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Protein

Ethylmalonyl-CoA decarboxylase

Gene

ECHDC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Decarboxylases ethylmalonyl-CoA decarboxylase, a potentially toxic metabolite, to form butyryl-CoA, suggesting it might be involved in metabolite proofreading. Also has methylmalonyl-CoA decarboxylase activity at lower level.1 Publication

Catalytic activityi

(S)-ethylmalonyl-CoA = butanoyl-CoA + CO2.
(S)-methylmalonyl-CoA = propanoyl-CoA + CO2.

GO - Molecular functioni

  1. carboxy-lyase activity Source: UniProtKB
  2. methylmalonyl-CoA decarboxylase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Names & Taxonomyi

Protein namesi
Recommended name:
Ethylmalonyl-CoA decarboxylase (EC:4.1.1.94)
Alternative name(s):
Enoyl-CoA hydratase domain-containing protein 1
Methylmalonyl-CoA decarboxylase (EC:4.1.1.41)
Short name:
MMCD
Gene namesi
Name:ECHDC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21489. ECHDC1.

Subcellular locationi

  1. Cytoplasmcytosol By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134871524.

Polymorphism and mutation databases

BioMutaiECHDC1.
DMDMi124007138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Ethylmalonyl-CoA decarboxylasePRO_0000273246Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei217 – 2171N6-acetyllysine; alternateBy similarity
Modified residuei217 – 2171N6-succinyllysine; alternateBy similarity
Modified residuei301 – 3011N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9NTX5.
PaxDbiQ9NTX5.
PRIDEiQ9NTX5.

PTM databases

PhosphoSiteiQ9NTX5.

Expressioni

Gene expression databases

BgeeiQ9NTX5.
CleanExiHS_ECHDC1.
ExpressionAtlasiQ9NTX5. baseline and differential.
GenevestigatoriQ9NTX5.

Organism-specific databases

HPAiHPA035445.

Interactioni

Protein-protein interaction databases

BioGridi120964. 3 interactions.
IntActiQ9NTX5. 2 interactions.
STRINGi9606.ENSP00000357278.

Structurei

3D structure databases

ProteinModelPortaliQ9NTX5.
SMRiQ9NTX5. Positions 57-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00720000108837.
HOGENOMiHOG000007808.
HOVERGENiHBG054783.
InParanoidiQ9NTX5.
KOiK18426.
OMAiHKHMGLV.
OrthoDBiEOG79W95T.
PhylomeDBiQ9NTX5.
TreeFamiTF315986.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NTX5-1) [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
MALKQEMAKS LLKTASLSGR TKLLHQTGLS LYSTSHGFYE EEVKKTLQQF
60 70 80 90 100
PGGSIDLQKE DNGIGILTLN NPSRMNAFSG VMMLQLLEKV IELENWTEGK
110 120 130 140 150
GLIVRGAKNT FSSGSDLNAV KSLGTPEDGM AVCMFMQNTL TRFMRLPLIS
160 170 180 190 200
VALVQGWALG GGAEFTTACD FRLMTPESKI RFVHKEMGII PSWGGTTRLV
210 220 230 240 250
EIIGSRQALK VLSGALKLDS KNALNIGMVE EVLQSSDETK SLEEAQEWLK
260 270 280 290 300
QFIQGPPEVI RALKKSVCSG RELYLEEALQ NERDLLGTVW GGPANLEAIA

KKGKFNK
Length:307
Mass (Da):33,698
Last modified:January 23, 2007 - v2
Checksum:i77A09FDE065FE0A4
GO
Isoform 2 (identifier: Q9NTX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.1 Publication

Show »
Length:301
Mass (Da):32,997
Checksum:iFB931678ECFB2EDA
GO
Isoform 3 (identifier: Q9NTX5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: No experimental confirmation available.

Show »
Length:226
Mass (Da):24,859
Checksum:iA2C02B29FEC517AA
GO
Isoform 4 (identifier: Q9NTX5-4) [UniParc]FASTAAdd to basket

Also known as: HEL-S-76

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
     128-307: DGMAVCMFMQ...AIAKKGKFNK → TSFNKCCAGSRLGIGWRSRIYYSM

Show »
Length:70
Mass (Da):7,745
Checksum:i97019CB346725D86
GO
Isoform 5 (identifier: Q9NTX5-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.
     128-307: DGMAVCMFMQ...AIAKKGKFNK → TSFNKCCAGSRLGIGWRSRIYYSM

Note: No experimental confirmation available. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.1 Publication

Show »
Length:145
Mass (Da):15,883
Checksum:i25FBCA2D6665D089
GO
Isoform 6 (identifier: Q9NTX5-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.
     125-144: TPEDGMAVCMFMQNTLTRFM → LQR

Note: No experimental confirmation available. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2.1 Publication

Show »
Length:284
Mass (Da):31,089
Checksum:i667B60F58667A5C4
GO

Sequence cautioni

The sequence AAF67657.1 differs from that shown. Reason: Frameshift at positions 121, 123 and 125. Curated
The sequence CAI20295.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI20297.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431E → G in BAH14056 (PubMed:14702039).Curated
Sequence conflicti263 – 2631L → M in BAH14056 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform 3 and isoform 4. 2 PublicationsVSP_042581Add
BLAST
Alternative sequencei1 – 66Missing in isoform 2, isoform 5 and isoform 6. 3 PublicationsVSP_022498
Alternative sequencei125 – 14420TPEDG…LTRFM → LQR in isoform 6. 1 PublicationVSP_042582Add
BLAST
Alternative sequencei128 – 307180DGMAV…GKFNK → TSFNKCCAGSRLGIGWRSRI YYSM in isoform 4 and isoform 5. 1 PublicationVSP_042583Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU668355 mRNA. Translation: ACF94508.1.
AL834469 mRNA. Translation: CAD39128.1.
AK303812 mRNA. Translation: BAH14056.1.
AF220192 mRNA. Translation: AAF67657.1. Frameshift.
AL109939 Genomic DNA. Translation: CAB76256.1.
AL109939 Genomic DNA. Translation: CAI20295.1. Sequence problems.
AL109939 Genomic DNA. Translation: CAI20297.1. Sequence problems.
AL109939 Genomic DNA. Translation: CAI20302.1.
AL109939 Genomic DNA. Translation: CAI20298.1.
CH471051 Genomic DNA. Translation: EAW48107.1.
BC003549 mRNA. Translation: AAH03549.1.
CCDSiCCDS34530.1. [Q9NTX5-5]
CCDS43504.1. [Q9NTX5-2]
CCDS47471.1. [Q9NTX5-1]
CCDS47472.1. [Q9NTX5-3]
CCDS55054.1. [Q9NTX5-4]
RefSeqiNP_001002030.1. NM_001002030.1. [Q9NTX5-2]
NP_001099014.1. NM_001105544.1. [Q9NTX5-3]
NP_001099015.1. NM_001105545.1. [Q9NTX5-4]
NP_001132982.1. NM_001139510.1. [Q9NTX5-1]
NP_060949.2. NM_018479.3. [Q9NTX5-5]
XP_005267104.1. XM_005267047.1. [Q9NTX5-2]
XP_005267105.1. XM_005267048.1. [Q9NTX5-2]
XP_005267107.1. XM_005267050.1. [Q9NTX5-5]
UniGeneiHs.486410.

Genome annotation databases

EnsembliENST00000368289; ENSP00000357272; ENSG00000093144. [Q9NTX5-5]
ENST00000368291; ENSP00000357274; ENSG00000093144. [Q9NTX5-5]
ENST00000430841; ENSP00000402492; ENSG00000093144. [Q9NTX5-2]
ENST00000454591; ENSP00000404866; ENSG00000093144. [Q9NTX5-3]
ENST00000454859; ENSP00000401751; ENSG00000093144. [Q9NTX5-2]
ENST00000474289; ENSP00000434908; ENSG00000093144. [Q9NTX5-2]
ENST00000528402; ENSP00000436109; ENSG00000093144. [Q9NTX5-4]
ENST00000531967; ENSP00000436585; ENSG00000093144. [Q9NTX5-1]
GeneIDi55862.
KEGGihsa:55862.
UCSCiuc003qax.3. human. [Q9NTX5-1]
uc003qay.4. human. [Q9NTX5-5]
uc010kez.3. human. [Q9NTX5-4]

Polymorphism and mutation databases

BioMutaiECHDC1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU668355 mRNA. Translation: ACF94508.1.
AL834469 mRNA. Translation: CAD39128.1.
AK303812 mRNA. Translation: BAH14056.1.
AF220192 mRNA. Translation: AAF67657.1. Frameshift.
AL109939 Genomic DNA. Translation: CAB76256.1.
AL109939 Genomic DNA. Translation: CAI20295.1. Sequence problems.
AL109939 Genomic DNA. Translation: CAI20297.1. Sequence problems.
AL109939 Genomic DNA. Translation: CAI20302.1.
AL109939 Genomic DNA. Translation: CAI20298.1.
CH471051 Genomic DNA. Translation: EAW48107.1.
BC003549 mRNA. Translation: AAH03549.1.
CCDSiCCDS34530.1. [Q9NTX5-5]
CCDS43504.1. [Q9NTX5-2]
CCDS47471.1. [Q9NTX5-1]
CCDS47472.1. [Q9NTX5-3]
CCDS55054.1. [Q9NTX5-4]
RefSeqiNP_001002030.1. NM_001002030.1. [Q9NTX5-2]
NP_001099014.1. NM_001105544.1. [Q9NTX5-3]
NP_001099015.1. NM_001105545.1. [Q9NTX5-4]
NP_001132982.1. NM_001139510.1. [Q9NTX5-1]
NP_060949.2. NM_018479.3. [Q9NTX5-5]
XP_005267104.1. XM_005267047.1. [Q9NTX5-2]
XP_005267105.1. XM_005267048.1. [Q9NTX5-2]
XP_005267107.1. XM_005267050.1. [Q9NTX5-5]
UniGeneiHs.486410.

3D structure databases

ProteinModelPortaliQ9NTX5.
SMRiQ9NTX5. Positions 57-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120964. 3 interactions.
IntActiQ9NTX5. 2 interactions.
STRINGi9606.ENSP00000357278.

PTM databases

PhosphoSiteiQ9NTX5.

Polymorphism and mutation databases

BioMutaiECHDC1.
DMDMi124007138.

Proteomic databases

MaxQBiQ9NTX5.
PaxDbiQ9NTX5.
PRIDEiQ9NTX5.

Protocols and materials databases

DNASUi55862.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368289; ENSP00000357272; ENSG00000093144. [Q9NTX5-5]
ENST00000368291; ENSP00000357274; ENSG00000093144. [Q9NTX5-5]
ENST00000430841; ENSP00000402492; ENSG00000093144. [Q9NTX5-2]
ENST00000454591; ENSP00000404866; ENSG00000093144. [Q9NTX5-3]
ENST00000454859; ENSP00000401751; ENSG00000093144. [Q9NTX5-2]
ENST00000474289; ENSP00000434908; ENSG00000093144. [Q9NTX5-2]
ENST00000528402; ENSP00000436109; ENSG00000093144. [Q9NTX5-4]
ENST00000531967; ENSP00000436585; ENSG00000093144. [Q9NTX5-1]
GeneIDi55862.
KEGGihsa:55862.
UCSCiuc003qax.3. human. [Q9NTX5-1]
uc003qay.4. human. [Q9NTX5-5]
uc010kez.3. human. [Q9NTX5-4]

Organism-specific databases

CTDi55862.
GeneCardsiGC06M127609.
H-InvDBHIX0006203.
HGNCiHGNC:21489. ECHDC1.
HPAiHPA035445.
MIMi612136. gene.
neXtProtiNX_Q9NTX5.
PharmGKBiPA134871524.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1024.
GeneTreeiENSGT00720000108837.
HOGENOMiHOG000007808.
HOVERGENiHBG054783.
InParanoidiQ9NTX5.
KOiK18426.
OMAiHKHMGLV.
OrthoDBiEOG79W95T.
PhylomeDBiQ9NTX5.
TreeFamiTF315986.

Miscellaneous databases

ChiTaRSiECHDC1. human.
GenomeRNAii55862.
NextBioi61169.
PROiQ9NTX5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NTX5.
CleanExiHS_ECHDC1.
ExpressionAtlasiQ9NTX5. baseline and differential.
GenevestigatoriQ9NTX5.

Family and domain databases

Gene3Di3.90.226.10. 1 hit.
InterProiIPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR018376. Enoyl-CoA_hyd/isom_CS.
[Graphical view]
PfamiPF00378. ECH. 1 hit.
[Graphical view]
SUPFAMiSSF52096. SSF52096. 1 hit.
PROSITEiPS00166. ENOYL_COA_HYDRATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Li J.Y., Wang H.Y., Liu F.J., Liu J.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Epididymis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Melanoma.
  3. "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 3).
    Tissue: Liver.
  4. "A novel gene expressed in human adrenal gland."
    Xiao H., Song H., Gao G., Ren S., Chen Z., Han Z.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
    Tissue: Hypothalamus.
  5. "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].
  6. 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] (ISOFORM 2).
    Tissue: Skin.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: FUNCTION.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 2; 5 AND 6), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORMS 2; 5 AND 6).
  11. "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.

Entry informationi

Entry nameiECHD1_HUMAN
AccessioniPrimary (citable) accession number: Q9NTX5
Secondary accession number(s): A6NFJ5
, B7Z8S0, E9PEN7, E9PR31, F8W851, Q5TEF6, Q5TEF7, Q5TEG0, Q5TEG4, Q9NZ30, V9HW18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 112 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.