Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q9H902

- REEP1_HUMAN

UniProt

Q9H902 - REEP1_HUMAN

Protein

Receptor expression-enhancing protein 1

Gene

REEP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Required for endoplasmic reticulum (ER) network formation, shaping and remodeling; it links ER tubules to the cytoskeleton. May also enhance the cell surface expression of odorant receptors.1 Publication

    GO - Molecular functioni

    1. microtubule binding Source: UniProtKB
    2. olfactory receptor binding Source: HGNC
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. endoplasmic reticulum tubular network organization Source: UniProtKB
    3. protein insertion into membrane Source: HGNC

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor expression-enhancing protein 1
    Gene namesi
    Name:REEP1
    Synonyms:C2orf23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:25786. REEP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. endoplasmic reticulum Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. mitochondrial membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Spastic paraplegia 31, autosomal dominant (SPG31) [MIM:610250]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191P → L in SPG31. 1 Publication
    VAR_067265
    Natural varianti20 – 201A → E in SPG31; loss of function mutation; shows severely altered localization to numerous punctate small structures throughout the cytoplasm and no localization to the endoplasmic reticulum; does not colocalize with ATL1. 2 Publications
    VAR_027351
    Natural varianti23 – 231S → F in SPG31. 1 Publication
    VAR_067266
    Natural varianti42 – 421W → R in SPG31. 1 Publication
    VAR_067267
    Natural varianti56 – 561D → N in SPG31. 1 Publication
    VAR_067268
    Neuronopathy, distal hereditary motor, 5B (HMN5B) [MIM:614751]: A disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. HMN5B is characterized by onset in the first or second decade of distal muscle weakness and atrophy, primarily affecting the intrinsic hand muscles, but also affecting the lower legs, resulting in abnormal gait and pes cavus.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

    Organism-specific databases

    MIMi610250. phenotype.
    614751. phenotype.
    Orphaneti101011. Autosomal dominant spastic paraplegia type 31.
    139536. Distal hereditary motor neuropathy type 5.
    PharmGKBiPA134906680.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Receptor expression-enhancing protein 1PRO_0000101821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei152 – 1521Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H902.
    PaxDbiQ9H902.
    PRIDEiQ9H902.

    PTM databases

    PhosphoSiteiQ9H902.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H902.
    BgeeiQ9H902.
    CleanExiHS_REEP1.
    GenevestigatoriQ9H902.

    Organism-specific databases

    HPAiHPA058061.

    Interactioni

    Subunit structurei

    Interacts with SPAST and ATL1; it preferentially interacts with SPAST isoform 1. Interacts (via C-terminus) with microtubules. Interacts with odorant receptor proteins By similarity.By similarity

    Protein-protein interaction databases

    BioGridi122377. 2 interactions.
    IntActiQ9H902. 1 interaction.
    STRINGi9606.ENSP00000165698.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H902.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1 – 2121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei35 – 5521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi170 – 1734Poly-Pro

    Sequence similaritiesi

    Belongs to the DP1 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5052.
    HOGENOMiHOG000007472.
    HOVERGENiHBG056861.
    InParanoidiQ9H902.
    KOiK17338.
    OMAiGANTNFG.
    PhylomeDBiQ9H902.
    TreeFamiTF314177.

    Family and domain databases

    InterProiIPR004345. TB2_DP1_HVA22.
    [Graphical view]
    PANTHERiPTHR12300. PTHR12300. 1 hit.
    PfamiPF03134. TB2_DP1_HVA22. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H902-1) [UniParc]FASTAAdd to Basket

    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

    MVSWIISRLV VLIFGTLYPA YYSYKAVKSK DIKEYVKWMM YWIIFALFTT    50
    AETFTDIFLC WFPFYYELKI AFVAWLLSPY TKGSSLLYRK FVHPTLSSKE 100
    KEIDDCLVQA KDRSYDALVH FGKRGLNVAA TAAVMAASKG QGALSERLRS 150
    FSMQDLTTIR GDGAPAPSGP PPPGSGRASG KHGQPKMSRS ASESASSSGT 200
    A 201
    Length:201
    Mass (Da):22,255
    Last modified:March 1, 2001 - v1
    Checksum:i98F120DE100276A9
    GO
    Isoform 2 (identifier: Q9H902-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: MVSWIISRLVVLIFGTLYPAYYSYKAVKSKDIKEY → MDHLQAGG

    Note: No experimental confirmation available.

    Show »
    Length:174
    Mass (Da):18,937
    Checksum:iA640F3EDC043D8C1
    GO
    Isoform 3 (identifier: Q9H902-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: MVSWIISRLVV → MQKVLSNGQTEEVRSGSR

    Note: No experimental confirmation available.

    Show »
    Length:208
    Mass (Da):22,958
    Checksum:i74EEC9189C8D5229
    GO
    Isoform 4 (identifier: Q9H902-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         62-201: FPFYYELKIA...SESASSSGTA → DRVPYRRDCG...STSSSATETT

    Note: No experimental confirmation available.

    Show »
    Length:143
    Mass (Da):16,036
    Checksum:i13E3F4B75BFF1C96
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti19 – 191P → L in SPG31. 1 Publication
    VAR_067265
    Natural varianti20 – 201A → E in SPG31; loss of function mutation; shows severely altered localization to numerous punctate small structures throughout the cytoplasm and no localization to the endoplasmic reticulum; does not colocalize with ATL1. 2 Publications
    VAR_027351
    Natural varianti23 – 231S → F in SPG31. 1 Publication
    VAR_067266
    Natural varianti42 – 421W → R in SPG31. 1 Publication
    VAR_067267
    Natural varianti56 – 561D → N in SPG31. 1 Publication
    VAR_067268

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535MVSWI…DIKEY → MDHLQAGG in isoform 2. 1 PublicationVSP_042573Add
    BLAST
    Alternative sequencei1 – 1111MVSWIISRLVV → MQKVLSNGQTEEVRSGSR in isoform 3. 1 PublicationVSP_043251Add
    BLAST
    Alternative sequencei62 – 201140FPFYY…SSGTA → DRVPYRRDCGASACRTSPPS GETAPLLPRAPHHRGLGGPA ANTASLRCPGVLLRALAAQA PPRILRSRFRKKSTSSSATE TT in isoform 4. 1 PublicationVSP_043252Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY562239 mRNA. Translation: AAT70684.1.
    AK023172 mRNA. Translation: BAB14444.1.
    AK297201 mRNA. Translation: BAH12523.1.
    AK297287 mRNA. Translation: BAH12538.1.
    AK299334 mRNA. Translation: BAH13005.1.
    CR457301 mRNA. Translation: CAG33582.1.
    AC009408 Genomic DNA. Translation: AAX93132.1.
    AC009309 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99457.1.
    CH471053 Genomic DNA. Translation: EAW99458.1.
    BC064846 mRNA. Translation: AAH64846.1.
    CCDSiCCDS1989.1. [Q9H902-1]
    CCDS54372.1. [Q9H902-2]
    CCDS54373.1. [Q9H902-4]
    CCDS54374.1. [Q9H902-3]
    RefSeqiNP_001158202.1. NM_001164730.1. [Q9H902-3]
    NP_001158203.1. NM_001164731.1. [Q9H902-2]
    NP_001158204.1. NM_001164732.1. [Q9H902-4]
    NP_075063.1. NM_022912.2. [Q9H902-1]
    UniGeneiHs.368884.

    Genome annotation databases

    EnsembliENST00000165698; ENSP00000165698; ENSG00000068615. [Q9H902-1]
    ENST00000535845; ENSP00000437567; ENSG00000068615. [Q9H902-2]
    ENST00000538924; ENSP00000438346; ENSG00000068615. [Q9H902-3]
    ENST00000541910; ENSP00000442681; ENSG00000068615. [Q9H902-4]
    GeneIDi65055.
    KEGGihsa:65055.
    UCSCiuc002srh.4. human. [Q9H902-1]
    uc010yth.2. human. [Q9H902-2]
    uc010yti.2. human. [Q9H902-4]
    uc021vke.1. human. [Q9H902-3]

    Polymorphism databases

    DMDMi74733929.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY562239 mRNA. Translation: AAT70684.1 .
    AK023172 mRNA. Translation: BAB14444.1 .
    AK297201 mRNA. Translation: BAH12523.1 .
    AK297287 mRNA. Translation: BAH12538.1 .
    AK299334 mRNA. Translation: BAH13005.1 .
    CR457301 mRNA. Translation: CAG33582.1 .
    AC009408 Genomic DNA. Translation: AAX93132.1 .
    AC009309 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99457.1 .
    CH471053 Genomic DNA. Translation: EAW99458.1 .
    BC064846 mRNA. Translation: AAH64846.1 .
    CCDSi CCDS1989.1. [Q9H902-1 ]
    CCDS54372.1. [Q9H902-2 ]
    CCDS54373.1. [Q9H902-4 ]
    CCDS54374.1. [Q9H902-3 ]
    RefSeqi NP_001158202.1. NM_001164730.1. [Q9H902-3 ]
    NP_001158203.1. NM_001164731.1. [Q9H902-2 ]
    NP_001158204.1. NM_001164732.1. [Q9H902-4 ]
    NP_075063.1. NM_022912.2. [Q9H902-1 ]
    UniGenei Hs.368884.

    3D structure databases

    ProteinModelPortali Q9H902.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122377. 2 interactions.
    IntActi Q9H902. 1 interaction.
    STRINGi 9606.ENSP00000165698.

    PTM databases

    PhosphoSitei Q9H902.

    Polymorphism databases

    DMDMi 74733929.

    Proteomic databases

    MaxQBi Q9H902.
    PaxDbi Q9H902.
    PRIDEi Q9H902.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000165698 ; ENSP00000165698 ; ENSG00000068615 . [Q9H902-1 ]
    ENST00000535845 ; ENSP00000437567 ; ENSG00000068615 . [Q9H902-2 ]
    ENST00000538924 ; ENSP00000438346 ; ENSG00000068615 . [Q9H902-3 ]
    ENST00000541910 ; ENSP00000442681 ; ENSG00000068615 . [Q9H902-4 ]
    GeneIDi 65055.
    KEGGi hsa:65055.
    UCSCi uc002srh.4. human. [Q9H902-1 ]
    uc010yth.2. human. [Q9H902-2 ]
    uc010yti.2. human. [Q9H902-4 ]
    uc021vke.1. human. [Q9H902-3 ]

    Organism-specific databases

    CTDi 65055.
    GeneCardsi GC02M086441.
    HGNCi HGNC:25786. REEP1.
    HPAi HPA058061.
    MIMi 609139. gene.
    610250. phenotype.
    614751. phenotype.
    neXtProti NX_Q9H902.
    Orphaneti 101011. Autosomal dominant spastic paraplegia type 31.
    139536. Distal hereditary motor neuropathy type 5.
    PharmGKBi PA134906680.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5052.
    HOGENOMi HOG000007472.
    HOVERGENi HBG056861.
    InParanoidi Q9H902.
    KOi K17338.
    OMAi GANTNFG.
    PhylomeDBi Q9H902.
    TreeFami TF314177.

    Miscellaneous databases

    GeneWikii REEP1.
    GenomeRNAii 65055.
    NextBioi 67222.
    PROi Q9H902.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H902.
    Bgeei Q9H902.
    CleanExi HS_REEP1.
    Genevestigatori Q9H902.

    Family and domain databases

    InterProi IPR004345. TB2_DP1_HVA22.
    [Graphical view ]
    PANTHERi PTHR12300. PTHR12300. 1 hit.
    Pfami PF03134. TB2_DP1_HVA22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RTP family members induce functional expression of mammalian odorant receptors."
      Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.
      Cell 119:679-691(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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.
      , 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; 2; 3 AND 4).
      Tissue: Brain.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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.
      , 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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
      Tissue: Testis.
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network."
      Park S.H., Zhu P.P., Parker R.L., Blackstone C.
      J. Clin. Invest. 120:1097-1110(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAST; ATL1 AND MICROTUBULES.
    9. Cited for: INVOLVEMENT IN HMN5B, CHARACTERIZATION OF VARIANT SPG31 GLU-20.
    10. "Mutations in the novel mitochondrial protein REEP1 cause hereditary spastic paraplegia type 31."
      Zuechner S., Wang G., Tran-Viet K.-N., Nance M.A., Gaskell P.C., Vance J.M., Ashley-Koch A.E., Pericak-Vance M.A.
      Am. J. Hum. Genet. 79:365-369(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPG31 GLU-20, SUBCELLULAR LOCATION.
    11. Cited for: VARIANT SPG31 GLU-20.
    12. Cited for: VARIANTS SPG31 LEU-19; PHE-23; ARG-42 AND ASN-56.

    Entry informationi

    Entry nameiREEP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H902
    Secondary accession number(s): B7Z4D7
    , B7Z4F2, B7Z5R9, D6W5M2, Q53TI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: March 1, 2001
    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
    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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3