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P02689

- MYP2_HUMAN

UniProt

P02689 - MYP2_HUMAN

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Protein
Myelin P2 protein
Gene
PMP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May play a role in lipid transport protein in Schwann cells. May bind cholesterol.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071Fatty acid

GO - Molecular functioni

  1. cholesterol binding Source: UniProtKB
  2. fatty acid binding Source: UniProtKB
  3. transporter activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. membrane organization Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin P2 protein
Alternative name(s):
Peripheral myelin protein 2
Gene namesi
Name:PMP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:9117. PMP2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33443.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 132131Myelin P2 protein
PRO_0000067388Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Disulfide bondi118 ↔ 1251 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiP02689.
PRIDEiP02689.

PTM databases

PhosphoSiteiP02689.

Expressioni

Gene expression databases

ArrayExpressiP02689.
BgeeiP02689.
CleanExiHS_PMP2.
GenevestigatoriP02689.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

MINTiMINT-5006340.
STRINGi9606.ENSP00000256103.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Beta strandi7 – 1610
Helixi17 – 237
Helixi28 – 369
Beta strandi40 – 467
Beta strandi49 – 557
Beta strandi61 – 655
Beta strandi71 – 744
Beta strandi80 – 889
Beta strandi91 – 988
Beta strandi101 – 11010
Beta strandi113 – 1208
Beta strandi123 – 1319

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WUTX-ray1.85A1-132[»]
3NR3X-ray1.95A3-132[»]
4A1HX-ray2.20A/B/C1-132[»]
4A1YX-ray1.20A/B/C/D1-132[»]
4A8ZX-ray1.80A1-132[»]
4BVMX-ray0.93A1-132[»]
ProteinModelPortaliP02689.
SMRiP02689. Positions 1-132.

Miscellaneous databases

EvolutionaryTraceiP02689.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1293Fatty acid binding

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG322298.
HOGENOMiHOG000004829.
HOVERGENiHBG005633.
InParanoidiP02689.
OMAiRTESAFK.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP02689.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02689-1 [UniParc]FASTAAdd to Basket

« Hide

MSNKFLGTWK LVSSENFDDY MKALGVGLAT RKLGNLAKPT VIISKKGDII    50
TIRTESTFKN TEISFKLGQE FEETTADNRK TKSIVTLQRG SLNQVQRWDG 100
KETTIKRKLV NGKMVAECKM KGVVCTRIYE KV 132
Length:132
Mass (Da):14,909
Last modified:January 23, 2007 - v3
Checksum:i3D515D32695899D2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251G → GG AA sequence 1 Publication
Sequence conflicti99 – 991D → N AA sequence 1 Publication
Sequence conflicti111 – 1111N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16181 Genomic DNA. Translation: BAA03726.1.
X62167 mRNA. Translation: CAA44096.1.
AK311758 mRNA. Translation: BAG34701.1.
CR541649 mRNA. Translation: CAG46450.1.
CR541738 mRNA. Translation: CAG46538.1.
AC018616 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW87090.1.
BC034997 mRNA. Translation: AAH34997.1.
AH004648 Genomic DNA. Translation: AAB32592.2.
CCDSiCCDS6229.1.
PIRiJT0977. MPHU2.
RefSeqiNP_002668.1. NM_002677.3.
UniGeneiHs.571512.

Genome annotation databases

EnsembliENST00000256103; ENSP00000256103; ENSG00000147588.
GeneIDi5375.
KEGGihsa:5375.
UCSCiuc003ycb.1. human.

Polymorphism databases

DMDMi127725.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16181 Genomic DNA. Translation: BAA03726.1 .
X62167 mRNA. Translation: CAA44096.1 .
AK311758 mRNA. Translation: BAG34701.1 .
CR541649 mRNA. Translation: CAG46450.1 .
CR541738 mRNA. Translation: CAG46538.1 .
AC018616 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW87090.1 .
BC034997 mRNA. Translation: AAH34997.1 .
AH004648 Genomic DNA. Translation: AAB32592.2 .
CCDSi CCDS6229.1.
PIRi JT0977. MPHU2.
RefSeqi NP_002668.1. NM_002677.3.
UniGenei Hs.571512.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WUT X-ray 1.85 A 1-132 [» ]
3NR3 X-ray 1.95 A 3-132 [» ]
4A1H X-ray 2.20 A/B/C 1-132 [» ]
4A1Y X-ray 1.20 A/B/C/D 1-132 [» ]
4A8Z X-ray 1.80 A 1-132 [» ]
4BVM X-ray 0.93 A 1-132 [» ]
ProteinModelPortali P02689.
SMRi P02689. Positions 1-132.
ModBasei Search...

Protein-protein interaction databases

MINTi MINT-5006340.
STRINGi 9606.ENSP00000256103.

PTM databases

PhosphoSitei P02689.

Polymorphism databases

DMDMi 127725.

Proteomic databases

PaxDbi P02689.
PRIDEi P02689.

Protocols and materials databases

DNASUi 5375.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000256103 ; ENSP00000256103 ; ENSG00000147588 .
GeneIDi 5375.
KEGGi hsa:5375.
UCSCi uc003ycb.1. human.

Organism-specific databases

CTDi 5375.
GeneCardsi GC08M082352.
HGNCi HGNC:9117. PMP2.
MIMi 170715. gene.
neXtProti NX_P02689.
PharmGKBi PA33443.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG322298.
HOGENOMi HOG000004829.
HOVERGENi HBG005633.
InParanoidi P02689.
OMAi RTESAFK.
OrthoDBi EOG7NW6BZ.
PhylomeDBi P02689.
TreeFami TF316894.

Miscellaneous databases

EvolutionaryTracei P02689.
GeneWikii PMP2.
GenomeRNAii 5375.
NextBioi 20852.
PROi P02689.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02689.
Bgeei P02689.
CleanExi HS_PMP2.
Genevestigatori P02689.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00178. FATTYACIDBP.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00214. FABP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and sequence determination of cDNA encoding P2 protein of human peripheral myelin."
    Hayasaka K., Nanao K., Tahara M., Sato W., Takada G., Miura M., Uyemura K.
    Biochem. Biophys. Res. Commun. 181:204-207(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    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].
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [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].
    Tissue: Testis.
  7. "Partial structure and mapping of the human myelin P2 protein gene."
    Narayanan V., Ripepi B., Jabs E.W., Hawkins A., Griffin C., Tennekoon G.
    J. Neurochem. 63:2010-2013(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
  8. "The complete amino acid sequence of human P2 protein."
    Suzuki M., Kitamura K., Sakamoto Y., Uyemura K.
    J. Neurochem. 39:1759-1762(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-132, ACETYLATION AT SER-2.
  9. "Structural and functional characterization of human peripheral nervous system myelin protein P2."
    Majava V., Polverini E., Mazzini A., Nanekar R., Knoll W., Peters J., Natali F., Baumgartel P., Kursula I., Kursula P.
    PLoS ONE 5:E10300-E10300(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH PALMITATE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, CIRCULAR DICHROISM, DOMAIN.
  10. "Crystal structure of human peripheral myelin protein 2."
    Structural genomics consortium (SGC)
    Submitted (AUG-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 3-132.

Entry informationi

Entry nameiMYP2_HUMAN
AccessioniPrimary (citable) accession number: P02689
Secondary accession number(s): Q6FHL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 126 of the entry and version 3 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

Miscellaneous

P2 protein and myelin basic protein together constitute a major fraction of peripheral nervous system myelin protein.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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