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Q8R0G7

- SPNS1_MOUSE

UniProt

Q8R0G7 - SPNS1_MOUSE

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Protein

Protein spinster homolog 1

Gene

Spns1

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

Functioni

Sphingolipid transporter. May be involved in necrotic or autophagic cell death (By similarity).By similarity

GO - Biological processi

  1. lipid transport Source: UniProtKB-KW
  2. transmembrane transport Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein spinster homolog 1
Gene namesi
Name:Spns1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1920908. Spns1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei60 – 8021HelicalSequence AnalysisAdd
BLAST
Transmembranei98 – 11821HelicalSequence AnalysisAdd
BLAST
Transmembranei126 – 14621HelicalSequence AnalysisAdd
BLAST
Transmembranei160 – 18021HelicalSequence AnalysisAdd
BLAST
Transmembranei187 – 20721HelicalSequence AnalysisAdd
BLAST
Transmembranei218 – 23821HelicalSequence AnalysisAdd
BLAST
Transmembranei278 – 29821HelicalSequence AnalysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence AnalysisAdd
BLAST
Transmembranei357 – 37721HelicalSequence AnalysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence AnalysisAdd
BLAST
Transmembranei421 – 44121HelicalSequence AnalysisAdd
BLAST
Transmembranei465 – 48521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. lysosomal membrane Source: Ensembl
  3. mitochondrial inner membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 528527Protein spinster homolog 1PRO_0000305040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8R0G7.
PaxDbiQ8R0G7.
PRIDEiQ8R0G7.

PTM databases

PhosphoSiteiQ8R0G7.

Expressioni

Gene expression databases

BgeeiQ8R0G7.
CleanExiMM_SPNS1.
ExpressionAtlasiQ8R0G7. baseline and differential.
GenevestigatoriQ8R0G7.

Interactioni

Subunit structurei

Interacts with BCL2 and BCL2L1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ8R0G7.
SMRiQ8R0G7. Positions 419-447.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00390000005976.
HOGENOMiHOG000276167.
HOVERGENiHBG055503.
InParanoidiQ8R0G7.
OMAiGPTDDRI.
OrthoDBiEOG783MVC.
PhylomeDBiQ8R0G7.
TreeFamiTF314395.

Family and domain databases

InterProiIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8R0G7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGSDTAPFL SQADDPDDGP APGHPGLPGP MGNPKSGELE VPDCEGLQRI
60 70 80 90 100
TGLSRGHSTL IVVVLCYINL LNYMDRFTVA GVLTDIEQFF NIGDGSTGLI
110 120 130 140 150
QTVFISSYMV LAPVFGYLGD RYNRKYLMCG GIAFWSLVTL GSSFIPREHF
160 170 180 190 200
WLLLLTRGLV GVGEASYSTI APTLIADLFV ADQRSRMLSI FYFAIPVGSG
210 220 230 240 250
LGYIAGSKVK DVAGDWHWAL RVTPGLGVLA VLLLFLVVQE PPRGAVERHS
260 270 280 290 300
GSPPLSPTSW WADLKALARN PSFVLSSLGF TSVAFVTGSL ALWAPAFLLR
310 320 330 340 350
SRVVLGETPP CLPGDSCSSS DSLIFGLITC LTGVLGVGLG VEISRRLRRF
360 370 380 390 400
NPRADPLVCA AGLLGSAPFL FLALACARGS IVATYIFIFI GETLLSMNWA
410 420 430 440 450
IVADILLYVV IPTRRSTAEA FQIVLSHLLG DAGSPYLIGL ISDRLRRSWP
460 470 480 490 500
PSFLSEFRAL QFSLMLCAFV GALGGAAFLG TAMFIEDDRR RAQLHVQGLL
510 520
HESGPSDDRI VVPQRGRSTR VPVSSVLI
Length:528
Mass (Da):56,709
Last modified:June 1, 2002 - v1
Checksum:iDDAB448D7D2B9E17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601L → I in BAE39125. (PubMed:16141072)Curated
Sequence conflicti121 – 1211R → K in AAH02297. (PubMed:15489334)Curated
Sequence conflicti127 – 1271L → F in AAG43831. (PubMed:11340170)Curated
Sequence conflicti154 – 1541L → F in AAG43831. (PubMed:11340170)Curated
Sequence conflicti159 – 1591L → M in AAG43831. (PubMed:11340170)Curated
Sequence conflicti178 – 1781L → F in AAG43831. (PubMed:11340170)Curated
Sequence conflicti341 – 3411V → M in AAG43831. (PubMed:11340170)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212372 mRNA. Translation: AAG43831.1.
AK166931 mRNA. Translation: BAE39125.1.
BC002297 mRNA. Translation: AAH02297.1.
BC026854 mRNA. Translation: AAH26854.1.
BC085491 mRNA. Translation: AAH85491.1.
CCDSiCCDS21826.1.
RefSeqiNP_076201.2. NM_023712.3.
UniGeneiMm.11112.

Genome annotation databases

EnsembliENSMUST00000032994; ENSMUSP00000032994; ENSMUSG00000030741.
GeneIDi73658.
KEGGimmu:73658.
UCSCiuc009jqy.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF212372 mRNA. Translation: AAG43831.1 .
AK166931 mRNA. Translation: BAE39125.1 .
BC002297 mRNA. Translation: AAH02297.1 .
BC026854 mRNA. Translation: AAH26854.1 .
BC085491 mRNA. Translation: AAH85491.1 .
CCDSi CCDS21826.1.
RefSeqi NP_076201.2. NM_023712.3.
UniGenei Mm.11112.

3D structure databases

ProteinModelPortali Q8R0G7.
SMRi Q8R0G7. Positions 419-447.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8R0G7.

Proteomic databases

MaxQBi Q8R0G7.
PaxDbi Q8R0G7.
PRIDEi Q8R0G7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032994 ; ENSMUSP00000032994 ; ENSMUSG00000030741 .
GeneIDi 73658.
KEGGi mmu:73658.
UCSCi uc009jqy.3. mouse.

Organism-specific databases

CTDi 83985.
MGIi MGI:1920908. Spns1.

Phylogenomic databases

eggNOGi COG0477.
GeneTreei ENSGT00390000005976.
HOGENOMi HOG000276167.
HOVERGENi HBG055503.
InParanoidi Q8R0G7.
OMAi GPTDDRI.
OrthoDBi EOG783MVC.
PhylomeDBi Q8R0G7.
TreeFami TF314395.

Miscellaneous databases

ChiTaRSi Spns1. mouse.
NextBioi 338727.
PROi Q8R0G7.
SOURCEi Search...

Gene expression databases

Bgeei Q8R0G7.
CleanExi MM_SPNS1.
ExpressionAtlasi Q8R0G7. baseline and differential.
Genevestigatori Q8R0G7.

Family and domain databases

InterProi IPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view ]
Pfami PF07690. MFS_1. 1 hit.
[Graphical view ]
SUPFAMi SSF103473. SSF103473. 1 hit.
PROSITEi PS50850. MFS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in the novel membrane protein spinster interfere with programmed cell death and cause neural degeneration in Drosophila melanogaster."
    Nakano Y., Fujitani K., Kurihara J., Ragan J., Usui-Aoki K., Shimoda L., Lukacsovich T., Suzuki K., Sezaki M., Sano Y., Ueda R., Awano W., Kaneda M., Umeda M., Yamamoto D.
    Mol. Cell. Biol. 21:3775-3788(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: C57BL/6J and Czech II.
    Tissue: Mammary tumor.
  3. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Kidney.

Entry informationi

Entry nameiSPNS1_MOUSE
AccessioniPrimary (citable) accession number: Q8R0G7
Secondary accession number(s): Q3TKM0, Q99LN7, Q9EQK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 90 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, 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

External Data

Dasty 3