

eggNOGiKOG2602. Eukaryota.
COG4775. LUCA.
GeneTreeiENSGT00390000011355.
HOGENOMiHOG000015411.
HOVERGENiHBG054614.
InParanoidiQ8BGH2.
KOiK07277.
OMAiWDQTSEV.
OrthoDBiEOG7VMP51.
PhylomeDBiQ8BGH2.
TreeFamiTF106126.

Miscellaneous databases

PROiQ8BGH2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGH2.
GenevisibleiQ8BGH2. MM.

Family and domain databases

InterProiIPR000184. Bac_surfAg_D15.
[Graphical view]
PfamiPF01103. Bac_surface_Ag. 1 hit.
[Graphical view]
PROSITEiPS51779. POTRA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Eye, Heart, Mammary gland, Stomach, Testis and Thymus.
  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: Brain.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-57; 281-297 AND 393-412, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "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 CHCHD3.

Entry informationi

Entry nameiSAM50_MOUSE
AccessioniPrimary (citable) accession number: Q8BGH2
Secondary accession number(s): Q3TIL3, Q3TTG7, Q3TWD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.