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Protein

Protein-L-isoaspartate(D-aspartate) O-methyltransferase

Gene

PCMT1

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

Functioni

Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein.By similarity

Catalytic activityi

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 601

GO - Molecular functioni

  • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • protein methylation Source: ProtInc
  • protein repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.77. 2681.
ReactomeiR-HSA-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (EC:2.1.1.77)
Short name:
PIMT
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl/D-aspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Gene namesi
Name:PCMT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:8728. PCMT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4240.

Polymorphism and mutation databases

BioMutaiPCMT1.
DMDMi317373537.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 227226Protein-L-isoaspartate(D-aspartate) O-methyltransferasePRO_0000111875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Disulfide bondi43 ↔ 95By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

EPDiP22061.
MaxQBiP22061.
PaxDbiP22061.
PRIDEiP22061.

2D gel databases

OGPiP22061.
REPRODUCTION-2DPAGEIPI00411680.
UCD-2DPAGEP22061.

PTM databases

iPTMnetiP22061.
PhosphoSiteiP22061.

Expressioni

Gene expression databases

BgeeiP22061.
ExpressionAtlasiP22061. baseline and differential.
GenevisibleiP22061. HS.

Organism-specific databases

HPAiHPA003239.

Interactioni

Subunit structurei

Monomer.

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP2Q131553EBI-353343,EBI-745226
RPIAP492473EBI-353343,EBI-744831

Protein-protein interaction databases

BioGridi111141. 95 interactions.
IntActiP22061. 20 interactions.
MINTiMINT-234244.
STRINGi9606.ENSP00000356348.

Chemistry

BindingDBiP22061.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Helixi26 – 338Combined sources
Helixi37 – 393Combined sources
Beta strandi47 – 493Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Helixi62 – 7110Combined sources
Turni72 – 754Combined sources
Beta strandi81 – 855Combined sources
Helixi91 – 10010Combined sources
Turni101 – 1033Combined sources
Beta strandi105 – 1117Combined sources
Helixi113 – 12614Combined sources
Helixi129 – 1324Combined sources
Beta strandi134 – 1418Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 1503Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi160 – 1645Combined sources
Helixi167 – 1715Combined sources
Beta strandi173 – 18412Combined sources
Beta strandi190 – 1978Combined sources
Beta strandi203 – 2119Combined sources
Helixi219 – 2224Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1NX-ray1.50A2-227[»]
1KR5X-ray2.10A2-227[»]
ProteinModelPortaliP22061.
SMRiP22061. Positions 3-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22061.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
HOVERGENiHBG004483.
InParanoidiP22061.
KOiK00573.
PhylomeDBiP22061.
TreeFamiTF314431.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000682. PCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11579. PTHR11579. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00080. pimt. 1 hit.
PROSITEiPS01279. PCMT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P22061-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP
60 70 80 90 100
QSIGFQATIS APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV
110 120 130 140 150
GCTGKVIGID HIKELVDDSV NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE
160 170 180 190 200
APYDAIHVGA AAPVVPQALI DQLKPGGRLI LPVGPAGGNQ MLEQYDKLQD
210 220
GSIKMKPLMG VIYVPLTDKE KQWSRWK
Length:227
Mass (Da):24,636
Last modified:January 11, 2011 - v4
Checksum:i4EB1122379C8040A
GO
Isoform 2 (identifier: P22061-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     226-227: WK → DEL

Show »
Length:228
Mass (Da):24,679
Checksum:i69E688C22379C804
GO

Sequence cautioni

The sequence EAW47786.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191K → G AA sequence (PubMed:3167043).Curated
Sequence conflicti23 – 231I → L AA sequence (PubMed:2684970).Curated
Sequence conflicti60 – 601S → A AA sequence (PubMed:3167043).Curated
Sequence conflicti102 – 1021C → Q AA sequence (PubMed:2684970).Curated
Sequence conflicti168 – 1681A → P AA sequence (PubMed:3167043).Curated
Sequence conflicti206 – 2061K → R in AAA90933 (PubMed:1339271).Curated

Polymorphismi

The allele frequencies for the polymorphism at codon 120 differ between ethnic groups; in the Caucasian population Ile-120 is present at a frequency of 0.45, while it is found at a frequency of 0.88 and 0.81 in the Asian and the African populations respectively. Val-120 is found at a frequency of 0.55 in the Caucasians, 0.12 and 0.19 in the Asian and African populations respectively. The Ile-120 variant has higher specific activity and thermostability than the Val-120 variant. The Val-120 variant has a higher affinity for protein substrates.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201V → I.Combined sources5 Publications
Corresponds to variant rs4816 [ dbSNP | Ensembl ].
VAR_006173

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei226 – 2272WK → DEL in isoform 2. 4 PublicationsVSP_004716

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93008 mRNA. Translation: AAA90934.1.
M93009 mRNA. Translation: AAA90933.1.
D25545 mRNA. Translation: BAA05028.1.
D25546 mRNA. Translation: BAA05029.1.
D25547 mRNA. Translation: BAA05030.1.
D13892 mRNA. Translation: BAA02991.1.
AK289724 mRNA. Translation: BAF82413.1.
AL355312 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW47786.1. Sequence problems.
BC007501 mRNA. Translation: AAH07501.1.
BC008748 mRNA. Translation: AAH08748.1.
U49740 Genomic DNA. Translation: AAB38386.1.
S73902 Genomic DNA. Translation: AAC60639.2.
S73903 Genomic DNA. Translation: AAC60640.1.
S73905 Genomic DNA. Translation: AAC60641.2.
PIRiA34489.
JH0624.
RefSeqiNP_001238978.1. NM_001252049.1.
NP_001238982.1. NM_001252053.1.
NP_005380.2. NM_005389.2.
UniGeneiHs.279257.

Genome annotation databases

EnsembliENST00000367380; ENSP00000356350; ENSG00000120265.
GeneIDi5110.
KEGGihsa:5110.
UCSCiuc011eeg.3. human. [P22061-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M93008 mRNA. Translation: AAA90934.1.
M93009 mRNA. Translation: AAA90933.1.
D25545 mRNA. Translation: BAA05028.1.
D25546 mRNA. Translation: BAA05029.1.
D25547 mRNA. Translation: BAA05030.1.
D13892 mRNA. Translation: BAA02991.1.
AK289724 mRNA. Translation: BAF82413.1.
AL355312 Genomic DNA. No translation available.
CH471051 Genomic DNA. Translation: EAW47786.1. Sequence problems.
BC007501 mRNA. Translation: AAH07501.1.
BC008748 mRNA. Translation: AAH08748.1.
U49740 Genomic DNA. Translation: AAB38386.1.
S73902 Genomic DNA. Translation: AAC60639.2.
S73903 Genomic DNA. Translation: AAC60640.1.
S73905 Genomic DNA. Translation: AAC60641.2.
PIRiA34489.
JH0624.
RefSeqiNP_001238978.1. NM_001252049.1.
NP_001238982.1. NM_001252053.1.
NP_005380.2. NM_005389.2.
UniGeneiHs.279257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I1NX-ray1.50A2-227[»]
1KR5X-ray2.10A2-227[»]
ProteinModelPortaliP22061.
SMRiP22061. Positions 3-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111141. 95 interactions.
IntActiP22061. 20 interactions.
MINTiMINT-234244.
STRINGi9606.ENSP00000356348.

Chemistry

BindingDBiP22061.
ChEMBLiCHEMBL4240.

PTM databases

iPTMnetiP22061.
PhosphoSiteiP22061.

Polymorphism and mutation databases

BioMutaiPCMT1.
DMDMi317373537.

2D gel databases

OGPiP22061.
REPRODUCTION-2DPAGEIPI00411680.
UCD-2DPAGEP22061.

Proteomic databases

EPDiP22061.
MaxQBiP22061.
PaxDbiP22061.
PRIDEiP22061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367380; ENSP00000356350; ENSG00000120265.
GeneIDi5110.
KEGGihsa:5110.
UCSCiuc011eeg.3. human. [P22061-1]

Organism-specific databases

CTDi5110.
GeneCardsiPCMT1.
HGNCiHGNC:8728. PCMT1.
HPAiHPA003239.
MIMi176851. gene.
neXtProtiNX_P22061.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
HOVERGENiHBG004483.
InParanoidiP22061.
KOiK00573.
PhylomeDBiP22061.
TreeFamiTF314431.

Enzyme and pathway databases

BRENDAi2.1.1.77. 2681.
ReactomeiR-HSA-5676934. Protein repair.

Miscellaneous databases

EvolutionaryTraceiP22061.
GeneWikiiPCMT1.
GenomeRNAii5110.
NextBioi19718.
PROiP22061.
SOURCEiSearch...

Gene expression databases

BgeeiP22061.
ExpressionAtlasiP22061. baseline and differential.
GenevisibleiP22061. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000682. PCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11579. PTHR11579. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00080. pimt. 1 hit.
PROSITEiPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases."
    Ingrosso D., Fowler A.V., Bleibaum J., Clarke S.
    J. Biol. Chem. 264:20131-20139(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE.
    Tissue: Erythrocyte.
  2. "Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II."
    Maclaren D.C., Kagan R.M., Clarke S.
    Biochem. Biophys. Res. Commun. 185:277-283(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-120.
    Tissue: Brain cortex.
  3. "Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells."
    Takeda R., Mizobuchi M., Murao K., Sato M., Takahara J.
    J. Biochem. 117:683-685(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  4. "Gene expression of carboxyl methyltransferase is altered in Alzheimer's disease and the product is localized to neurofibrillary tangles."
    Shirasawa T., Takahashi H., Endoh R., Sakamoto K., Hirokawa K., Mori H.
    Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  5. "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] (ISOFORM 1).
    Tissue: Brain.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORMS 1 AND 2), VARIANT ILE-120.
    Tissue: Muscle and Skin.
  9. "Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase."
    Devry C.G., Tsai W., Clarke S.
    Arch. Biochem. Biophys. 335:321-332(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
    Tissue: Foreskin.
  10. "Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes."
    Gilbert J.M., Fowler A., Bleibaum J., Clarke S.
    Biochemistry 27:5227-5233(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-19; 44-60; 106-170; 179-198 AND 205-220.
  11. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-18; 25-37; 82-98; 114-144 AND 179-221, VARIANT ILE-120, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  12. "Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair."
    Tsai W., Clarke S.
    Biochem. Biophys. Res. Commun. 203:491-497(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-53; 100-139 AND 169-224.
  13. "Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase."
    Ingrosso D., Kagan R.M., Clarke S.
    Biochem. Biophys. Res. Commun. 175:351-358(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE (ISOFORM 2), VARIANT ILE-120.
    Tissue: Erythrocyte.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins."
    DeVry C.G., Clarke S.
    J. Hum. Genet. 44:275-288(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ILE-120.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
  18. "Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site."
    Smith C.D., Carson M., Friedman A.M., Skinner M.M., Delucas L., Chantalat L., Weise L., Shirasawa T., Chattopadhyay D.
    Protein Sci. 11:625-635(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  19. Cited for: VARIANT [LARGE SCALE ANALYSIS] ILE-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPIMT_HUMAN
AccessioniPrimary (citable) accession number: P22061
Secondary accession number(s): A8K109
, J3KP72, Q14661, Q16556, Q5VYC1, Q5VYC2, Q93061, Q96II9, Q99625, Q9BQV7, Q9BQV8, Q9NP03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 11, 2011
Last modified: May 11, 2016
This is version 174 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.