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Q9UJZ1

- STML2_HUMAN

UniProt

Q9UJZ1 - STML2_HUMAN

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Protein

Stomatin-like protein 2, mitochondrial

Gene

STOML2

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

Functioni

Mitochondrial protein that probably regulates the biogenesis and the activity of mitochondria. Stimulates cardiolipin biosynthesis, binds cardiolipin-enriched membranes where it recruits and stabilizes some proteins including prohibitin and may therefore act in the organization of functional microdomains in mitochondrial membranes. Through regulation of the mitochondrial function may play a role into several biological processes including cell migration, cell proliferation, T-cell activation, calcium homeostasis and cellular response to stress. May play a role in calcium homeostasis through negative regulation of calcium efflux from mitochondria. Required for mitochondrial hyperfusion a pro-survival cellular response to stress which results in increased ATP production by mitochondria. May also regulate the organization of functional domains at the plasma membrane and play a role in T-cell activation through association with the T-cell receptor signaling complex and its regulation.6 Publications

GO - Molecular functioni

  1. cardiolipin binding Source: UniProtKB
  2. receptor binding Source: ProtInc

GO - Biological processi

  1. CD4-positive, alpha-beta T cell activation Source: UniProtKB
  2. cellular calcium ion homeostasis Source: UniProtKB
  3. interleukin-2 production Source: UniProtKB
  4. lipid localization Source: UniProtKB
  5. mitochondrial ATP synthesis coupled proton transport Source: UniProtKB
  6. mitochondrial calcium ion transport Source: UniProtKB
  7. mitochondrial protein processing Source: UniProtKB
  8. mitochondrion organization Source: UniProtKB
  9. positive regulation of cardiolipin metabolic process Source: UniProtKB
  10. positive regulation of mitochondrial DNA replication Source: UniProtKB
  11. positive regulation of mitochondrial membrane potential Source: UniProtKB
  12. protein oligomerization Source: UniProtKB
  13. stress-induced mitochondrial fusion Source: UniProtKB
  14. T cell receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Stomatin-like protein 2, mitochondrial
Short name:
SLP-2
Alternative name(s):
EPB72-like protein 2
Paraprotein target 7
Short name:
Paratarg-7
Gene namesi
Name:STOML2
Synonyms:SLP2
ORF Names:HSPC108
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:14559. STOML2.

Subcellular locationi

Mitochondrion inner membrane. Mitochondrion intermembrane space. Cell membrane; Peripheral membrane protein. Membrane raft; Peripheral membrane protein
Note: Behaves as an integral membrane protein of the mitochondrion despite the absence of a detectable transmembrane domain. A minor pool is associated with the plasma membrane and is enriched at the immunological synapse in activated T-cells. Also associates with the actin cytoskeleton and membrane rafts in activated T-cells.

GO - Cellular componenti

  1. cytoskeleton Source: ProtInc
  2. extrinsic component of plasma membrane Source: UniProtKB
  3. membrane raft Source: UniProtKB
  4. mitochondrial inner membrane Source: UniProtKB
  5. mitochondrial intermembrane space Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828MitochondrionCuratedAdd
BLAST
Chaini29 – 356328Stomatin-like protein 2, mitochondrialPRO_0000094031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine; by PKC/PRKCZ1 Publication
Modified residuei124 – 1241Phosphotyrosine1 Publication
Modified residuei145 – 1451N6-acetyllysine; alternate1 Publication
Modified residuei145 – 1451N6-succinyllysine; alternateBy similarity
Modified residuei233 – 2331N6-acetyllysine1 Publication

Post-translational modificationi

Hyperphosphorylated at Ser-17 in some patients with monoclonal gammopathy of undetermined significance (MGUS), multiple myeloma (MM) and Waldenstrom macroglobulinemia due to impaired dephosphorylation by PP2A.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UJZ1.
PaxDbiQ9UJZ1.
PeptideAtlasiQ9UJZ1.
PRIDEiQ9UJZ1.

2D gel databases

OGPiQ9UJZ1.
REPRODUCTION-2DPAGEIPI00334190.

PTM databases

PhosphoSiteiQ9UJZ1.

Expressioni

Tissue specificityi

Ubiquitously expressed at low levels. Expressed in lymphoid tissues (at protein level).3 Publications

Inductioni

Up-regulated in activated B- and T-cells and upon mitochondrial stress by chloramphenicol.2 Publications

Gene expression databases

BgeeiQ9UJZ1.
CleanExiHS_STOML2.
ExpressionAtlasiQ9UJZ1. baseline and differential.
GenevestigatoriQ9UJZ1.

Organism-specific databases

HPAiCAB015944.

Interactioni

Subunit structurei

Forms homooligomers. Interacts with MFN2; may form heterooligomers. Interacts with CACNA2D2 (By similarity). Interacts with PHB and PHB2; recruits them to cardiolipin-enriched mitochondrial membranes and stabilizes them.By similarity3 Publications

Protein-protein interaction databases

BioGridi119062. 27 interactions.
IntActiQ9UJZ1. 8 interactions.
MINTiMINT-2999996.
STRINGi9606.ENSP00000348886.

Structurei

3D structure databases

ProteinModelPortaliQ9UJZ1.
SMRiQ9UJZ1. Positions 76-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili215 – 25238Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the band 7/mec-2 family.Curated

Keywords - Domaini

Coiled coil, Transit peptide

Phylogenomic databases

eggNOGiCOG0330.
GeneTreeiENSGT00550000074454.
HOGENOMiHOG000217038.
HOVERGENiHBG061488.
InParanoidiQ9UJZ1.
OMAiDYWGIRC.
OrthoDBiEOG77M8NR.
PhylomeDBiQ9UJZ1.
TreeFamiTF105750.

Family and domain databases

InterProiIPR001107. Band_7.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERiPTHR10264. PTHR10264. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSiPR00721. STOMATIN.
SMARTiSM00244. PHB. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJZ1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLARAARGTG ALLLRGSLLA SGRAPRRASS GLPRNTVVLF VPQQEAWVVE
60 70 80 90 100
RMGRFHRILE PGLNILIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ
110 120 130 140 150
IDGVLYLRIM DPYKASYGVE DPEYAVTQLA QTTMRSELGK LSLDKVFRER
160 170 180 190 200
ESLNASIVDA INQAADCWGI RCLRYEIKDI HVPPRVKESM QMQVEAERRK
210 220 230 240 250
RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA AGEASAVLAK
260 270 280 290 300
AKAKAEAIRI LAAALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTILLPS
310 320 330 340 350
NPGDVTSMVA QAMGVYGALT KAPVPGTPDS LSSGSSRDVQ GTDASLDEEL

DRVKMS
Length:356
Mass (Da):38,534
Last modified:May 1, 2000 - v1
Checksum:i672331B57C82654E
GO
Isoform 2 (identifier: Q9UJZ1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-193: Missing.

Note: No experimental confirmation available.

Show »
Length:311
Mass (Da):33,337
Checksum:i3C391E1AFC830705
GO

Sequence cautioni

The sequence AAC07983.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence AAF29073.1 differs from that shown. Reason: Frameshift at positions 14 and 26. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141L → M in AAC07983. (PubMed:15164053)Curated
Sequence conflicti83 – 831V → I in BAD96822. 1 PublicationCurated
Sequence conflicti202 – 2021A → P in AAF29073. (PubMed:11042152)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291L → P.1 Publication
Corresponds to variant rs17856326 [ dbSNP | Ensembl ].
VAR_026830

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei149 – 19345Missing in isoform 2. 1 PublicationVSP_054651Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190167 mRNA. Translation: AAF09142.1.
AF282596 mRNA. Translation: AAF91466.1.
AK027405 mRNA. Translation: BAB55091.1.
AK303883 mRNA. Translation: BAG64819.1.
AK223102 mRNA. Translation: BAD96822.1.
AL353795 Genomic DNA. Translation: CAH70998.1.
AC004472 Genomic DNA. Translation: AAC07983.1. Sequence problems.
CH471071 Genomic DNA. Translation: EAW58395.1.
CH471071 Genomic DNA. Translation: EAW58396.1.
BC002442 mRNA. Translation: AAH02442.1.
BC003025 mRNA. Translation: AAH03025.1.
BC010152 mRNA. Translation: AAH10152.1.
BC014990 mRNA. Translation: AAH14990.1.
AF161458 mRNA. Translation: AAF29073.1. Frameshift.
CCDSiCCDS6577.1. [Q9UJZ1-1]
CCDS69588.1. [Q9UJZ1-2]
PIRiT02246.
RefSeqiNP_001273960.1. NM_001287031.1. [Q9UJZ1-2]
NP_001273961.1. NM_001287032.1.
NP_038470.1. NM_013442.2. [Q9UJZ1-1]
UniGeneiHs.3439.

Genome annotation databases

EnsembliENST00000356493; ENSP00000348886; ENSG00000165283. [Q9UJZ1-1]
ENST00000452248; ENSP00000395743; ENSG00000165283. [Q9UJZ1-2]
GeneIDi30968.
KEGGihsa:30968.
UCSCiuc003zwi.3. human. [Q9UJZ1-1]
uc011lou.2. human.

Polymorphism databases

DMDMi60415944.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190167 mRNA. Translation: AAF09142.1 .
AF282596 mRNA. Translation: AAF91466.1 .
AK027405 mRNA. Translation: BAB55091.1 .
AK303883 mRNA. Translation: BAG64819.1 .
AK223102 mRNA. Translation: BAD96822.1 .
AL353795 Genomic DNA. Translation: CAH70998.1 .
AC004472 Genomic DNA. Translation: AAC07983.1 . Sequence problems.
CH471071 Genomic DNA. Translation: EAW58395.1 .
CH471071 Genomic DNA. Translation: EAW58396.1 .
BC002442 mRNA. Translation: AAH02442.1 .
BC003025 mRNA. Translation: AAH03025.1 .
BC010152 mRNA. Translation: AAH10152.1 .
BC014990 mRNA. Translation: AAH14990.1 .
AF161458 mRNA. Translation: AAF29073.1 . Frameshift.
CCDSi CCDS6577.1. [Q9UJZ1-1 ]
CCDS69588.1. [Q9UJZ1-2 ]
PIRi T02246.
RefSeqi NP_001273960.1. NM_001287031.1. [Q9UJZ1-2 ]
NP_001273961.1. NM_001287032.1.
NP_038470.1. NM_013442.2. [Q9UJZ1-1 ]
UniGenei Hs.3439.

3D structure databases

ProteinModelPortali Q9UJZ1.
SMRi Q9UJZ1. Positions 76-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119062. 27 interactions.
IntActi Q9UJZ1. 8 interactions.
MINTi MINT-2999996.
STRINGi 9606.ENSP00000348886.

PTM databases

PhosphoSitei Q9UJZ1.

Polymorphism databases

DMDMi 60415944.

2D gel databases

OGPi Q9UJZ1.
REPRODUCTION-2DPAGE IPI00334190.

Proteomic databases

MaxQBi Q9UJZ1.
PaxDbi Q9UJZ1.
PeptideAtlasi Q9UJZ1.
PRIDEi Q9UJZ1.

Protocols and materials databases

DNASUi 30968.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356493 ; ENSP00000348886 ; ENSG00000165283 . [Q9UJZ1-1 ]
ENST00000452248 ; ENSP00000395743 ; ENSG00000165283 . [Q9UJZ1-2 ]
GeneIDi 30968.
KEGGi hsa:30968.
UCSCi uc003zwi.3. human. [Q9UJZ1-1 ]
uc011lou.2. human.

Organism-specific databases

CTDi 30968.
GeneCardsi GC09M035099.
HGNCi HGNC:14559. STOML2.
HPAi CAB015944.
MIMi 608292. gene.
neXtProti NX_Q9UJZ1.
PharmGKBi PA37897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0330.
GeneTreei ENSGT00550000074454.
HOGENOMi HOG000217038.
HOVERGENi HBG061488.
InParanoidi Q9UJZ1.
OMAi DYWGIRC.
OrthoDBi EOG77M8NR.
PhylomeDBi Q9UJZ1.
TreeFami TF105750.

Miscellaneous databases

ChiTaRSi STOML2. human.
GeneWikii STOML2.
GenomeRNAii 30968.
NextBioi 35477056.
PROi Q9UJZ1.
SOURCEi Search...

Gene expression databases

Bgeei Q9UJZ1.
CleanExi HS_STOML2.
ExpressionAtlasi Q9UJZ1. baseline and differential.
Genevestigatori Q9UJZ1.

Family and domain databases

InterProi IPR001107. Band_7.
IPR001972. Stomatin_fam.
[Graphical view ]
PANTHERi PTHR10264. PTHR10264. 1 hit.
Pfami PF01145. Band_7. 1 hit.
[Graphical view ]
PRINTSi PR00721. STOMATIN.
SMARTi SM00244. PHB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of human SLP-2, a novel homologue of stomatin (band 7.2b) present in erythrocytes and other tissues."
    Wang Y., Morrow J.S.
    J. Biol. Chem. 275:8062-8071(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Heart muscle.
  2. "A novel member of the stomatin/EPB72/mec-2 family, stomatin-like 2 (STOML2), is ubiquitously expressed and localizes to HSA chromosome 9p13.1."
    Owczarek C.M., Treutlein H.R., Portbury K.J., Gulluyan L.M., Kola I., Hertzog P.J.
    Cytogenet. Cell Genet. 92:196-203(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Trachea.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1), VARIANT PRO-129.
    Tissue: Lung, Pancreas and Skin.
  8. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-356 (ISOFORM 1).
    Tissue: Umbilical cord blood.
  9. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 188-197; 201-211 AND 234-250, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  10. "Mass spectrometrical verification of stomatin-like protein 2 (SLP-2) primary structure."
    John J.P., Anrather D., Pollak A., Lubec G.
    Proteins 64:543-551(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Identification of a novel mitochondrial complex containing mitofusin 2 and stomatin-like protein 2."
    Hajek P., Chomyn A., Attardi G.
    J. Biol. Chem. 282:5670-5681(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MFN2, SUBCELLULAR LOCATION.
  13. "SLP-2 interacts with prohibitins in the mitochondrial inner membrane and contributes to their stability."
    Da Cruz S., Parone P.A., Gonzalo P., Bienvenut W.V., Tondera D., Jourdain A., Quadroni M., Martinou J.C.
    Biochim. Biophys. Acta 1783:904-911(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PHB AND PHB2.
  14. Cited for: FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  15. "Downregulation of a mitochondria associated protein SLP-2 inhibits tumor cell motility, proliferation and enhances cell sensitivity to chemotherapeutic reagents."
    Wang Y., Cao W., Yu Z., Liu Z.
    Cancer Biol. Ther. 8:1651-1658(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. "A frequent target of paraproteins in the sera of patients with multiple myeloma and MGUS."
    Preuss K.D., Pfreundschuh M., Ahlgrimm M., Fadle N., Regitz E., Murawski N., Grass S.
    Int. J. Cancer 125:656-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A COMMON ANTIGEN IN B-CELL NEOPLASMS.
  17. "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-145 AND LYS-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "SLP-2 negatively modulates mitochondrial sodium-calcium exchange."
    Da Cruz S., De Marchi U., Frieden M., Parone P.A., Martinou J.C., Demaurex N.
    Cell Calcium 47:11-18(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CALCIUM HOMEOSTASIS.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Hyperphosphorylation of autoantigenic targets of paraproteins is due to inactivation of PP2A."
    Preuss K.D., Pfreundschuh M., Fadle N., Regitz E., Raudies S., Murwaski N., Ahlgrimm M., Bittenbring J., Klotz M., Schafer K.H., Held G., Neumann F., Grass S.
    Blood 118:3340-3346(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-17.
  21. "Stomatin-like protein 2 binds cardiolipin and regulates mitochondrial biogenesis and function."
    Christie D.A., Lemke C.D., Elias I.M., Chau L.A., Kirchhof M.G., Li B., Ball E.H., Dunn S.D., Hatch G.M., Madrenas J.
    Mol. Cell. Biol. 31:3845-3856(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MITOCHONDRIAL BIOGENESIS, SUBCELLULAR LOCATION, INTERACTION WITH PHB AND PHB2, CARDIOLIPIN-BINDING, INDUCTION.
  22. "Mitochondrial and plasma membrane pools of stomatin-like protein 2 coalesce at the immunological synapse during T cell activation."
    Christie D.A., Kirchhof M.G., Vardhana S., Dustin M.L., Madrenas J.
    PLoS ONE 7:E37144-E37144(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN T-CELL ACTIVATION, SUBCELLULAR LOCATION, HOMOOLIGOMERIZATION.

Entry informationi

Entry nameiSTML2_HUMAN
AccessioniPrimary (citable) accession number: Q9UJZ1
Secondary accession number(s): B4E1K7
, D3DRN3, O60376, Q53G29, Q96FY2, Q9P042
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 118 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

Miscellaneous

Paratarg-7/STOML2 is a frequent autoantigenic target in monoclonal gammopathy of undetermined significance (MGUS), multiple myeloma (MM) and Waldenstrom macroglobulinemia, 3 B-cell neoplasms associated with excessive secretion of a single monoclonal gammaglobulin (also named paraprotein) in the blood.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3