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P60201 (MYPR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myelin proteolipid protein

Short name=PLP
Alternative name(s):
Lipophilin
Gene names
Name:PLP1
Synonyms:PLP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.48.

Involvement in disease

Leukodystrophy, hypomyelinating, 1 (HLD1) [MIM:312080]: A X-linked recessive disorder of the central nervous system in which myelin is not formed properly. Clinically characterized by nystagmus, spastic quadriplegia, ataxia, and developmental delay.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.42 Ref.43 Ref.44 Ref.46

Spastic paraplegia 2, X-linked (SPG2) [MIM:312920]: 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. SPG2 is characterized by spastic gait and hyperreflexia. In some patients, complicating features include nystagmus, dysarthria, sensory disturbance, mental retardation, optic atrophy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.28 Ref.29 Ref.34 Ref.41 Ref.43 Ref.45 Ref.47 Ref.48

Sequence similarities

Belongs to the myelin proteolipid protein family.

Sequence caution

The sequence AAA60350.1 differs from that shown. Reason: The submitted sequence only contains the last exon but the authors annotated a CDS including all exons of that gene.

The sequence AAD13880.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Hereditary spastic paraplegia
Leukodystrophy
Neurodegeneration
   DomainTransmembrane
Transmembrane helix
   PTMDisulfide bond
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon ensheathment

Traceable author statement Ref.3. Source: ProtInc

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cell maturation

Inferred from electronic annotation. Source: Ensembl

central nervous system myelination

Inferred from electronic annotation. Source: Ensembl

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

synaptic transmission

Traceable author statement Ref.3. Source: ProtInc

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

myelin sheath

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.48. Source: UniProtKB

   Molecular_functionstructural constituent of myelin sheath

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Traceable author statement Ref.3. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P60201-1)

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 DM-20 (identifier: P60201-2)

The sequence of this isoform differs from the canonical sequence as follows:
     117-151: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 277276Myelin proteolipid protein
PRO_0000159005

Regions

Topological domain2 – 98Cytoplasmic Probable
Transmembrane10 – 3627Helical; Name=1; Probable
Topological domain37 – 6327Extracellular Probable
Transmembrane64 – 8825Helical; Name=2; Probable
Topological domain89 – 15163Cytoplasmic Probable
Transmembrane152 – 17726Helical; Name=3; Probable
Topological domain178 – 23356Extracellular Probable
Transmembrane234 – 26027Helical; Name=4; Probable
Topological domain261 – 27717Cytoplasmic Probable

Amino acid modifications

Lipidation61S-palmitoyl cysteine By similarity
Lipidation71S-palmitoyl cysteine By similarity
Lipidation101S-palmitoyl cysteine By similarity
Lipidation1091S-palmitoyl cysteine By similarity
Lipidation1391S-palmitoyl cysteine By similarity
Lipidation1411S-palmitoyl cysteine By similarity
Lipidation1991O-palmitoyl serine By similarity
Disulfide bond184 ↔ 228 By similarity
Disulfide bond201 ↔ 220 By similarity

Natural variations

Alternative sequence117 – 15135Missing in isoform DM-20.
VSP_003325
Natural variant151P → L in HLD1. Ref.12
VAR_004546
Natural variant301A → P in SPG2; partially retained in the endoplasmic reticulum; does not induce unfolded protein response. Ref.48
VAR_070667
Natural variant311L → P in HLD1. Ref.43
VAR_015014
Natural variant321F → L in HLD1. Ref.43
VAR_015015
Natural variant321F → V in HLD1. Ref.37
VAR_015016
Natural variant331C → Y in HLD1. Ref.46
VAR_046906
Natural variant351C → R in HLD1. Ref.46
VAR_046907
Natural variant351C → Y in HLD1. Ref.38
VAR_015017
Natural variant391A → T in HLD1. Ref.38 Ref.46
VAR_015018
Natural variant431T → I in HLD1. Ref.25
VAR_004547
Natural variant461L → P in HLD1/SPG2. Ref.39 Ref.46
VAR_015019
Natural variant461L → R in HLD1. Ref.40
VAR_015020
Natural variant501Y → C in HLD1. Ref.46
VAR_046908
Natural variant511F → S in HLD1. Ref.43
VAR_015021
Natural variant601Y → C in HLD1. Ref.38
VAR_015022
Natural variant741G → R in HLD1. Ref.16 Ref.38 Ref.43
VAR_004548
Natural variant761A → P in HLD1. Ref.46
VAR_046909
Natural variant1161T → K in HLD1. Ref.30
VAR_015023
Natural variant117 – 16549Missing in HLD1.
VAR_004550
Natural variant1301H → Y in SPG2. Ref.43
VAR_015024
Natural variant1371R → W in SPG2. Ref.47
VAR_046910
Natural variant1401H → Y in SPG2. Ref.22
VAR_004551
Natural variant1481H → Y in HLD1/SPG2. Ref.41 Ref.46
VAR_015025
Natural variant1511K → N in HLD1. Ref.27
VAR_015026
Natural variant1561T → I in HLD1. Ref.13 Ref.14
VAR_004552
Natural variant1621V → E in HLD1. Ref.46
VAR_046911
Natural variant1631W → R in HLD1. Ref.3
VAR_004553
Natural variant1661V → E in HLD1. Ref.18
VAR_004554
Natural variant1661V → G in HLD1/SPG2. Ref.39
VAR_015027
Natural variant1691C → R in HLD1. Ref.38
VAR_015028
Natural variant1701S → F in SPG2. Ref.34
VAR_015029
Natural variant1701S → P in HLD1. Ref.46
VAR_046912
Natural variant1721V → A in HLD1. Ref.37
VAR_015030
Natural variant1731P → S in HLD1. Ref.46
VAR_046913
Natural variant1751Y → C in HLD1. Ref.38
VAR_015031
Natural variant1811W → C in HLD1. Ref.38 Ref.43
VAR_015032
Natural variant1821T → P in HLD1. Ref.17
VAR_004555
Natural variant1831T → N in HLD1. Ref.38
VAR_015033
Natural variant1871I → T in SPG2. Ref.23
VAR_004556
Natural variant2031D → E in HLD1. Ref.38 Ref.43
VAR_015034
Natural variant2031D → G in HLD1. Ref.38
VAR_015035
Natural variant2031D → H in HLD1. Ref.16
VAR_004557
Natural variant2031D → N in HLD1. Ref.38
VAR_015036
Natural variant2031D → V in HLD1. Ref.36
VAR_007956
Natural variant2051R → G in HLD1. Ref.37
VAR_015037
Natural variant2071Y → C in HLD1. Ref.37
VAR_015038
Natural variant2091V → D in HLD1. Ref.32 Ref.40
VAR_015039
Natural variant2101L → H in HLD1. Ref.38
VAR_015040
Natural variant2111P → L in HLD1. Ref.32 Ref.40
VAR_015041
Natural variant2121W → R in HLD1. Ref.38 Ref.43
VAR_015042
Natural variant2161P → A in HLD1. Ref.43
VAR_015043
Natural variant2161P → L in SPG2. Ref.45
VAR_046914
Natural variant2161P → S in HLD1. Ref.21 Ref.38
VAR_004558
Natural variant2171G → S in HLD1. Ref.11 Ref.19
VAR_004559
Natural variant2191V → F in HLD1. Ref.15
VAR_004560
Natural variant2201C → Y in HLD1. Ref.40
VAR_015044
Natural variant2211G → C in HLD1. Ref.20
VAR_004561
Natural variant2241L → I in HLD1/SPG2. Ref.39
VAR_015045
Natural variant2241L → P in HLD1. Ref.17
VAR_004562
Natural variant2251L → P in HLD1. Ref.46
VAR_046915
Natural variant2261S → P in SPG2. Ref.29
VAR_015046
Natural variant2281C → Y in HLD1. Ref.38
VAR_015047
Natural variant2341Q → P in HLD1. Ref.38
VAR_015048
Natural variant2371F → S in SPG2. Ref.28
VAR_004563
Natural variant2391L → P in HLD1. Ref.46
VAR_046916
Natural variant2421A → P in HLD1. Ref.31 Ref.40
VAR_015049
Natural variant2431A → E in HLD1. Ref.44
VAR_046917
Natural variant2431A → V in HLD1. Ref.33
VAR_046918
Natural variant2461G → A in HLD1. Ref.46
VAR_046919
Natural variant2461G → E in HLD1. Ref.38
VAR_015050
Natural variant2471A → T in HLD1. Ref.42
VAR_046920
Natural variant2481A → E in HLD1. Ref.38
VAR_015051
Natural variant2491A → P in HLD1. Ref.26
VAR_004565
Natural variant2531S → F in HLD1. Ref.35
VAR_015052

Experimental info

Sequence conflict1401H → T in AAA60117. Ref.7
Sequence conflict1851Q → D in AAA59565. Ref.3
Sequence conflict2131N → I in AAA59565. Ref.3

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: 3C2BC973C3061C38

FASTA27730,077
        10         20         30         40         50         60 
MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY 

        70         80         90        100        110        120 
LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG 

       130        140        150        160        170        180 
QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT 

       190        200        210        220        230        240 
WTTCQSIAFP SKTSASIGSL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF 

       250        260        270 
IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF 

« Hide

Isoform DM-20 [UniParc].

Checksum: 90DEFE60148DC659
Show »

FASTA24226,274

References

« Hide 'large scale' references
[1]"Individual exons encode the integral membrane domains of human myelin proteolipid protein."
Diehl H.-J., Schaich M., Budzinski R.-M., Stoffel W.
Proc. Natl. Acad. Sci. U.S.A. 83:9807-9811(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human myelin DM-20 proteolipid protein deletion defined by cDNA sequence."
Simons R., Alon N., Riordan J.R.
Biochem. Biophys. Res. Commun. 146:666-671(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DM-20).
[3]"Mutation of the proteolipid protein gene PLP in a human X chromosome-linked myelin disorder."
Hudson L.D., Puckett C., Berndt J., Chan J., Gencic S.
Proc. Natl. Acad. Sci. U.S.A. 86:8128-8131(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HLD1 ARG-163.
[4]"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 DM-20).
[5]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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].
[7]"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] (ISOFORMS 1 AND DM-20).
Tissue: Spinal cord and Uterus.
[8]"Amino-acid sequence of human and bovine brain myelin proteolipid protein (lipophilin) is completely conserved."
Stoffel W., Giersiefen H., Hillen H., Schroeder W., Tunggal B.
Biol. Chem. Hoppe-Seyler 366:627-635(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-277.
[9]"Expression of myelin proteins in the developing human spinal cord: cloning and sequencing of human proteolipid protein cDNA."
Kronquist K.E., Crandall B.F., Macklin W.B., Campagnoni A.T.
J. Neurosci. Res. 18:395-401(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spinal cord.
[10]"Major myelin proteolipid: the 4-alpha-helix topology."
Popot J.-L., Pham-Dinh D., Dautigny A.
J. Membr. Biol. 120:233-246(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[11]"Pelizaeus-Merzbacher disease: an X-linked neurologic disorder of myelin metabolism with a novel mutation in the gene encoding proteolipid protein."
Gencic S., Abuelo D., Ambler M., Hudson L.D.
Am. J. Hum. Genet. 45:435-442(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 SER-217.
[12]"Pelizaeus-Merzbacher disease: tight linkage to proteolipid protein gene exon variant."
Trofatter J., Dlouhy S.R., Demyer W., Conneally P.M., Hodes M.E.
Proc. Natl. Acad. Sci. U.S.A. 86:9427-9430(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 LEU-15.
[13]"A point mutation at the X-chromosomal proteolipid protein locus in Pelizaeus-Merzbacher disease leads to disruption of myelinogenesis."
Weimbs T., Dick T., Stoffel W., Boltshauser E.
Biol. Chem. Hoppe-Seyler 371:1175-1183(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 ILE-156.
[14]"A new mutation in the proteolipid protein (PLP) gene in a German family with Pelizaeus-Merzbacher disease."
Pratt V.M., Trofatter J.A., Schinzel A., Dlouhy S.R., Conneally P.M., Hodes M.E.
Am. J. Med. Genet. 38:136-139(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 ILE-156.
[15]"Pelizaeus-Merzbacher disease: a valine to phenylalanine point mutation in a putative extracellular loop of myelin proteolipid."
Pham-Dinh D., Popot J.-L., Bosepflug-Tanguy O., Landrieu P., Deleuze P., Boue J., Jolles P., Dautigny A.
Proc. Natl. Acad. Sci. U.S.A. 88:7562-7566(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 PHE-219.
[16]"Molecular diagnostics for myelin proteolipid protein gene mutations in Pelizaeus-Merzbacher disease."
Doll R., Natowicz M.R., Schiffmann R., Smith F.I.
Am. J. Hum. Genet. 51:161-169(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 ARG-74 AND HIS-203.
[17]"Pelizaeus-Merzbacher disease: detection of mutations Thr181-->Pro and Leu223-->Pro in the proteolipid protein gene, and prenatal diagnosis."
Strautnieks S., Rutland P., Winter R.M., Baraitser M., Malcolm S.
Am. J. Hum. Genet. 51:871-878(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 PRO-182 AND PRO-224.
[18]"Linkage of a new mutation in the proteolipid protein (PLP) gene to Pelizaeus-Merzbacher disease (PMD) in a large Finnish kindred."
Pratt V.M., Kiefer J.R., Lahdetie J., Schleutker J., Hodes M.E., Dlouhy S.R.
Am. J. Hum. Genet. 52:1053-1056(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 GLU-166.
[19]"A novel mutation in the proteolipid protein gene leading to Pelizaeus-Merzbacher disease."
Otterbach B., Stoffel W., Ramaekers V.
Biol. Chem. Hoppe-Seyler 374:75-83(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 SER-217.
[20]"A missense mutation in the proteolipid protein gene responsible for Pelizaeus-Merzbacher disease in a Japanese family."
Iwaki A., Muramoto T., Iwaki I., Furumi H., Dario-Deleon M.L., Tateishi J., Fukumaki Y.
Hum. Mol. Genet. 2:19-22(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 CYS-221.
[21]"Comparison of statistics for candidate-gene association studies using cases and parents."
Pratt V.M., Boyadjiev S., Dlouhy S.R., Silver K., der Kaloustian V.M., Hodes M.E.
Am. J. Hum. Genet. 55:402-409(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 SER-216.
[22]"X-linked spastic paraplegia and Pelizaeus-Merzbacher disease are allelic disorders at the proteolipid protein locus."
Saugier-Veber P., Munnich A., Bonneau D., Rozet J.-M., le Merrer M., Gil R., Boespflug-Tanguy O.
Nat. Genet. 6:257-262(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 TYR-140.
[23]"The rumpshaker mutation in spastic paraplegia."
Kobayashi H., Hoffman E.P., Marks H.G.
Nat. Genet. 7:351-352(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 THR-187.
[24]"In-frame deletion in the proteolipid protein gene of a family with Pelizaeus-Merzbacher disease."
Kleindorfer D.O., Dlouhy S.R., Pratt V.M., Jones M.C., Trofatter J.A., Hodes M.E.
Am. J. Med. Genet. 55:405-407(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 116-VAL--LEU-165 DEL.
[25]"Pelizaeus-Merzbacher disease caused by a de novo mutation that originated in exon 2 of the maternal great-grandfather of the propositus."
Pratt V.M., Boyadjiev S., Green K., Hodes M.E., Dlouhy S.R.
Am. J. Med. Genet. 58:70-73(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 ILE-43.
[26]"Pelizaeus-Merzbacher disease: a point mutation in exon 6 of the proteolipid protein (PLP) gene."
Pratt V.M., Dlouhy S.R., Hodes M.E.
Clin. Genet. 47:99-100(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 PRO-249.
[27]"A novel mutation in exon 3 of the proteolipid protein gene in Pelizaeus-Merzbacher disease."
Pratt V.M., Naidu S., Dlouhy S.R., Marks H.G., Hodes M.E.
Neurology 45:394-395(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 ASN-151.
[28]"A novel mutation in exon 6 (F236S) of the proteolipid protein gene is associated with spastic paraplegia."
Donnelly A., Colley A., Crimmins D., Mulley J.
Hum. Mutat. 8:384-385(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 SER-237.
[29]"Refined genetic mapping and proteolipid protein mutation analysis in X-linked pure hereditary spastic paraplegia."
Cambi F., Tang X.M., Cordray P., Fain P.R., Keppen L.D., Barker D.F.
Neurology 46:1112-1117(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 PRO-226.
[30]"Adult-onset neurodegenerative disorder due to proteolipid protein gene mutation in the mother of a man with Pelizaeus-Merzbacher disease."
Nance M.A., Boyadjiev S., Pratt V.M., Taylor S., Hodes M.E., Dlouhy S.R.
Neurology 47:1333-1335(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 LYS-116.
[31]"A new missense mutation in exon 6 of the proteolipid protein gene in a patient with Pelizaeus-Merzbacher disease."
Kawanishi C., Osaka H., Owa K., Inoue K., Miyakawa T., Onishi H., Yamada Y., Suzuki K., Kimura S., Kosaka K.
Hum. Mutat. 9:475-476(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 PRO-242.
[32]"Mutations in the proteolipid protein gene in Japanese families with Pelizaeus-Merzbacher disease."
Inoue K., Osaka H., Kawanishi C., Sugiyama N., Ishii M., Sugita K., Yamada Y., Kosaka K.
Neurology 48:283-285(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 ASP-209 AND LEU-211.
[33]"Jimpy(msd) mouse mutation and connatal Pelizaeus-Merzbacher disease."
Yamamoto T., Nanba E., Zhang H., Sasaki M., Komaki H., Takeshita K.
Am. J. Med. Genet. 75:439-440(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 VAL-243.
[34]"X-linked spastic paraplegia due to a mutation (C506T; Ser169Phe) in exon 4 of the proteolipid protein gene (PLP)."
Hodes M.E., Hadjisavvas A., Butler I.J., Aydanian A., Dlouhy S.R.
Am. J. Med. Genet. 75:516-517(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 PHE-170.
[35]"A de novo mutation (C755T; Ser252Phe) in exon 6 of the proteolipid protein gene responsible for Pelizaeus-Merzbacher disease."
Hodes M.E., Aydanian A., Dlouhy S.R., Whelan D.T., Heshka T., Ronen G.
Clin. Genet. 54:248-249(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 PHE-253.
[36]"Connatal Pelizaeus-Merzbacher disease: a missense mutation in exon 4 of the proteolipid protein 'PLP' gene."
Nagao M., Kadowaki J.
J. Hum. Genet. 43:206-208(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 VAL-203.
[37]"Duplication of the proteolipid protein gene is the major cause of Pelizaeus-Merzbacher disease."
Sistermans E.A., de Coo R.F.M., De Wijs I.J., Van Oost B.A.
Neurology 50:1749-1754(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 VAL-32; ALA-172; GLY-205 AND CYS-207.
[38]"Proteolipoprotein gene analysis in 82 patients with sporadic Pelizaeus-Merzbacher Disease: duplications, the major cause of the disease, originate more frequently in male germ cells, but point mutations do not."
Mimault C., Giraud G., Courtois V., Cailloux F., Boire J.Y., Dastugue B., Boespflug-Tanguy O., Baethmann M., Bertini E., Cuisset J.M., Gaertner J., Hanefeld F., Kohlschutter A., Landrieu P., Mayer M., Peudenier S., Rodriguez D., Rating D. expand/collapse author list , Surtees R., Uziel G., Vallee L., Voit T.
Am. J. Hum. Genet. 65:360-369(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 TYR-35; THR-39; CYS-60; ARG-74; ARG-169; CYS-175; CYS-181; ASN-183; ASN-203; GLU-203; GLY-203; HIS-210; ARG-212; SER-216; TYR-228; PRO-234; GLU-246 AND GLU-248.
[39]"Different mutations in the same codon of the proteolipid protein gene, PLP, may help in correlating genotype with phenotype in Pelizaeus-Merzbacher disease/X-linked spastic paraplegia (PMD/SPG2)."
Hodes M.E., Zimmerman A.W., Aydanian A., Naidu S., Miller N.R., Garcia Oller J.L., Barker B., Aleck K.A., Hurley T.D., Dlouhy S.R.
Am. J. Med. Genet. 82:132-139(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1/SPG2 PRO-46; GLY-166 AND ILE-224.
[40]"Pelizaeus-Merzbacher disease: three novel mutations and implication for locus heterogeneity."
Osaka H., Kawanishi C., Inoue K., Onishi H., Kobayashi T., Sugiyama N., Kosaka K., Nezu A., Fujii K., Sugita K., Kodama K., Murayama K., Murayama S., Kanazawa I., Kimura S.
Ann. Neurol. 45:59-64(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 ARG-46; ASP-209; LEU-211; TYR-220 AND PRO-242.
[41]"Novel exon 3B proteolipid protein gene mutation causing late-onset spastic paraplegia type 2 with variable penetrance in female family members."
Sivakumar K., Sambuughin N., Selenge B., Nagle J.W., Baasanjav D., Hudson L.D., Goldfarb L.G.
Ann. Neurol. 45:680-683(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 TYR-148.
[42]"A novel mutation (A246T) in exon 6 of the proteolipid protein gene associated with connatal Pelizaeus-Merzbacher disease."
Yamamoto T., Nanba E.
Hum. Mutat. 14:182-182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 THR-247.
[43]"Genotype-phenotype correlation in inherited brain myelination defects due to proteolipid protein gene mutations."
Cailloux F., Gauthier-Barichard F., Mimault C., Isabelle V., Courtois V., Giraud G., Dastugue B., Boespflug-Tanguy O., Baethmann M., Bertini E., Cuisset J.M., Gaertner J., Hanefeld F., Kohlschutter A., Landrieu P., Mayer M., Peudenier S., Rodriguez D. expand/collapse author list , Rating D., Surtees R., Uziel G., Vallee L., Voit T.
Eur. J. Hum. Genet. 8:837-845(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 PRO-31; LEU-32; SER-51; ARG-74; CYS-181; GLU-203; ARG-212 AND ALA-216, VARIANT SPG2 TYR-130.
[44]"A severe connatal form of Pelizaeus Merzbacher disease in a Czech boy caused by a novel mutation (725C>A, Ala242Glu) at the 'jimpy(msd) codon' in the PLP gene."
Seeman P., Paderova K., Benes V. Jr., Sistermans E.A.
Int. J. Mol. Med. 9:125-129(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HLD1 GLU-243.
[45]"A case of complicated spastic paraplegia 2 due to a point mutation in the proteolipid protein 1 gene."
Lee E.S., Moon H.K., Park Y.H., Garbern J., Hobson G.M.
J. Neurol. Sci. 224:83-87(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 LEU-216.
[46]"Seventeen novel PLP1 mutations in patients with Pelizaeus-Merzbacher disease."
Huebner C.A., Orth U., Senning A., Steglich C., Kohlschuetter A., Korinthenberg R., Gal A.
Hum. Mutat. 25:321-322(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HLD1 TYR-33; ARG-35; THR-39; PRO-46; CYS-50; PRO-76; TYR-148; GLU-162; PRO-170; SER-173; PRO-225; PRO-239 AND ALA-246.
[47]"Steroid-responsive neurologic relapses in a child with a proteolipid protein-1 mutation."
Gorman M.P., Golomb M.R., Walsh L.E., Hobson G.M., Garbern J.Y., Kinkel R.P., Darras B.T., Urion D.K., Eksioglu Y.Z.
Neurology 68:1305-1307(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 TRP-137.
[48]"A novel mutation in PLP1 causes severe hereditary spastic paraplegia type 2."
Noetzli L., Sanz P.G., Brodsky G.L., Hinckley J.D., Giugni J.C., Giannaula R.J., Gonzalez-Alegre P., Di Paola J.
Gene 533:447-450(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG2 PRO-30, CHARACTERIZATION OF VARIANT SPG2 PRO-30, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15032 expand/collapse EMBL AC list , M15026, M15027, M15028, M15029, M15031 Genomic DNA. Translation: AAA60350.1. Sequence problems.
AJ006976 Genomic DNA. Translation: CAA07364.1.
M54927 mRNA. Translation: AAA59565.1.
M17085 mRNA. Translation: AAA60118.1.
M27110 mRNA. Translation: AAA60117.1.
CR536542 mRNA. Translation: CAG38779.1.
Z73964 Genomic DNA. Translation: CAA98191.1.
Z73964 Genomic DNA. Translation: CAI42028.1.
CH471190 Genomic DNA. Translation: EAW54690.1.
BC002665 mRNA. Translation: AAH02665.1.
BC095452 mRNA. Translation: AAH95452.1.
D13320 Genomic DNA. Translation: BAA02577.1.
S55837 Genomic DNA. Translation: AAD13880.1. Sequence problems.
PIRMPHUPL. A26665.
RefSeqNP_000524.3. NM_000533.3.
NP_001122306.1. NM_001128834.1.
NP_955772.1. NM_199478.1.
UniGeneHs.1787.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XPGX-ray2.60C45-53[»]
ProteinModelPortalP60201.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111368. 5 interactions.
IntActP60201. 2 interactions.
STRING9606.ENSP00000305152.

PTM databases

PhosphoSiteP60201.

Polymorphism databases

DMDM41393531.

2D gel databases

UCD-2DPAGEP60201.

Proteomic databases

PaxDbP60201.
PRIDEP60201.

Protocols and materials databases

DNASU5354.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000303958; ENSP00000305152; ENSG00000123560. [P60201-1]
ENST00000361621; ENSP00000354860; ENSG00000123560. [P60201-2]
ENST00000418604; ENSP00000405750; ENSG00000123560. [P60201-1]
GeneID5354.
KEGGhsa:5354.
UCSCuc004elj.3. human. [P60201-2]
uc004elk.3. human. [P60201-1]

Organism-specific databases

CTD5354.
GeneCardsGC0XP103028.
HGNCHGNC:9086. PLP1.
HPAHPA004128.
MIM300401. gene.
312080. phenotype.
312920. phenotype.
neXtProtNX_P60201.
Orphanet280234. Null syndrome.
280229. Pelizaeus-Merzbacher disease in female carriers.
280219. Pelizaeus-Merzbacher disease, classic form.
280210. Pelizaeus-Merzbacher disease, connatal form.
280224. Pelizaeus-Merzbacher disease, transitional form.
99015. Spastic paraplegia type 2.
PharmGKBPA33414.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311658.
HOGENOMHOG000231338.
HOVERGENHBG000096.
InParanoidP60201.
KOK17271.
OMAIGTLCAD.
PhylomeDBP60201.
TreeFamTF315162.

Gene expression databases

ArrayExpressP60201.
BgeeP60201.
CleanExHS_PLP1.
GenevestigatorP60201.

Family and domain databases

InterProIPR001614. Myelin_PLP.
IPR018237. Myelin_PLP_CS.
[Graphical view]
PANTHERPTHR11683. PTHR11683. 1 hit.
PfamPF01275. Myelin_PLP. 1 hit.
[Graphical view]
PRINTSPR00214. MYELINPLP.
SMARTSM00002. PLP. 1 hit.
[Graphical view]
PROSITEPS00575. MYELIN_PLP_1. 1 hit.
PS01004. MYELIN_PLP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLP1. human.
GeneWikiProteolipid_protein_1.
GenomeRNAi5354.
NextBio20752.
PROP60201.
SOURCESearch...

Entry information

Entry nameMYPR_HUMAN
AccessionPrimary (citable) accession number: P60201
Secondary accession number(s): P04400 expand/collapse secondary AC list , P06905, Q502Y1, Q6FHZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 X

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