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P04370

- MBP_MOUSE

UniProt

P04370 - MBP_MOUSE

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Protein

Myelin basic protein

Gene
Mbp, Shi
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The classic group of MBP isoforms (isoform 4-isoform 13) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined to optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function.1 Publication

GO - Molecular functioni

  1. protease binding Source: BHF-UCL
  2. structural constituent of myelin sheath Source: Ensembl

GO - Biological processi

  1. membrane organization Source: MGI
  2. myelination Source: MGI
  3. negative regulation of axonogenesis Source: Ensembl
  4. response to toxic substance Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Myelin basic protein
Short name:
MBP
Alternative name(s):
Myelin A1 protein
Gene namesi
Name:Mbp
Synonyms:Shi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:96925. Mbp.

Subcellular locationi

GO - Cellular componenti

  1. cell periphery Source: MGI
  2. cell projection Source: MGI
  3. compact myelin Source: Ensembl
  4. cytoplasm Source: UniProtKB-SubCell
  5. internode region of axon Source: MGI
  6. myelin sheath Source: MGI
  7. neuronal cell body Source: MGI
  8. nucleus Source: UniProtKB-SubCell
  9. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in Mbp are a cause of dysmyelinating diseases such as the shiverer (SHI) and myelin deficient (MLD) diseases characterized by decreased myelination in the CNS, tremors, and convulsions of progressively increasing severity leading to early death. The shiverer mice only express isoform 2, the MLD mice have a reduced amount of Mbp.

Keywords - Diseasei

Autoimmune encephalomyelitis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Myelin basic proteinPRO_0000158991Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei141 – 1411Phosphoserine By similarity
Modified residuei157 – 1571Citrulline By similarity
Modified residuei163 – 1631Citrulline By similarity
Modified residuei167 – 1671Phosphothreonine1 Publication
Modified residuei172 – 1721Phosphoserine1 Publication
Modified residuei188 – 1881Phosphoserine By similarity
Modified residuei199 – 1991Phosphotyrosine1 Publication
Modified residuei226 – 2261Phosphothreonine By similarity
Modified residuei229 – 2291Phosphothreonine1 Publication
Modified residuei234 – 2341Deamidated glutamine By similarity
Modified residuei239 – 2391Citrulline By similarity
Modified residuei241 – 2411Phosphoserine By similarity
Modified residuei245 – 2451Phosphoserine; by UHMK1
Modified residuei250 – 2501Citrulline By similarity

Post-translational modificationi

As in other animals, several charge isomers may be produced as a result of optional post-translatonial modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.
Methylated on arginine residues; decreases with the age of the animal, making MBP more cationic.
Phosphorylated by TAOK2, VRK2, MAPK11, MAPK12, MAPK14 and MINK1 By similarity.

Keywords - PTMi

Acetylation, Citrullination, Methylation, Phosphoprotein

Proteomic databases

MaxQBiP04370.
PaxDbiP04370.
PRIDEiP04370.

PTM databases

PhosphoSiteiP04370.

Miscellaneous databases

PMAP-CutDBP04370.

Expressioni

Tissue specificityi

In the embryo, isoform 1-isoform 3 are found in neurons within the central nervous system (primarily in pioneer neurons important in the formation of the cortex) and the peripheral nervous system. They are also expressed in the thymus, gut, lung and kidney. In the adult, isoform 1-isoform 3 are highly expressed in the brain (mainly in brain regions rich in oligodendrocytes) and spleen. Lower levels are seen in the heart, kidney and lung. Isoform 2 is also found in cells of the immune system. The isoforms missing the 134 first amino acids (isoform 4-isoform 13) are almost exclusively produced in the myelin-forming cells, the mature oligodendrocytes.

Developmental stagei

The differential expression of MBP isoforms is developmentally regulated. Isoform 2 and isoform 3 are first expressed during embryonic stages (as early as at embryonic day 11.5), expression of isoform 1 is turned on shortly after birth. Expression of the isoforms missing the 134 first amino acids occurs later, presumably as the oligodendrocytes approach their terminally differentiated state.1 Publication

Gene expression databases

ArrayExpressiP04370.
BgeeiP04370.
CleanExiMM_MBP.
GenevestigatoriP04370.

Interactioni

Subunit structurei

Homodimer By similarity.

Protein-protein interaction databases

BioGridi201336. 42 interactions.
IntActiP04370. 30 interactions.
MINTiMINT-4101448.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi209 – 2113
Helixi216 – 22510
Turni242 – 2443

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LUGNMR-A206-245[»]
DisProtiDP00237.
ProteinModelPortaliP04370.
SMRiP04370. Positions 206-237.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG75180.
GeneTreeiENSGT00390000014772.
HOVERGENiHBG008347.
InParanoidiP04370.
KOiK17269.
OMAiCAERRGH.
OrthoDBiEOG7M0NRZ.
PhylomeDBiP04370.
TreeFamiTF333391.

Family and domain databases

InterProiIPR000548. Myelin_BP.
[Graphical view]
PANTHERiPTHR11429. PTHR11429. 1 hit.
PfamiPF01669. Myelin_MBP. 1 hit.
[Graphical view]
PRINTSiPR00212. MYELINMBP.
PROSITEiPS00569. MYELIN_MBP. 1 hit.
[Graphical view]

Sequences (13)i

Sequence statusi: Complete.

This entry describes 13 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P04370-1) [UniParc]FASTAAdd to Basket

Also known as: Golli-MBP1, J37

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

MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGEAD    50
AIQNNGTSAE DTAVTDSKHT ADPKNNWQGA HPADPGNRPH LIRLFSRDAP 100
GREDNTFKDR PSESDELQTI QEDPTAASGG LDVMASQKRP SQRSKYLATA 150
STMDHARHGF LPRHRDTGIL DSIGRFFSGD RGAPKRGSGK DSHTRTTHYG 200
SLPQKSQHGR TQDENPVVHF FKNIVTPRTP PPSQGKGGRD SRSGSPMARR 250
Length:250
Mass (Da):27,168
Last modified:October 18, 2001 - v2
Checksum:iB418ED11C27B0C43
GO
Isoform 2 (identifier: P04370-2) [UniParc]FASTAAdd to Basket

Also known as: Golli-MBP2, BG21, HMBPR

The sequence of this isoform differs from the canonical sequence as follows:
     191-250: DSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR → VSSEP

Show »
Length:195
Mass (Da):21,004
Checksum:i1C5C6AEFB561D2DA
GO
Isoform 3 (identifier: P04370-3) [UniParc]FASTAAdd to Basket

Also known as: Golli-MBP3, TP8

The sequence of this isoform differs from the canonical sequence as follows:
     48-250: EADAIQNNGT...SRSGSPMARR → LTHENYPLWLPAPEVAARPDPR

Show »
Length:69
Mass (Da):7,498
Checksum:i067EABB28D687D99
GO
Isoform 4 (identifier: P04370-4) [UniParc]FASTAAdd to Basket

Also known as: 21.5-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK
     236-236: K → KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 122. Contains a phosphoserine at position 139. Contains a phosphotyrosine at position 151.

Show »
Length:195
Mass (Da):21,502
Checksum:i4B57CA6F06C4AC7D
GO
Isoform 5 (identifier: P04370-5) [UniParc]FASTAAdd to Basket

Also known as: 18.5-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     236-236: K → KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 96. Contains a phosphoserine at position 113. Contains a phosphotyrosine at position 125.

Show »
Length:169
Mass (Da):18,488
Checksum:iE609240A863F36CD
GO
Isoform 6 (identifier: P04370-6) [UniParc]FASTAAdd to Basket

Also known as: 17-kDa-a

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK
     236-236: K → KGRGLSLSRFSW

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 122.

Show »
Length:154
Mass (Da):17,225
Checksum:i00F1F10ECF90421B
GO
Isoform 7 (identifier: P04370-7) [UniParc]FASTAAdd to Basket

Also known as: 17-kDa-b

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     236-236: K → KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).

Show »
Length:158
Mass (Da):17,240
Checksum:i7AA39D2A263A2BF3
GO
Isoform 8 (identifier: P04370-8) [UniParc]FASTAAdd to Basket

Also known as: 14-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     236-236: K → KGRGLSLSRFSW

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity). Contains a phosphothreonine at position 96.

Show »
Length:128
Mass (Da):14,211
Checksum:iE1DB77B2010455FB
GO
Isoform 9 (identifier: P04370-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK
     236-236: K → KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL

Note: Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).

Show »
Length:184
Mass (Da):20,255
Checksum:iB7F672275771E3F4
GO
Isoform 10 (identifier: P04370-10) [UniParc]FASTAAdd to Basket

Also known as: 21-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     236-236: K → KDFVPGDHHV...QGTLSKIFKL

Note: Contains a phosphoserine at position 135. Contains a phosphotyrosine at position 147.

Show »
Length:191
Mass (Da):20,814
Checksum:iD986AA8B506E2AE9
GO
Isoform 11 (identifier: P04370-11) [UniParc]FASTAAdd to Basket

Also known as: 19.7-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK
     236-236: K → KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSW

Show »
Length:176
Mass (Da):19,552
Checksum:i159154971A58A0CF
GO
Isoform 12 (identifier: P04370-13) [UniParc]FASTAAdd to Basket

Also known as: 15.6-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.
     190-190: K → KVPWLKQSRSPLPSHARSRPGLCHMYK

Show »
Length:143
Mass (Da):15,978
Checksum:i932F8612537F93E2
GO
Isoform 13 (identifier: P04370-14) [UniParc]FASTAAdd to Basket

Also known as: 13-kDa

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Show »
Length:117
Mass (Da):12,963
Checksum:i7FC65A7A1A8C7E53
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 133133Missing in isoform 4, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 11, isoform 12 and isoform 13. VSP_003312Add
BLAST
Alternative sequencei48 – 250203EADAI…PMARR → LTHENYPLWLPAPEVAARPD PR in isoform 3. VSP_003313Add
BLAST
Alternative sequencei190 – 1901K → KVPWLKQSRSPLPSHARSRP GLCHMYK in isoform 4, isoform 6, isoform 9, isoform 11 and isoform 12. VSP_003315
Alternative sequencei191 – 25060DSHTR…PMARR → VSSEP in isoform 2. VSP_003314Add
BLAST
Alternative sequencei236 – 2361K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSWGAEGQK PGFGYGGRASDYKSAHKGFK GAYDAQGTLSKIFKL in isoform 10. VSP_003317
Alternative sequencei236 – 2361K → KDFVPGDHHVNVSVVTVSFS SSQGRGLSLSRFSW in isoform 11. VSP_003316
Alternative sequencei236 – 2361K → KGRGLSLSRFSWGAEGQKPG FGYGGRASDYKSAHKGFKGA YDAQGTLSKIFKL in isoform 4 and isoform 5. VSP_003319
Alternative sequencei236 – 2361K → KGRGLSLSRFSW in isoform 6 and isoform 8. VSP_003318
Alternative sequencei236 – 2361K → KGAEGQKPGFGYGGRASDYK SAHKGFKGAYDAQGTLSKIF KL in isoform 7 and isoform 9. VSP_003320

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2052QK → HN1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11533
, M11291, M11529, M11530, M11531, M11532 Genomic DNA. Translation: AAA39496.1.
M11533
, M11291, M11529, M11530, M11531 Genomic DNA. Translation: AAA39497.1.
L00404
, L00398, L00400, L00401, L00402 Genomic DNA. Translation: AAA39499.1.
L00404
, L00398, L00399, L00400, L00401, L00402 Genomic DNA. Translation: AAA39500.1.
L00404
, L00398, L00400, L00401, L00402, L00403 Genomic DNA. Translation: AAA39501.1.
L00404
, L00398, L00399, L00400, L00401, L00402, L00403 Genomic DNA. Translation: AAA39502.1.
M15060 mRNA. Translation: AAB59711.1.
M15062 mRNA. Translation: AAB59712.1.
X67319 mRNA. Translation: CAA47733.1.
L07507 mRNA. Translation: AAA37720.1.
L07508 mRNA. Translation: AAA37721.1.
L07509 mRNA. Translation: AAA37722.1.
L07505, L07504 Genomic DNA. Translation: AAA37719.1.
AK005129 mRNA. Translation: BAB23830.1.
BC004704 mRNA. Translation: AAH04704.1.
M24410 Genomic DNA. Translation: AAA39498.1.
M36275 Genomic DNA. Translation: AAA39504.1.
K00989 mRNA. Translation: AAA39495.1.
M20010 mRNA. Translation: AAA39503.1.
CCDSiCCDS29373.1. [P04370-1]
CCDS29374.1. [P04370-2]
CCDS29376.1. [P04370-4]
CCDS29377.1. [P04370-5]
CCDS29378.1. [P04370-6]
CCDS29379.1. [P04370-7]
CCDS37875.1. [P04370-9]
PIRiA45421. MBMSB.
RefSeqiNP_001020416.1. NM_001025245.1. [P04370-2]
NP_001020422.1. NM_001025251.2. [P04370-4]
NP_001020425.1. NM_001025254.2. [P04370-9]
NP_001020426.1. NM_001025255.2. [P04370-5]
NP_001020427.1. NM_001025256.2. [P04370-6]
NP_001020429.1. NM_001025258.2. [P04370-7]
NP_001020430.1. NM_001025259.2. [P04370-8]
NP_034907.1. NM_010777.3. [P04370-1]
UniGeneiMm.252063.
Mm.454459.

Genome annotation databases

EnsembliENSMUST00000047865; ENSMUSP00000046185; ENSMUSG00000041607. [P04370-1]
ENSMUST00000062446; ENSMUSP00000053495; ENSMUSG00000041607. [P04370-4]
ENSMUST00000075372; ENSMUSP00000074836; ENSMUSG00000041607. [P04370-7]
ENSMUST00000080658; ENSMUSP00000079488; ENSMUSG00000041607. [P04370-6]
ENSMUST00000091789; ENSMUSP00000089393; ENSMUSG00000041607. [P04370-2]
ENSMUST00000102812; ENSMUSP00000099876; ENSMUSG00000041607. [P04370-5]
ENSMUST00000114674; ENSMUSP00000110322; ENSMUSG00000041607. [P04370-9]
ENSMUST00000143506; ENSMUSP00000138313; ENSMUSG00000041607. [P04370-3]
GeneIDi17196.
KEGGimmu:17196.
UCSCiuc008fts.1. mouse. [P04370-1]
uc008ftu.1. mouse. [P04370-4]
uc008ftv.1. mouse. [P04370-9]
uc008ftw.1. mouse. [P04370-5]
uc008fty.1. mouse. [P04370-7]
uc029tqh.1. mouse. [P04370-14]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M11533
, M11291 , M11529 , M11530 , M11531 , M11532 Genomic DNA. Translation: AAA39496.1 .
M11533
, M11291 , M11529 , M11530 , M11531 Genomic DNA. Translation: AAA39497.1 .
L00404
, L00398 , L00400 , L00401 , L00402 Genomic DNA. Translation: AAA39499.1 .
L00404
, L00398 , L00399 , L00400 , L00401 , L00402 Genomic DNA. Translation: AAA39500.1 .
L00404
, L00398 , L00400 , L00401 , L00402 , L00403 Genomic DNA. Translation: AAA39501.1 .
L00404
, L00398 , L00399 , L00400 , L00401 , L00402 , L00403 Genomic DNA. Translation: AAA39502.1 .
M15060 mRNA. Translation: AAB59711.1 .
M15062 mRNA. Translation: AAB59712.1 .
X67319 mRNA. Translation: CAA47733.1 .
L07507 mRNA. Translation: AAA37720.1 .
L07508 mRNA. Translation: AAA37721.1 .
L07509 mRNA. Translation: AAA37722.1 .
L07505 , L07504 Genomic DNA. Translation: AAA37719.1 .
AK005129 mRNA. Translation: BAB23830.1 .
BC004704 mRNA. Translation: AAH04704.1 .
M24410 Genomic DNA. Translation: AAA39498.1 .
M36275 Genomic DNA. Translation: AAA39504.1 .
K00989 mRNA. Translation: AAA39495.1 .
M20010 mRNA. Translation: AAA39503.1 .
CCDSi CCDS29373.1. [P04370-1 ]
CCDS29374.1. [P04370-2 ]
CCDS29376.1. [P04370-4 ]
CCDS29377.1. [P04370-5 ]
CCDS29378.1. [P04370-6 ]
CCDS29379.1. [P04370-7 ]
CCDS37875.1. [P04370-9 ]
PIRi A45421. MBMSB.
RefSeqi NP_001020416.1. NM_001025245.1. [P04370-2 ]
NP_001020422.1. NM_001025251.2. [P04370-4 ]
NP_001020425.1. NM_001025254.2. [P04370-9 ]
NP_001020426.1. NM_001025255.2. [P04370-5 ]
NP_001020427.1. NM_001025256.2. [P04370-6 ]
NP_001020429.1. NM_001025258.2. [P04370-7 ]
NP_001020430.1. NM_001025259.2. [P04370-8 ]
NP_034907.1. NM_010777.3. [P04370-1 ]
UniGenei Mm.252063.
Mm.454459.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LUG NMR - A 206-245 [» ]
DisProti DP00237.
ProteinModelPortali P04370.
SMRi P04370. Positions 206-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201336. 42 interactions.
IntActi P04370. 30 interactions.
MINTi MINT-4101448.

Chemistry

ChEMBLi CHEMBL1764935.

PTM databases

PhosphoSitei P04370.

Proteomic databases

MaxQBi P04370.
PaxDbi P04370.
PRIDEi P04370.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047865 ; ENSMUSP00000046185 ; ENSMUSG00000041607 . [P04370-1 ]
ENSMUST00000062446 ; ENSMUSP00000053495 ; ENSMUSG00000041607 . [P04370-4 ]
ENSMUST00000075372 ; ENSMUSP00000074836 ; ENSMUSG00000041607 . [P04370-7 ]
ENSMUST00000080658 ; ENSMUSP00000079488 ; ENSMUSG00000041607 . [P04370-6 ]
ENSMUST00000091789 ; ENSMUSP00000089393 ; ENSMUSG00000041607 . [P04370-2 ]
ENSMUST00000102812 ; ENSMUSP00000099876 ; ENSMUSG00000041607 . [P04370-5 ]
ENSMUST00000114674 ; ENSMUSP00000110322 ; ENSMUSG00000041607 . [P04370-9 ]
ENSMUST00000143506 ; ENSMUSP00000138313 ; ENSMUSG00000041607 . [P04370-3 ]
GeneIDi 17196.
KEGGi mmu:17196.
UCSCi uc008fts.1. mouse. [P04370-1 ]
uc008ftu.1. mouse. [P04370-4 ]
uc008ftv.1. mouse. [P04370-9 ]
uc008ftw.1. mouse. [P04370-5 ]
uc008fty.1. mouse. [P04370-7 ]
uc029tqh.1. mouse. [P04370-14 ]

Organism-specific databases

CTDi 4155.
MGIi MGI:96925. Mbp.

Phylogenomic databases

eggNOGi NOG75180.
GeneTreei ENSGT00390000014772.
HOVERGENi HBG008347.
InParanoidi P04370.
KOi K17269.
OMAi CAERRGH.
OrthoDBi EOG7M0NRZ.
PhylomeDBi P04370.
TreeFami TF333391.

Miscellaneous databases

ChiTaRSi MBP. mouse.
NextBioi 291554.
PMAP-CutDB P04370.
PROi P04370.
SOURCEi Search...

Gene expression databases

ArrayExpressi P04370.
Bgeei P04370.
CleanExi MM_MBP.
Genevestigatori P04370.

Family and domain databases

InterProi IPR000548. Myelin_BP.
[Graphical view ]
PANTHERi PTHR11429. PTHR11429. 1 hit.
Pfami PF01669. Myelin_MBP. 1 hit.
[Graphical view ]
PRINTSi PR00212. MYELINMBP.
PROSITEi PS00569. MYELIN_MBP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the myelin basic protein gene from mouse: one gene can encode both 14 kd and 18.5 kd MBPs by alternate use of exons."
    Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E.
    Cell 42:139-148(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Alternative splicing accounts for the four forms of myelin basic protein."
    de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S., Lazzarini R.A.
    Cell 43:721-727(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Identification of a cDNA coding for a fifth form of myelin basic protein in mouse."
    Newman S., Kitamura K., Campagnoni A.T.
    Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), NUCLEOTIDE SEQUENCE [MRNA] OF 9-194.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
  5. "A novel transcript overlapping the myelin basic protein gene."
    Grima B., Zelenika D., Pessac B.
    J. Neurochem. 59:2318-2323(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6.
    Tissue: Bone marrow.
  6. "Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain."
    Campagnoni A.T., Pribyl T.M., Campagnoni C.W., Kampf K., Amur-Umarjee S., Landry C.F., Handley V.W., Newman S., Garbay B., Kitamura K.
    J. Biol. Chem. 268:4930-4938(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6.
    Tissue: Brain.
  7. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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 9).
    Tissue: Mammary tumor.
  9. "The promoter elements of the mouse myelin basic protein gene function efficiently in NG108-15 neuronal/glial cells."
    Miura M., Tamura T.A., Aoyama A., Mikoshiba K.
    Gene 75:31-38(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157.
  10. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  11. "Gene organization and transcription of duplicated MBP genes of myelin deficient (shi(mld)) mutant mouse."
    Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M., Mikoshiba K.
    EMBO J. 7:77-83(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224.
  12. "Characterization of mouse myelin basic protein messenger RNAs with a myelin basic protein cDNA clone."
    Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J., Lazzarini R.A.
    Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 193-222.
  13. "Identification of three forms of human myelin basic protein by cDNA cloning."
    Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.
    Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9).
  14. "Identification of the new isoforms of mouse myelin basic protein: the existence of exon 5a."
    Aruga J., Okano H., Mikoshiba K.
    J. Neurochem. 56:1222-1226(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11).
    Tissue: Spinal cord.
  15. "Novel isoforms of mouse myelin basic protein predominantly expressed in embryonic stage."
    Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K., Shiota C., Kim S.U., Mikoshiba K.
    J. Neurochem. 60:1554-1563(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13).
    Tissue: Embryonic brain.
  16. "Embryonic expression of the myelin basic protein gene: identification of a promoter region that targets transgene expression to pioneer neurons."
    Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K., Campagnoni C.W., Campagnoni A.T.
    J. Neurosci. 18:7315-7327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  17. "The pathobiology of myelin mutants reveal novel biological functions of the MBP and PLP genes."
    Campagnoni A.T., Skoff R.P.
    Brain Pathol. 11:74-91(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
    Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
    Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND THR-229, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122 (ISOFORMS 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96 (ISOFORMS 5 AND 8), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  20. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147 (ISOFORM 10), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-125 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  21. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMBP_MOUSE
AccessioniPrimary (citable) accession number: P04370
Secondary accession number(s): Q01585
, Q03139, Q03176, Q61836, Q61837, Q99KE4, Q9QWP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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