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O54990

- PROM1_MOUSE

UniProt

O54990 - PROM1_MOUSE

Protein

Prominin-1

Gene

Prom1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis (PubMed:19228982). Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner.1 Publication

    GO - Biological processi

    1. camera-type eye photoreceptor cell differentiation Source: UniProtKB
    2. retina layer formation Source: UniProtKB

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prominin-1
    Alternative name(s):
    Antigen AC133 homolog
    Prominin-like protein 1
    CD_antigen: CD133
    Gene namesi
    Name:Prom1
    Synonyms:Prom, Proml1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1100886. Prom1.

    Subcellular locationi

    Apical cell membrane; Multi-pass membrane protein. Cell projectionmicrovillus membrane; Multi-pass membrane protein. Cell projectionciliumphotoreceptor outer segment. Endoplasmic reticulum By similarity. Endoplasmic reticulum-Golgi intermediate compartment By similarity
    Note: Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine.

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProt
    2. brush border Source: MGI
    3. cell projection Source: MGI
    4. cell surface Source: MGI
    5. cilium Source: UniProt
    6. extracellular space Source: MGI
    7. integral component of plasma membrane Source: MGI
    8. microvillus Source: MGI
    9. microvillus membrane Source: UniProtKB-SubCell
    10. photoreceptor outer segment Source: UniProtKB
    11. plasma membrane Source: MGI
    12. prominosome Source: UniProtKB
    13. stereocilium Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cilium, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Progressive degeneration and functional deterioration of both cone and rod photoreceptors associated with impaired morphogenesis of the disks and OS.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 867848Prominin-1PRO_0000025814Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei226 – 2261N6-acetyllysineBy similarity
    Modified residuei258 – 2581N6-acetyllysineBy similarity
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
    Glycosylationi291 – 2911N-linked (GlcNAc...)1 Publication
    Glycosylationi332 – 3321N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)1 Publication
    Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi581 – 5811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi732 – 7321N-linked (GlcNAc...)Sequence Analysis
    Modified residuei865 – 8651PhosphoserineBy similarity

    Post-translational modificationi

    Acetylation at Lys-226, Lys-258 and Lys-265 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis.

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO54990.
    PaxDbiO54990.
    PRIDEiO54990.

    PTM databases

    PhosphoSiteiO54990.

    Expressioni

    Tissue specificityi

    In the submandibular gland, expressed on the apical side of epithelial cells. In the parotid gland, expressed in the intercalated ducts. In the sublingual gland, expressed in intercalated ducts. In the extraorbital lacrimal gland, expressed in the intercalated tubules and larger intralobular ducts. Expressed in the retina. Present in urine within small membrane particles (at protein level). In the embryo, expressed on the apical side of neuroepithelial cells and of other epithelia such as lung buds, gut and ureter buds. In the adult, expressed at the apical side of the kidney tubules and of the ependymal layer of the brain. Not expressed in gut, liver, lung, pituitary, adrenal, heart or spleen. Localized to the nascent disk membranes at the base of the rod outer segment in the retina (at protein level).4 Publications

    Developmental stagei

    At birth, is detected at the interface between the developing neuroretina and the retinal pigment epithelium (RPE) layer. In the postnatal retina (P20) detected in photoreceptors, with particular concentration in the region of plasma membrane evaginations at the basal part of the outer segment (OS). Expressed by rod and cone photoreceptor cells, most abundantly between the OS and inner segment (IS), in close proximity to the connecting cilium.1 Publication

    Gene expression databases

    ArrayExpressiO54990.
    BgeeiO54990.
    CleanExiMM_PROM1.
    GenevestigatoriO54990.

    Interactioni

    Subunit structurei

    Interacts with CDHR1 and with actin filaments. Interacts with NAT8 and NAT8B By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202393. 1 interaction.
    IntActiO54990. 1 interaction.
    MINTiMINT-4108629.
    STRINGi10090.ENSMUSP00000073751.

    Structurei

    3D structure databases

    ProteinModelPortaliO54990.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 10788ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini129 – 15830CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini180 – 434255ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini456 – 48732CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini509 – 794286ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini816 – 86752CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei108 – 12821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei159 – 17921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei435 – 45521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei488 – 50821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei795 – 81521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prominin family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG322325.
    GeneTreeiENSGT00530000063586.
    HOGENOMiHOG000115704.
    HOVERGENiHBG053690.
    InParanoidiO54990.
    KOiK06532.
    OrthoDBiEOG7TQV02.
    PhylomeDBiO54990.

    Family and domain databases

    InterProiIPR008795. Prominin.
    [Graphical view]
    PANTHERiPTHR22730. PTHR22730. 1 hit.
    PfamiPF05478. Prominin. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: O54990-1) [UniParc]FASTAAdd to Basket

    Also known as: S2

    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

    MALVFSALLL LGLCGKISSE GQPAFHNTPG AMNYELPTTK YETQDTFNAG    50
    IVGPLYKMVH IFLSVVQPND FPLDLIKKLI QNKKFDISVD SKEPEIIVLA 100
    LKIALYEIGV LICAILGLLF IILMPLVGCF FCMCRCCNKC GGEMHQRQKQ 150
    NAPCRRKCLG LSLLVICLLM SLGIIYGFVA NQQTRTRIKG TQKLAKSNFR 200
    DFQTLLTETP KQIDYVVEQY TNTKNKAFSD LDGIGSVLGG RIKDQLKPKV 250
    TPVLEEIKAM ATAIKQTKDA LQNMSSSLKS LQDAATQLNT NLSSVRNSIE 300
    NSLSSSDCTS DPASKICDSI RPSLSSLGSS LNSSQLPSVD RELNTVTEVD 350
    KTDLESLVKR GYTTIDEIPN TIQNQTVDVI KDVKNTLDSI SSNIKDMSQS 400
    IPIEDMLLQV SHYLNNSNRY LNQELPKLEE YDSYWWLGGL IVCFLLTLIV 450
    TFFFLGLLCG VFGYDKHATP TRRGCVSNTG GIFLMAGVGF GFLFCWILMI 500
    LVVLTFVVGA NVEKLLCEPY ENKKLLQVLD TPYLLKEQWQ FYLSGMLFNN 550
    PDINMTFEQV YRDCKRGRGI YAAFQLENVV NVSDHFNIDQ ISENINTELE 600
    NLNVNIDSIE LLDNTGRKSL EDFAHSGIDT IDYSTYLKET EKSPTEVNLL 650
    TFASTLEAKA NQLPEGKPKQ AFLLDVQNIR AIHQHLLPPV QQSLNTLRQS 700
    VWTLQQTSNK LPEKVKKILA SLDSVQHFLT NNVSLIVIGE TKKFGKTILG 750
    YFEHYLHWVF YAITEKMTSC KPMATAMDSA VNGILCGYVA DPLNLFWFGI 800
    GKATVLLLPA VIIAIKLAKY YRRMDSEDVY DDVETVPMKN LEIGSNGYHK 850
    DHLYGVHNPV MTSPSRY 867
    Length:867
    Mass (Da):97,113
    Last modified:June 1, 1998 - v1
    Checksum:iD442F6372552B3C8
    GO
    Isoform 2 (identifier: O54990-2) [UniParc]FASTAAdd to Basket

    Also known as: S1

    The sequence of this isoform differs from the canonical sequence as follows:
         94-102: Missing.

    Show »
    Length:858
    Mass (Da):96,136
    Checksum:iCAFCAD4C3039848D
    GO
    Isoform 3 (identifier: O54990-3) [UniParc]FASTAAdd to Basket

    Also known as: S3

    The sequence of this isoform differs from the canonical sequence as follows:
         94-102: Missing.
         833-843: VETVPMKNLEI → SSVSGMWHFTL
         844-867: Missing.

    Show »
    Length:834
    Mass (Da):93,416
    Checksum:iCAFC85B2596BAB9C
    GO
    Isoform 4 (identifier: O54990-4) [UniParc]FASTAAdd to Basket

    Also known as: S4

    The sequence of this isoform differs from the canonical sequence as follows:
         94-107: Missing.
         335-360: QLPSVDRELNTVTEVDKTDLESLVKR → Q
         833-843: VETVPMKNLEI → SSVSGMWHFTL
         844-867: Missing.

    Show »
    Length:804
    Mass (Da):89,987
    Checksum:iA8C6925524AE94D5
    GO
    Isoform 5 (identifier: O54990-5) [UniParc]FASTAAdd to Basket

    Also known as: S5

    The sequence of this isoform differs from the canonical sequence as follows:
         94-102: Missing.
         335-360: QLPSVDRELNTVTEVDKTDLESLVKR → Q
         833-843: VETVPMKNLEI → SSVSGMWHFTL
         844-867: Missing.

    Show »
    Length:809
    Mass (Da):90,577
    Checksum:i1FF6FB4EF6CB7095
    GO
    Isoform 6 (identifier: O54990-6) [UniParc]FASTAAdd to Basket

    Also known as: S6

    The sequence of this isoform differs from the canonical sequence as follows:
         94-102: Missing.
         832-832: D → E
         833-867: Missing.

    Show »
    Length:823
    Mass (Da):92,197
    Checksum:iE8425D90B970938A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641S → N in AAB86715. (PubMed:9356465)Curated
    Sequence conflicti64 – 641S → N in AAM28245. (PubMed:15316084)Curated
    Sequence conflicti64 – 641S → N in AAO11840. (PubMed:15316084)Curated
    Sequence conflicti64 – 641S → N in AAO72429. (PubMed:15316084)Curated
    Sequence conflicti64 – 641S → N in AAO72430. (PubMed:15316084)Curated
    Sequence conflicti64 – 641S → N in BAC26745. (PubMed:16141072)Curated
    Sequence conflicti84 – 841K → N in AAB86715. (PubMed:9356465)Curated
    Sequence conflicti84 – 841K → N in AAM28245. (PubMed:15316084)Curated
    Sequence conflicti84 – 841K → N in AAO11840. (PubMed:15316084)Curated
    Sequence conflicti84 – 841K → N in AAO72429. (PubMed:15316084)Curated
    Sequence conflicti84 – 841K → N in AAO72430. (PubMed:15316084)Curated
    Sequence conflicti84 – 841K → N in BAC26745. (PubMed:16141072)Curated
    Sequence conflicti668 – 6681P → L in AAB86715. (PubMed:9356465)Curated
    Sequence conflicti668 – 6681P → L in AAM28245. (PubMed:15316084)Curated
    Sequence conflicti668 – 6681P → L in AAO72429. (PubMed:15316084)Curated
    Sequence conflicti668 – 6681P → L in AAO72430. (PubMed:15316084)Curated
    Sequence conflicti668 – 6681P → L in BAC26745. (PubMed:16141072)Curated
    Sequence conflicti844 – 8441G → D in AAB86715. (PubMed:9356465)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei94 – 10714Missing in isoform 4. 1 PublicationVSP_040005Add
    BLAST
    Alternative sequencei94 – 1029Missing in isoform 2, isoform 3, isoform 5 and isoform 6. 3 PublicationsVSP_040006
    Alternative sequencei335 – 36026QLPSV…SLVKR → Q in isoform 4 and isoform 5. 1 PublicationVSP_040007Add
    BLAST
    Alternative sequencei832 – 8321D → E in isoform 6. 1 PublicationVSP_040008
    Alternative sequencei833 – 86735Missing in isoform 6. 1 PublicationVSP_040009Add
    BLAST
    Alternative sequencei833 – 84311VETVPMKNLEI → SSVSGMWHFTL in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_040010Add
    BLAST
    Alternative sequencei844 – 86724Missing in isoform 3, isoform 4 and isoform 5. 2 PublicationsVSP_040011Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039663 mRNA. Translation: AAB96916.1.
    AF026269 mRNA. Translation: AAB86715.1.
    AF305215 mRNA. Translation: AAO11840.1.
    AY099088 mRNA. Translation: AAM28245.1.
    AY223521 mRNA. Translation: AAO72429.1.
    AY223522 mRNA. Translation: AAO72430.1.
    AK030027 mRNA. Translation: BAC26745.1.
    CCDSiCCDS39082.1. [O54990-2]
    CCDS51491.1. [O54990-5]
    CCDS51493.1. [O54990-3]
    CCDS51494.1. [O54990-1]
    PIRiT08881.
    RefSeqiNP_001157050.1. NM_001163578.1.
    NP_001157053.1. NM_001163581.1.
    NP_001157054.1. NM_001163582.1.
    NP_001157055.1. NM_001163583.1.
    UniGeneiMm.6250.

    Genome annotation databases

    EnsembliENSMUST00000030973; ENSMUSP00000030973; ENSMUSG00000029086.
    ENSMUST00000087442; ENSMUSP00000084709; ENSMUSG00000029086.
    GeneIDi19126.
    KEGGimmu:19126.
    UCSCiuc008xii.1. mouse. [O54990-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039663 mRNA. Translation: AAB96916.1 .
    AF026269 mRNA. Translation: AAB86715.1 .
    AF305215 mRNA. Translation: AAO11840.1 .
    AY099088 mRNA. Translation: AAM28245.1 .
    AY223521 mRNA. Translation: AAO72429.1 .
    AY223522 mRNA. Translation: AAO72430.1 .
    AK030027 mRNA. Translation: BAC26745.1 .
    CCDSi CCDS39082.1. [O54990-2 ]
    CCDS51491.1. [O54990-5 ]
    CCDS51493.1. [O54990-3 ]
    CCDS51494.1. [O54990-1 ]
    PIRi T08881.
    RefSeqi NP_001157050.1. NM_001163578.1.
    NP_001157053.1. NM_001163581.1.
    NP_001157054.1. NM_001163582.1.
    NP_001157055.1. NM_001163583.1.
    UniGenei Mm.6250.

    3D structure databases

    ProteinModelPortali O54990.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202393. 1 interaction.
    IntActi O54990. 1 interaction.
    MINTi MINT-4108629.
    STRINGi 10090.ENSMUSP00000073751.

    PTM databases

    PhosphoSitei O54990.

    Proteomic databases

    MaxQBi O54990.
    PaxDbi O54990.
    PRIDEi O54990.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030973 ; ENSMUSP00000030973 ; ENSMUSG00000029086 .
    ENSMUST00000087442 ; ENSMUSP00000084709 ; ENSMUSG00000029086 .
    GeneIDi 19126.
    KEGGi mmu:19126.
    UCSCi uc008xii.1. mouse. [O54990-4 ]

    Organism-specific databases

    CTDi 8842.
    MGIi MGI:1100886. Prom1.

    Phylogenomic databases

    eggNOGi NOG322325.
    GeneTreei ENSGT00530000063586.
    HOGENOMi HOG000115704.
    HOVERGENi HBG053690.
    InParanoidi O54990.
    KOi K06532.
    OrthoDBi EOG7TQV02.
    PhylomeDBi O54990.

    Miscellaneous databases

    NextBioi 295734.
    PROi O54990.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54990.
    Bgeei O54990.
    CleanExi MM_PROM1.
    Genevestigatori O54990.

    Family and domain databases

    InterProi IPR008795. Prominin.
    [Graphical view ]
    PANTHERi PTHR22730. PTHR22730. 1 hit.
    Pfami PF05478. Prominin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel five-transmembrane hematopoietic stem cell antigen: isolation, characterization, and molecular cloning."
      Miraglia S., Godfrey W., Yin A.H., Atkins K., Warnke R., Holden J.T., Bray R.A., Waller E.K., Buck D.W.
      Blood 90:5013-5021(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prominin, a novel microvilli-specific polytopic membrane protein of the apical surface of epithelial cells, is targeted to plasmalemmal protrusions of non-epithelial cells."
      Weigmann A., Corbeil D., Hellwig A., Huttner W.B.
      Proc. Natl. Acad. Sci. U.S.A. 94:12425-12430(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Kidney.
    3. "Identification of novel Prominin-1/CD133 splice variants with alternative C-termini and their expression in epididymis and testis."
      Fargeas C.A., Joester A., Missol-Kolka E., Hellwig A., Huttner W.B., Corbeil D.
      J. Cell Sci. 117:4301-4311(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5 AND 6).
      Strain: BALB/c.
      Tissue: Testis.
    4. "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] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Testis.
    5. "Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane."
      Roeper K., Corbeil D., Huttner W.B.
      Nat. Cell Biol. 2:582-592(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CHOLESTEROL BINDING.
    6. "Characterization of prominin-2, a new member of the prominin family of pentaspan membrane glycoproteins."
      Fargeas C.A., Florek M., Huttner W.B., Corbeil D.
      J. Biol. Chem. 278:8586-8596(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. "Nomenclature of prominin-1 (CD133) splice variants - an update."
      Fargeas C.A., Huttner W.B., Corbeil D.
      Tissue Antigens 69:602-606(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE OF ISOFORMS.
    8. "Prominin-2 is a cholesterol-binding protein associated with apical and basolateral plasmalemmal protrusions in polarized epithelial cells and released into urine."
      Florek M., Bauer N., Janich P., Wilsch-Braeuninger M., Fargeas C.A., Marzesco A.-M., Ehninger G., Thiele C., Huttner W.B., Corbeil D.
      Cell Tissue Res. 328:31-47(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Differential expression of prominin-1 (CD133) and prominin-2 in major cephalic exocrine glands of adult mice."
      Jaszai J., Janich P., Farkas L.M., Fargeas C.A., Huttner W.B., Corbeil D.
      Histochem. Cell Biol. 128:409-419(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "Midbody and primary cilium of neural progenitors release extracellular membrane particles enriched in the stem cell marker prominin-1."
      Dubreuil V., Marzesco A.M., Corbeil D., Huttner W.B., Wilsch-Braeuninger M.
      J. Cell Biol. 176:483-495(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    11. Cited for: TISSUE SPECIFICITY.
    12. "Loss of the cholesterol-binding protein prominin-1/CD133 causes disk dysmorphogenesis and photoreceptor degeneration."
      Zacchigna S., Oh H., Wilsch-Brauninger M., Missol-Kolka E., Jaszai J., Jansen S., Tanimoto N., Tonagel F., Seeliger M., Huttner W.B., Corbeil D., Dewerchin M., Vinckier S., Moons L., Carmeliet P.
      J. Neurosci. 29:2297-2308(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    13. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273; ASN-291 AND ASN-374.

    Entry informationi

    Entry nameiPROM1_MOUSE
    AccessioniPrimary (citable) accession number: O54990
    Secondary accession number(s): O35408
    , Q80XB2, Q80XB3, Q80XB6, Q8BH12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Fundus images and light microscopy of retinal sections from transgenic mice expressing mutant PROM1 reveal progressive retinal abnormalities visible as subretinal deposits and photoreceptor atrophy.

    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