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

O43490 (PROM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prominin-1
Alternative name(s):
Antigen AC133
Prominin-like protein 1
CD_antigen=CD133
Gene names
Name:PROM1
Synonyms:PROML1
ORF Names:MSTP061
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length865 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds cholesterol in cholesterol-containing plasma membrane microdomains. Proposed to play a role in apical plasma membrane organization of epithelial cells. During early 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. Ref.14

Subunit structure

Interacts with CDHR1 and with actin filaments. Ref.18

Subcellular location

Cell projectionciliumphotoreceptor outer segment By similarity Ref.2 Ref.12 Ref.13.

Isoform 1: Apical cell membrane; Multi-pass membrane protein By similarity. Cell projectionmicrovillus membrane; Multi-pass membrane protein By similarity. Note: Found in extracellular membrane particles in various body fluids such as cerebrospinal fluid, saliva, seminal fluid and urine. Ref.2 Ref.12 Ref.13

Tissue specificity

Isoform 1 is selectively expressed on CD34 hematopoietic stem and progenitor cells in adult and fetal bone marrow, fetal liver, cord blood and adult peripheral blood. Isoform 1 is not detected on other blood cells. Isoform 1 is also expressed in a number of non-lymphoid tissues including retina, pancreas, placenta, kidney, liver, lung, brain and heart. Found in saliva within small membrane particles. Isoform 2 is predominantly expressed in fetal liver, skeletal muscle, kidney, and heart as well as adult pancreas, kidney, liver, lung, and placenta. Isoform 2 is highly expressed in fetal liver, low in bone marrow, and barely detectable in peripheral blood. Isoform 2 is expressed on hematopoietic stem cells and in epidermal basal cells (at protein level). Expressed in adult retina by rod and cone photoreceptor cells (at protein level). Ref.2 Ref.10

Post-translational modification

Isoform 1 and isoform 2 are glycosylated. Ref.2

Involvement in disease

Retinitis pigmentosa 41 (RP41) [MIM:612095]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.16

Cone-rod dystrophy 12 (CORD12) [MIM:612657]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Stargardt disease 4 (STGD4) [MIM:603786]: A common hereditary macular degeneration. It is characterized by decreased central vision, atrophy of the macula and underlying retinal pigment epithelium, and frequent presence of prominent flecks in the posterior pole of the retina.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Retinal macular dystrophy 2 (MCDR2) [MIM:608051]: A bull's-eye macular dystrophy characterized by bilateral annular atrophy of retinal pigment epithelium at the macula.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous

Is used as marker for hematopoietic stem and progenitor cells (HSPC) for somatic stem cell isolation.

Sequence similarities

Belongs to the prominin family.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cilium
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCone-rod dystrophy
Disease mutation
Retinitis pigmentosa
Stargardt disease
   DomainSignal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcamera-type eye photoreceptor cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

glomerular parietal epithelial cell differentiation

Inferred from mutant phenotype PubMed 19092120. Source: UniProtKB

glomerular visceral epithelial cell differentiation

Inferred from mutant phenotype PubMed 19092120. Source: UniProtKB

photoreceptor cell maintenance

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

positive regulation of nephron tubule epithelial cell differentiation

Inferred from mutant phenotype PubMed 16885410. Source: UniProtKB

retina layer formation

Inferred from sequence or structural similarity. Source: UniProtKB

retina morphogenesis in camera-type eye

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

brush border

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 16809613. Source: BHF-UCL

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.9. Source: ProtInc

microvillus membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

photoreceptor outer segment

Inferred from sequence or structural similarity. Source: UniProtKB

photoreceptor outer segment membrane

Inferred from direct assay Ref.18. Source: BHF-UCL

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

stereocilium

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactinin binding

Inferred from direct assay Ref.18. Source: BHF-UCL

cadherin binding

Inferred from physical interaction Ref.18. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.18. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdhr1Q8VHP63EBI-3447549,EBI-4395045From a different organism.

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43490-1)

Also known as: AC133-1; 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.
Isoform 2 (identifier: O43490-2)

Also known as: AC133-2; S1;

The sequence of this isoform differs from the canonical sequence as follows:
     92-100: Missing.
Isoform 3 (identifier: O43490-3)

Also known as: S3;

The sequence of this isoform differs from the canonical sequence as follows:
     93-101: Missing.
     831-839: VETIPMKNM → SSWVTSVQC
     840-865: Missing.
Isoform 4 (identifier: O43490-4)

Also known as: S10;

The sequence of this isoform differs from the canonical sequence as follows:
     93-101: Missing.
     839-861: Missing.
Isoform 5 (identifier: O43490-5)

Also known as: S7;

The sequence of this isoform differs from the canonical sequence as follows:
     93-101: Missing.
     831-861: Missing.
Isoform 6 (identifier: O43490-6)

Also known as: S11;

The sequence of this isoform differs from the canonical sequence as follows:
     831-861: Missing.
Isoform 7 (identifier: O43490-7)

Also known as: S12;

The sequence of this isoform differs from the canonical sequence as follows:
     839-861: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 865846Prominin-1
PRO_0000025813

Regions

Topological domain20 – 10889Extracellular Potential
Transmembrane109 – 12921Helical; Potential
Topological domain130 – 15728Cytoplasmic Potential
Transmembrane158 – 17821Helical; Potential
Topological domain179 – 433255Extracellular Potential
Transmembrane434 – 45421Helical; Potential
Topological domain455 – 48632Cytoplasmic Potential
Transmembrane487 – 50721Helical; Potential
Topological domain508 – 792285Extracellular Potential
Transmembrane793 – 81321Helical; Potential
Topological domain814 – 86552Cytoplasmic Potential

Amino acid modifications

Modified residue8631Phosphoserine Ref.17
Glycosylation2201N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation5481N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation7291N-linked (GlcNAc...) Potential
Glycosylation7301N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence92 – 1009Missing in isoform 2.
VSP_039069
Alternative sequence93 – 1019Missing in isoform 3, isoform 4 and isoform 5.
VSP_040000
Alternative sequence831 – 86131Missing in isoform 5 and isoform 6.
VSP_040001
Alternative sequence831 – 8399VETIPMKNM → SSWVTSVQC in isoform 3.
VSP_040002
Alternative sequence839 – 86123Missing in isoform 4 and isoform 7.
VSP_040003
Alternative sequence840 – 86526Missing in isoform 3.
VSP_040004
Natural variant311A → G.
VAR_010382
Natural variant311A → S.
VAR_010383
Natural variant3731R → C in CORD12, STGD4 and MCDR2; affects the interaction with actin. Ref.18
VAR_057961

Experimental info

Sequence conflict2001D → A AA sequence Ref.1
Sequence conflict2001D → P AA sequence Ref.1
Sequence conflict2841S → D AA sequence Ref.1
Sequence conflict2881S → R AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (AC133-1) (S2) [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: D21CBC05ADB2DEDF

FASTA86597,202
        10         20         30         40         50         60 
MALVLGSLLL LGLCGNSFSG GQPSSTDAPK AWNYELPATN YETQDSHKAG PIGILFELVH 

        70         80         90        100        110        120 
IFLYVVQPRD FPEDTLRKFL QKAYESKIDY DKPETVILGL KIVYYEAGII LCCVLGLLFI 

       130        140        150        160        170        180 
ILMPLVGYFF CMCRCCNKCG GEMHQRQKEN GPFLRKCFAI SLLVICIIIS IGIFYGFVAN 

       190        200        210        220        230        240 
HQVRTRIKRS RKLADSNFKD LRTLLNETPE QIKYILAQYN TTKDKAFTDL NSINSVLGGG 

       250        260        270        280        290        300 
ILDRLRPNII PVLDEIKSMA TAIKETKEAL ENMNSTLKSL HQQSTQLSSS LTSVKTSLRS 

       310        320        330        340        350        360 
SLNDPLCLVH PSSETCNSIR LSLSQLNSNP ELRQLPPVDA ELDNVNNVLR TDLDGLVQQG 

       370        380        390        400        410        420 
YQSLNDIPDR VQRQTTTVVA GIKRVLNSIG SDIDNVTQRL PIQDILSAFS VYVNNTESYI 

       430        440        450        460        470        480 
HRNLPTLEEY DSYWWLGGLV ICSLLTLIVI FYYLGLLCGV CGYDRHATPT TRGCVSNTGG 

       490        500        510        520        530        540 
VFLMVGVGLS FLFCWILMII VVLTFVFGAN VEKLICEPYT SKELFRVLDT PYLLNEDWEY 

       550        560        570        580        590        600 
YLSGKLFNKS KMKLTFEQVY SDCKKNRGTY GTLHLQNSFN ISEHLNINEH TGSISSELES 

       610        620        630        640        650        660 
LKVNLNIFLL GAAGRKNLQD FAACGIDRMN YDSYLAQTGK SPAGVNLLSF AYDLEAKANS 

       670        680        690        700        710        720 
LPPGNLRNSL KRDAQTIKTI HQQRVLPIEQ SLSTLYQSVK ILQRTGNGLL ERVTRILASL 

       730        740        750        760        770        780 
DFAQNFITNN TSSVIIEETK KYGRTIIGYF EHYLQWIEFS ISEKVASCKP VATALDTAVD 

       790        800        810        820        830        840 
VFLCSYIIDP LNLFWFGIGK ATVFLLPALI FAVKLAKYYR RMDSEDVYDD VETIPMKNME 

       850        860 
NGNNGYHKDH VYGIHNPVMT SPSQH 

« Hide

Isoform 2 (AC133-2) (S1) [UniParc].

Checksum: DFF0B7AFE0A02582
Show »

FASTA85696,251
Isoform 3 (S3) [UniParc].

Checksum: 00784B26BE20782F
Show »

FASTA83093,270
Isoform 4 (S10) [UniParc].

Checksum: FB1AA693EBCAC598
Show »

FASTA83393,654
Isoform 5 (S7) [UniParc].

Checksum: 735D8F41DA466FE8
Show »

FASTA82592,741
Isoform 6 (S11) [UniParc].

Checksum: 2640B433DC3E9328
Show »

FASTA83493,692
Isoform 7 (S12) [UniParc].

Checksum: 8B7B74818E26D76C
Show »

FASTA84294,605

References

« Hide 'large scale' references
[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), PROTEIN SEQUENCE OF 31-42; 200-211; 280-291 AND 641-656.
Tissue: Fetal liver and Retinoblastoma.
[2]"AC133-2, a novel isoform of human AC133 stem cell antigen."
Yu Y., Flint A., Dvorin E.L., Bischoff J.
J. Biol. Chem. 277:20711-20716(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION.
[3]"Identification and functional analysis of several isoforms of hematopoitic stem cell surface maker prominin-1 (AC133)."
Lin J., Shmelkov S.V., Karajannis M.A., StClair R., Walsh K., Gordon R., Shido K., Lam G., Moussazadeh N., Shim W., Rafii S.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]Wang X.Y., Zhao B., Liu B., Xu Y.Y., Liu Y.Q., Cao H.Q., Sheng H., Ye J., Song L., Wei Y.J., Liu S., Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Aorta.
[5]"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] (ISOFORM 2).
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 2).
Tissue: Colon.
[9]"AC133, a novel marker for human hematopoietic stem and progenitor cells."
Yin A.H., Miraglia S., Zanjani E.D., Almeida-Porada G., Ogawa M., Leary A.G., Olweus J., Kearney J., Buck D.W.
Blood 90:5002-5012(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Fetal liver.
[10]"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.
[11]"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.
[12]"The stem cell marker prominin-1/CD133 on membrane particles in human cerebrospinal fluid offers novel approaches for studying central nervous system disease."
Huttner H.B., Janich P., Koehrmann M., Jaszai J., Siebzehnrubl F., Bluemcke I., Suttorp M., Gahr M., Kuhnt D., Nimsky C., Krex D., Schackert G., Loewenbrueck K., Reichmann H., Juettler E., Hacke W., Schellinger P.D., Schwab S. expand/collapse author list , Wilsch-Braeuninger M., Marzesco A.M., Corbeil D.
Stem Cells 26:698-705(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Release of extracellular membrane vesicles from microvilli of epithelial cells is enhanced by depleting membrane cholesterol."
Marzesco A.M., Wilsch-Brauninger M., Dubreuil V., Janich P., Langenfeld K., Thiele C., Huttner W.B., Corbeil D.
FEBS Lett. 583:897-902(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"CD133 suppresses neuroblastoma cell differentiation via signal pathway modification."
Takenobu H., Shimozato O., Nakamura T., Ochiai H., Yamaguchi Y., Ohira M., Nakagawara A., Kamijo T.
Oncogene 30:97-105(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"A frameshift mutation in prominin (mouse)-like 1 causes human retinal degeneration."
Maw M.A., Corbeil D., Koch J., Hellwig A., Wilson-Wheeler J.C., Bridges R.J., Kumaramanickavel G., John S., Nancarrow D., Roeper K., Weigmann A., Huttner W.B., Denton M.J.
Hum. Mol. Genet. 9:27-34(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RP41.
[16]"Severe retinitis pigmentosa mapped to 4p15 and associated with a novel mutation in the PROM1 gene."
Zhang Q., Zulfiqar F., Xiao X., Riazuddin S.A., Ahmad Z., Caruso R., MacDonald I., Sieving P., Riazuddin S., Hejtmancik J.F.
Hum. Genet. 122:293-299(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RP41.
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Mutant prominin 1 found in patients with macular degeneration disrupts photoreceptor disk morphogenesis in mice."
Yang Z., Chen Y., Lillo C., Chien J., Yu Z., Michaelides M., Klein M., Howes K.A., Li Y., Kaminoh Y., Chen H., Zhao C., Chen Y., Al-Sheikh Y.T., Karan G., Corbeil D., Escher P., Kamaya S. expand/collapse author list , Li C., Johnson S., Frederick J.M., Zhao Y., Wang C., Cameron D.J., Huttner W.B., Schorderet D.F., Munier F.L., Moore A.T., Birch D.G., Baehr W., Hunt D.M., Williams D.S., Zhang K.
J. Clin. Invest. 118:2908-2916(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CORD12/STGD4/MCDR2 CYS-373, INTERACTION WITH CDHR1 AND ACTIN, CHARACTERIZATION OF VARIANT CORD12/STGD4/MCDR2 CYS-373.
+Additional computationally mapped references.

Web resources

Mutations of the PROM1 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027208 mRNA. Translation: AAB92514.1.
AF507034 mRNA. Translation: AAM33415.1.
AY449689 mRNA. Translation: AAS19705.1.
AY449690 mRNA. Translation: AAS19706.1.
AY449691 mRNA. Translation: AAS19707.1.
AY449692 mRNA. Translation: AAS19708.1.
AY449693 mRNA. Translation: AAS19709.1.
AF117225 mRNA. Translation: AAO15307.1.
AK027422 mRNA. Translation: BAG51317.1.
AC005598 Genomic DNA. No translation available.
AC108063 Genomic DNA. No translation available.
CH471069 Genomic DNA. Translation: EAW92750.1.
BC012089 mRNA. Translation: AAH12089.1.
CCDSCCDS47029.1. [O43490-1]
CCDS54746.1. [O43490-2]
CCDS54747.1. [O43490-6]
CCDS54748.1. [O43490-7]
PIRT09050.
RefSeqNP_001139319.1. NM_001145847.1. [O43490-2]
NP_001139320.1. NM_001145848.1. [O43490-2]
NP_001139321.1. NM_001145849.1. [O43490-7]
NP_001139322.1. NM_001145850.1. [O43490-6]
NP_001139323.1. NM_001145851.1. [O43490-4]
NP_001139324.1. NM_001145852.1. [O43490-5]
NP_006008.1. NM_006017.2. [O43490-1]
XP_005248252.1. XM_005248195.2. [O43490-4]
XP_005248253.1. XM_005248196.2. [O43490-5]
XP_006714036.1. XM_006713973.1. [O43490-2]
UniGeneHs.614734.

3D structure databases

ProteinModelPortalO43490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114369. 3 interactions.
IntActO43490. 4 interactions.
MINTMINT-4724549.
STRING9606.ENSP00000415481.

PTM databases

PhosphoSiteO43490.

Proteomic databases

MaxQBO43490.
PaxDbO43490.
PRIDEO43490.

Protocols and materials databases

DNASU8842.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000447510; ENSP00000415481; ENSG00000007062. [O43490-1]
ENST00000505450; ENSP00000426090; ENSG00000007062. [O43490-2]
ENST00000508167; ENSP00000427346; ENSG00000007062. [O43490-2]
ENST00000510224; ENSP00000426809; ENSG00000007062. [O43490-1]
ENST00000539194; ENSP00000443620; ENSG00000007062. [O43490-6]
ENST00000540805; ENSP00000438045; ENSG00000007062. [O43490-7]
ENST00000543373; ENSP00000445526; ENSG00000007062. [O43490-3]
GeneID8842.
KEGGhsa:8842.
UCSCuc003goo.2. human. [O43490-1]
uc003gop.2. human. [O43490-2]
uc003gor.2. human. [O43490-7]
uc003gos.2. human. [O43490-4]
uc003got.2. human. [O43490-6]
uc003gou.2. human. [O43490-5]

Organism-specific databases

CTD8842.
GeneCardsGC04M015965.
GeneReviewsPROM1.
H-InvDBHIX0004116.
HGNCHGNC:9454. PROM1.
HPACAB011525.
HPA004922.
HPA031053.
MIM603786. phenotype.
604365. gene.
608051. phenotype.
612095. phenotype.
612657. phenotype.
neXtProtNX_O43490.
Orphanet1872. Cone rod dystrophy.
319640. Retinal macular dystrophy type 2.
791. Retinitis pigmentosa.
827. Stargardt disease.
PharmGKBPA33807.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322325.
HOGENOMHOG000115704.
HOVERGENHBG053690.
InParanoidO43490.
KOK06532.
OMAIHNPVMT.
OrthoDBEOG7TQV02.
PhylomeDBO43490.
TreeFamTF324631.

Gene expression databases

ArrayExpressO43490.
BgeeO43490.
CleanExHS_PROM1.
GenevestigatorO43490.

Family and domain databases

InterProIPR008795. Prominin.
[Graphical view]
PANTHERPTHR22730. PTHR22730. 1 hit.
PfamPF05478. Prominin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPROM1. human.
GeneWikiCD133.
GenomeRNAi8842.
NextBio33194.
PROO43490.
SOURCESearch...

Entry information

Entry namePROM1_HUMAN
AccessionPrimary (citable) accession number: O43490
Secondary accession number(s): Q6SV49 expand/collapse secondary AC list , Q6SV50, Q6SV51, Q6SV52, Q6SV53, Q96EN6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 136 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 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries