Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UJZ1 (STML2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:STOML2
Synonyms:SLP2
ORF Names:HSPC108
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.14 Ref.15 Ref.18 Ref.21 Ref.22

Subunit structure

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. Ref.12 Ref.13 Ref.21 Ref.22

Subcellular location

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. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21 Ref.22

Tissue specificity

Ubiquitously expressed at low levels. Expressed in lymphoid tissues (at protein level). Ref.1 Ref.2 Ref.14

Induction

Up-regulated in activated B- and T-cells and upon mitochondrial stress by chloramphenicol. Ref.14 Ref.21

Post-translational modification

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. Ref.20

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 (Ref.16).

Sequence similarities

Belongs to the band 7/mec-2 family.

Sequence caution

The sequence AAC07983.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAF29073.1 differs from that shown. Reason: Frameshift at positions 14 and 26.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Transit peptide
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, alpha-beta T cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

T cell receptor signaling pathway

Inferred from mutant phenotype Ref.14. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

interleukin-2 production

Inferred from sequence or structural similarity. Source: UniProtKB

lipid localization

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial ATP synthesis coupled proton transport

Inferred from mutant phenotype Ref.21. Source: UniProtKB

mitochondrial calcium ion transport

Inferred from mutant phenotype Ref.18. Source: UniProtKB

mitochondrial protein processing

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion organization

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of cardiolipin metabolic process

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of mitochondrial DNA replication

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of mitochondrial membrane potential

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein oligomerization

Inferred from direct assay Ref.12. Source: UniProtKB

stress-induced mitochondrial fusion

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoskeleton

Traceable author statement Ref.1. Source: ProtInc

extrinsic component of plasma membrane

Inferred from direct assay Ref.22. Source: UniProtKB

membrane raft

Inferred from direct assay Ref.14. Source: UniProtKB

mitochondrial inner membrane

Inferred from direct assay Ref.12. Source: UniProtKB

mitochondrial intermembrane space

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functioncardiolipin binding

Inferred from direct assay Ref.21. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.21. Source: UniProtKB

receptor binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJZ1-1)

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.
Isoform 2 (identifier: Q9UJZ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-193: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Probable
Chain29 – 356328Stomatin-like protein 2, mitochondrial
PRO_0000094031

Regions

Coiled coil215 – 25238 Potential

Amino acid modifications

Modified residue171Phosphoserine; by PKC/PRKCZ Ref.20
Modified residue1241Phosphotyrosine Ref.11
Modified residue1451N6-acetyllysine; alternate Ref.17
Modified residue1451N6-succinyllysine; alternate By similarity
Modified residue2331N6-acetyllysine Ref.17

Natural variations

Alternative sequence149 – 19345Missing in isoform 2.
VSP_054651
Natural variant1291L → P. Ref.7
Corresponds to variant rs17856326 [ dbSNP | Ensembl ].
VAR_026830

Experimental info

Sequence conflict141L → M in AAC07983. Ref.5
Sequence conflict831V → I in BAD96822. Ref.4
Sequence conflict2021A → P in AAF29073. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 672331B57C82654E

FASTA35638,534
        10         20         30         40         50         60 
MLARAARGTG ALLLRGSLLA SGRAPRRASS GLPRNTVVLF VPQQEAWVVE RMGRFHRILE 

        70         80         90        100        110        120 
PGLNILIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ IDGVLYLRIM DPYKASYGVE 

       130        140        150        160        170        180 
DPEYAVTQLA QTTMRSELGK LSLDKVFRER ESLNASIVDA INQAADCWGI RCLRYEIKDI 

       190        200        210        220        230        240 
HVPPRVKESM QMQVEAERRK RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA 

       250        260        270        280        290        300 
AGEASAVLAK AKAKAEAIRI LAAALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTILLPS 

       310        320        330        340        350 
NPGDVTSMVA QAMGVYGALT KAPVPGTPDS LSSGSSRDVQ GTDASLDEEL DRVKMS 

« Hide

Isoform 2 [UniParc].

Checksum: 3C391E1AFC830705
Show »

FASTA31133,337

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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
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. expand/collapse author list , 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]"Modulation of T cell activation by stomatin-like protein 2."
Kirchhof M.G., Chau L.A., Lemke C.D., Vardhana S., Darlington P.J., Marquez M.E., Taylor R., Rizkalla K., Blanca I., Dustin M.L., Madrenas J.
J. Immunol. 181:1927-1936(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6577.1.
PIRT02246.
RefSeqNP_001273960.1. NM_001287031.1. [Q9UJZ1-2]
NP_001273961.1. NM_001287032.1.
NP_038470.1. NM_013442.2. [Q9UJZ1-1]
UniGeneHs.3439.

3D structure databases

ProteinModelPortalQ9UJZ1.
SMRQ9UJZ1. Positions 76-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119062. 25 interactions.
IntActQ9UJZ1. 8 interactions.
MINTMINT-2999996.
STRING9606.ENSP00000348886.

PTM databases

PhosphoSiteQ9UJZ1.

Polymorphism databases

DMDM60415944.

2D gel databases

OGPQ9UJZ1.
REPRODUCTION-2DPAGEIPI00334190.

Proteomic databases

MaxQBQ9UJZ1.
PaxDbQ9UJZ1.
PeptideAtlasQ9UJZ1.
PRIDEQ9UJZ1.

Protocols and materials databases

DNASU30968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356493; ENSP00000348886; ENSG00000165283.
ENST00000452248; ENSP00000395743; ENSG00000165283.
GeneID30968.
KEGGhsa:30968.
UCSCuc003zwi.3. human. [Q9UJZ1-1]

Organism-specific databases

CTD30968.
GeneCardsGC09M035099.
HGNCHGNC:14559. STOML2.
HPACAB015944.
MIM608292. gene.
neXtProtNX_Q9UJZ1.
PharmGKBPA37897.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0330.
HOGENOMHOG000217038.
HOVERGENHBG061488.
InParanoidQ9UJZ1.
OMADYWGIRC.
OrthoDBEOG77M8NR.
PhylomeDBQ9UJZ1.
TreeFamTF105750.

Gene expression databases

ArrayExpressQ9UJZ1.
BgeeQ9UJZ1.
CleanExHS_STOML2.
GenevestigatorQ9UJZ1.

Family and domain databases

InterProIPR001107. Band_7.
IPR001972. Stomatin_fam.
[Graphical view]
PANTHERPTHR10264. PTHR10264. 1 hit.
PfamPF01145. Band_7. 1 hit.
[Graphical view]
PRINTSPR00721. STOMATIN.
SMARTSM00244. PHB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSTOML2. human.
GeneWikiSTOML2.
GenomeRNAi30968.
NextBio35477056.
PROQ9UJZ1.
SOURCESearch...

Entry information

Entry nameSTML2_HUMAN
AccessionPrimary (citable) accession number: Q9UJZ1
Secondary accession number(s): B4E1K7 expand/collapse secondary AC list , D3DRN3, O60376, Q53G29, Q96FY2, Q9P042
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM