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Q9H902 (REEP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor expression-enhancing protein 1
Gene names
Name:REEP1
Synonyms:C2orf23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.8

Subcellular location

Membrane. Mitochondrion membrane; Multi-pass membrane protein. Endoplasmic reticulum Ref.8 Ref.10.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the DP1 family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H902-1)

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: Q9H902-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: MVSWIISRLVVLIFGTLYPAYYSYKAVKSKDIKEY → MDHLQAGG
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9H902-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MVSWIISRLVV → MQKVLSNGQTEEVRSGSR
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9H902-4)

The sequence of this isoform differs from the canonical sequence as follows:
     62-201: FPFYYELKIA...SESASSSGTA → DRVPYRRDCG...STSSSATETT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Receptor expression-enhancing protein 1
PRO_0000101821

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane35 – 5521Helical; Potential
Compositional bias170 – 1734Poly-Pro

Amino acid modifications

Modified residue1521Phosphoserine Ref.7

Natural variations

Alternative sequence1 – 3535MVSWI…DIKEY → MDHLQAGG in isoform 2.
VSP_042573
Alternative sequence1 – 1111MVSWIISRLVV → MQKVLSNGQTEEVRSGSR in isoform 3.
VSP_043251
Alternative sequence62 – 201140FPFYY…SSGTA → DRVPYRRDCGASACRTSPPS GETAPLLPRAPHHRGLGGPA ANTASLRCPGVLLRALAAQA PPRILRSRFRKKSTSSSATE TT in isoform 4.
VSP_043252
Natural variant191P → L in SPG31. Ref.12
VAR_067265
Natural variant201A → 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. Ref.9 Ref.10 Ref.11
VAR_027351
Natural variant231S → F in SPG31. Ref.12
VAR_067266
Natural variant421W → R in SPG31. Ref.12
VAR_067267
Natural variant561D → N in SPG31. Ref.12
VAR_067268

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 98F120DE100276A9

FASTA20122,255
        10         20         30         40         50         60 
MVSWIISRLV VLIFGTLYPA YYSYKAVKSK DIKEYVKWMM YWIIFALFTT AETFTDIFLC 

        70         80         90        100        110        120 
WFPFYYELKI AFVAWLLSPY TKGSSLLYRK FVHPTLSSKE KEIDDCLVQA KDRSYDALVH 

       130        140        150        160        170        180 
FGKRGLNVAA TAAVMAASKG QGALSERLRS FSMQDLTTIR GDGAPAPSGP PPPGSGRASG 

       190        200 
KHGQPKMSRS ASESASSSGT A 

« Hide

Isoform 2 [UniParc].

Checksum: A640F3EDC043D8C1
Show »

FASTA17418,937
Isoform 3 [UniParc].

Checksum: 74EEC9189C8D5229
Show »

FASTA20822,958
Isoform 4 [UniParc].

Checksum: 13E3F4B75BFF1C96
Show »

FASTA14316,036

References

« Hide 'large scale' references
[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. 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] (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. 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].
[5]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Exome sequencing identifies a REEP1 mutation involved in distal hereditary motor neuropathy type V."
Beetz C., Pieber T.R., Hertel N., Schabhuttl M., Fischer C., Trajanoski S., Graf E., Keiner S., Kurth I., Wieland T., Varga R.E., Timmerman V., Reilly M.M., Strom T.M., Auer-Grumbach M.
Am. J. Hum. Genet. 91:139-145(2012) [PubMed] [Europe PMC] [Abstract]
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]"Mutation screening of spastin, atlastin, and REEP1 in hereditary spastic paraplegia."
McCorquodale D.S. III, Ozomaro U., Huang J., Montenegro G., Kushman A., Citrigno L., Price J., Speziani F., Pericak-Vance M.A., Zuchner S.
Clin. Genet. 79:523-530(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG31 GLU-20.
[12]"REEP1 mutations in SPG31: frequency, mutational spectrum, and potential association with mitochondrial morpho-functional dysfunction."
Goizet C., Depienne C., Benard G., Boukhris A., Mundwiller E., Sole G., Coupry I., Pilliod J., Martin-Negrier M.L., Fedirko E., Forlani S., Cazeneuve C., Hannequin D., Charles P., Feki I., Pinel J.F., Ouvrard-Hernandez A.M., Lyonnet S. expand/collapse author list , Ollagnon-Roman E., Yaouanq J., Toutain A., Dussert C., Fontaine B., Leguern E., Lacombe D., Durr A., Rossignol R., Brice A., Stevanin G.
Hum. Mutat. 32:1118-1127(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SPG31 LEU-19; PHE-23; ARG-42 AND ASN-56.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001158202.1. NM_001164730.1.
NP_001158203.1. NM_001164731.1.
NP_001158204.1. NM_001164732.1.
NP_075063.1. NM_022912.2.
UniGeneHs.368884.

3D structure databases

ProteinModelPortalQ9H902.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122377. 2 interactions.
IntActQ9H902. 1 interaction.
STRING9606.ENSP00000165698.

PTM databases

PhosphoSiteQ9H902.

Polymorphism databases

DMDM74733929.

Proteomic databases

PaxDbQ9H902.
PRIDEQ9H902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000165698; ENSP00000165698; ENSG00000068615. [Q9H902-1]
ENST00000535845; ENSP00000437567; ENSG00000068615. [Q9H902-2]
ENST00000538924; ENSP00000438346; ENSG00000068615. [Q9H902-3]
ENST00000541910; ENSP00000442681; ENSG00000068615. [Q9H902-4]
GeneID65055.
KEGGhsa:65055.
UCSCuc002srh.4. human. [Q9H902-1]
uc010yth.2. human. [Q9H902-2]
uc010yti.2. human. [Q9H902-4]
uc021vke.1. human. [Q9H902-3]

Organism-specific databases

CTD65055.
GeneCardsGC02M086441.
HGNCHGNC:25786. REEP1.
HPAHPA058061.
MIM609139. gene.
610250. phenotype.
614751. phenotype.
neXtProtNX_Q9H902.
Orphanet101011. Autosomal dominant spastic paraplegia type 31.
139536. Distal hereditary motor neuropathy type 5.
PharmGKBPA134906680.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5052.
HOGENOMHOG000007472.
HOVERGENHBG056861.
InParanoidQ9H902.
KOK17338.
OMARTSGKHG.
PhylomeDBQ9H902.
TreeFamTF314177.

Gene expression databases

ArrayExpressQ9H902.
BgeeQ9H902.
CleanExHS_REEP1.
GenevestigatorQ9H902.

Family and domain databases

InterProIPR004345. TB2_DP1_HVA22.
[Graphical view]
PANTHERPTHR12300. PTHR12300. 1 hit.
PfamPF03134. TB2_DP1_HVA22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiREEP1.
GenomeRNAi65055.
NextBio67222.
PROQ9H902.
SOURCESearch...

Entry information

Entry nameREEP1_HUMAN
AccessionPrimary (citable) accession number: Q9H902
Secondary accession number(s): B7Z4D7 expand/collapse secondary AC list , B7Z4F2, B7Z5R9, D6W5M2, Q53TI0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 105 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 2

Human chromosome 2: entries, gene names and cross-references to MIM