SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O54990

- PROM1_MOUSE

UniProt

O54990 - PROM1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Prominin-1
Gene
Prom1, Prom, Proml1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds cholesterol in cholesterol-containing plasma membrane microdomains. Proposed to play a role in apical plasma membrane organization of epithelial cells. During early during retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner By similarity.1 Publication

GO - Biological processi

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

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
Note: Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine.4 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 10788Extracellular Reviewed prediction
Add
BLAST
Transmembranei108 – 12821Helical; Reviewed prediction
Add
BLAST
Topological domaini129 – 15830Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei159 – 17921Helical; Reviewed prediction
Add
BLAST
Topological domaini180 – 434255Extracellular Reviewed prediction
Add
BLAST
Transmembranei435 – 45521Helical; Reviewed prediction
Add
BLAST
Topological domaini456 – 48732Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei488 – 50821Helical; Reviewed prediction
Add
BLAST
Topological domaini509 – 794286Extracellular Reviewed prediction
Add
BLAST
Transmembranei795 – 81521Helical; Reviewed prediction
Add
BLAST
Topological domaini816 – 86752Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cilium, 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 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 867848Prominin-1
PRO_0000025814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi273 – 2731N-linked (GlcNAc...)1 Publication
Glycosylationi291 – 2911N-linked (GlcNAc...)1 Publication
Glycosylationi332 – 3321N-linked (GlcNAc...) Reviewed prediction
Glycosylationi374 – 3741N-linked (GlcNAc...)1 Publication
Glycosylationi415 – 4151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi554 – 5541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi581 – 5811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi732 – 7321N-linked (GlcNAc...) Reviewed prediction
Modified residuei865 – 8651Phosphoserine By similarity

Keywords - PTMi

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 By similarity.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliO54990.

Family & Domainsi

Sequence similaritiesi

Belongs to the prominin family.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei94 – 10714Missing in isoform 4.
VSP_040005Add
BLAST
Alternative sequencei94 – 1029Missing in isoform 2, isoform 3, isoform 5 and isoform 6.
VSP_040006
Alternative sequencei335 – 36026QLPSV…SLVKR → Q in isoform 4 and isoform 5.
VSP_040007Add
BLAST
Alternative sequencei832 – 8321D → E in isoform 6.
VSP_040008
Alternative sequencei833 – 86735Missing in isoform 6.
VSP_040009Add
BLAST
Alternative sequencei833 – 84311VETVPMKNLEI → SSVSGMWHFTL in isoform 3, isoform 4 and isoform 5.
VSP_040010Add
BLAST
Alternative sequencei844 – 86724Missing in isoform 3, isoform 4 and isoform 5.
VSP_040011Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641S → N in AAB86715. 1 Publication
Sequence conflicti64 – 641S → N in AAM28245. 1 Publication
Sequence conflicti64 – 641S → N in AAO11840. 1 Publication
Sequence conflicti64 – 641S → N in AAO72429. 1 Publication
Sequence conflicti64 – 641S → N in AAO72430. 1 Publication
Sequence conflicti64 – 641S → N in BAC26745. 1 Publication
Sequence conflicti84 – 841K → N in AAB86715. 1 Publication
Sequence conflicti84 – 841K → N in AAM28245. 1 Publication
Sequence conflicti84 – 841K → N in AAO11840. 1 Publication
Sequence conflicti84 – 841K → N in AAO72429. 1 Publication
Sequence conflicti84 – 841K → N in AAO72430. 1 Publication
Sequence conflicti84 – 841K → N in BAC26745. 1 Publication
Sequence conflicti668 – 6681P → L in AAB86715. 1 Publication
Sequence conflicti668 – 6681P → L in AAM28245. 1 Publication
Sequence conflicti668 – 6681P → L in AAO72429. 1 Publication
Sequence conflicti668 – 6681P → L in AAO72430. 1 Publication
Sequence conflicti668 – 6681P → L in BAC26745. 1 Publication
Sequence conflicti844 – 8441G → D in AAB86715. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 108 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

Similar proteinsi