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O75521

- ECI2_HUMAN

UniProt

O75521 - ECI2_HUMAN

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Protein

Enoyl-CoA delta isomerase 2, mitochondrial

Gene

ECI2

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

Functioni

Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity).By similarity

Catalytic activityi

(3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei92 – 921Acyl-CoABy similarity
Binding sitei111 – 1111Acyl-CoABy similarity

GO - Molecular functioni

  1. dodecenoyl-CoA delta-isomerase activity Source: UniProtKB
  2. fatty-acyl-CoA binding Source: InterPro
  3. receptor binding Source: UniProtKB

GO - Biological processi

  1. fatty acid catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-CoA delta isomerase 2, mitochondrial (EC:5.3.3.8)
Alternative name(s):
DRS-1
Delta(3),delta(2)-enoyl-CoA isomerase
Short name:
D3,D2-enoyl-CoA isomerase
Diazepam-binding inhibitor-related protein 1
Short name:
DBI-related protein 1
Dodecenoyl-CoA isomerase
Hepatocellular carcinoma-associated antigen 88
Peroxisomal 3,2-trans-enoyl-CoA isomerase
Short name:
pECI
Renal carcinoma antigen NY-REN-1
Gene namesi
Name:ECI2
Synonyms:DRS1, HCA88, PECI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:14601. ECI2.

Subcellular locationi

Isoform 1 : Mitochondrion By similarity

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. membrane Source: UniProtKB
  3. mitochondrion Source: LIFEdb
  4. nucleus Source: HPA
  5. peroxisomal matrix Source: UniProtKB
  6. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3838MitochondrionSequence AnalysisAdd
BLAST
Chaini39 – 394356Enoyl-CoA delta isomerase 2, mitochondrialPRO_0000214027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine; alternate1 Publication
Modified residuei51 – 511N6-succinyllysine; alternateBy similarity
Modified residuei55 – 551N6-succinyllysineBy similarity
Modified residuei62 – 621N6-acetyllysine; alternateBy similarity
Modified residuei62 – 621N6-succinyllysine; alternateBy similarity
Modified residuei70 – 701N6-succinyllysineBy similarity
Modified residuei81 – 811N6-succinyllysineBy similarity
Modified residuei90 – 901N6-succinyllysineBy similarity
Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Modified residuei161 – 1611N6-succinyllysineBy similarity
Modified residuei289 – 2891N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO75521.
PaxDbiO75521.
PRIDEiO75521.

2D gel databases

REPRODUCTION-2DPAGEIPI00419263.
UCD-2DPAGEO75521.

PTM databases

PhosphoSiteiO75521.

Expressioni

Tissue specificityi

Abundant in heart, skeletal muscle and liver. Expressed in CD34+ T-cells and CD34+ bone marrow cells.1 Publication

Gene expression databases

BgeeiO75521.
ExpressionAtlasiO75521. baseline and differential.
GenevestigatoriO75521.

Organism-specific databases

HPAiHPA022130.
HPA031626.

Interactioni

Protein-protein interaction databases

BioGridi115718. 16 interactions.
IntActiO75521. 7 interactions.
MINTiMINT-3001383.

Structurei

Secondary structure

1
394
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 5213
Helixi59 – 6911
Turni70 – 745
Helixi87 – 9913
Helixi104 – 11815
Beta strandi140 – 1478
Beta strandi150 – 1556
Helixi158 – 1603
Helixi166 – 18116
Beta strandi185 – 1928
Helixi212 – 23221
Beta strandi238 – 2425
Helixi249 – 2524
Helixi253 – 2564
Beta strandi258 – 2636
Beta strandi267 – 2693
Helixi273 – 2753
Helixi283 – 2919
Helixi293 – 3008
Helixi308 – 3136
Beta strandi318 – 3214
Turni323 – 3253
Helixi326 – 33712
Helixi342 – 35312
Helixi354 – 3563
Helixi357 – 37519
Helixi378 – 3814

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQUNMR-A31-133[»]
2F6QX-ray1.95A/B/C138-394[»]
ProteinModelPortaliO75521.
SMRiO75521. Positions 31-133, 139-390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75521.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 12486ACBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 705Acyl-CoA bindingBy similarity
Regioni151 – 322172ECH-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi392 – 3943Microbody targeting signalSequence Analysis

Sequence similaritiesi

In the C-terminal section; belongs to the enoyl-CoA hydratase/isomerase family.Curated
Contains 1 ACB (acyl-CoA-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG4281.
GeneTreeiENSGT00760000119100.
HOVERGENiHBG006723.
InParanoidiO75521.
KOiK13239.
OMAiRWLSDEC.
OrthoDBiEOG72RN06.
PhylomeDBiO75521.
TreeFamiTF313375.

Family and domain databases

Gene3Di1.20.80.10. 1 hit.
3.90.226.10. 1 hit.
InterProiIPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view]
PfamiPF00887. ACBP. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view]
PRINTSiPR00689. ACOABINDINGP.
SUPFAMiSSF47027. SSF47027. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEiPS00880. ACB_1. 1 hit.
PS51228. ACB_2. 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. Align

Isoform 1 (identifier: O75521-1) [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
MAMAYLAWRL ARRSCPSSLQ VTSFPVVQLH MNRTAMRASQ KDFENSMNQV
60 70 80 90 100
KLLKKDPGNE VKLKLYALYK QATEGPCNMP KPGVFDLINK AKWDAWNALG
110 120 130 140 150
SLPKEAARQN YVDLVSSLSP SLESSSQVEP GTDRKSTGFE TLVVTSEDGI
160 170 180 190 200
TKIMFNRPKK KNAINTEMYH EIMRALKAAS KDDSIITVLT GNGDYYSSGN
210 220 230 240 250
DLTNFTDIPP GGVEEKAKNN AVLLREFVGC FIDFPKPLIA VVNGPAVGIS
260 270 280 290 300
VTLLGLFDAV YASDRATFHT PFSHLGQSPE GCSSYTFPKI MSPAKATEML
310 320 330 340 350
IFGKKLTAGE ACAQGLVTEV FPDSTFQKEV WTRLKAFAKL PPNALRISKE
360 370 380 390
VIRKREREKL HAVNAEECNV LQGRWLSDEC TNAVVNFLSR KSKL
Length:394
Mass (Da):43,585
Last modified:September 1, 2009 - v4
Checksum:i8AC633D43A320102
GO
Isoform 2 (identifier: O75521-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Show »
Length:359
Mass (Da):39,609
Checksum:iB9EC60A0D445C9F0
GO

Sequence cautioni

The sequence AAC19317.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAD34173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAF66247.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH02668.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH16781.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH17474.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH33841.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAH34702.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAG52068.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191S → C in CAB66577. (PubMed:11230166)Curated
Sequence conflicti195 – 1951Y → C in AAC19317. (PubMed:10354522)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471M → I.
Corresponds to variant rs3177253 [ dbSNP | Ensembl ].
VAR_058493
Natural varianti344 – 3441A → V.2 Publications
Corresponds to variant rs7166 [ dbSNP | Ensembl ].
VAR_058494

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3535Missing in isoform 2. 3 PublicationsVSP_037854Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF069301 mRNA. Translation: AAC19317.1. Different initiation.
AL136642 mRNA. Translation: CAB66577.1.
AK075108 mRNA. Translation: BAG52068.1. Different initiation.
AL033383 Genomic DNA. Translation: CAI42125.1.
AL033383 Genomic DNA. Translation: CAI42127.1.
BC002668 mRNA. Translation: AAH02668.3. Different initiation.
BC016781 mRNA. Translation: AAH16781.1. Different initiation.
BC017474 mRNA. Translation: AAH17474.1. Different initiation.
BC033841 mRNA. Translation: AAH33841.3. Different initiation.
BC034702 mRNA. Translation: AAH34702.1. Different initiation.
AF153612 mRNA. Translation: AAD34173.1. Different initiation.
AF244138 mRNA. Translation: AAF66247.1. Different initiation.
CCDSiCCDS43420.2. [O75521-1]
RefSeqiNP_001159482.1. NM_001166010.1.
NP_006108.2. NM_006117.2.
NP_996667.2. NM_206836.2. [O75521-1]
UniGeneiHs.15250.

Genome annotation databases

EnsembliENST00000361538; ENSP00000354737; ENSG00000198721.
ENST00000380118; ENSP00000369461; ENSG00000198721. [O75521-1]
ENST00000380125; ENSP00000369468; ENSG00000198721.
ENST00000465828; ENSP00000420309; ENSG00000198721.
GeneIDi10455.
KEGGihsa:10455.
UCSCiuc003mwc.3. human. [O75521-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF069301 mRNA. Translation: AAC19317.1 . Different initiation.
AL136642 mRNA. Translation: CAB66577.1 .
AK075108 mRNA. Translation: BAG52068.1 . Different initiation.
AL033383 Genomic DNA. Translation: CAI42125.1 .
AL033383 Genomic DNA. Translation: CAI42127.1 .
BC002668 mRNA. Translation: AAH02668.3 . Different initiation.
BC016781 mRNA. Translation: AAH16781.1 . Different initiation.
BC017474 mRNA. Translation: AAH17474.1 . Different initiation.
BC033841 mRNA. Translation: AAH33841.3 . Different initiation.
BC034702 mRNA. Translation: AAH34702.1 . Different initiation.
AF153612 mRNA. Translation: AAD34173.1 . Different initiation.
AF244138 mRNA. Translation: AAF66247.1 . Different initiation.
CCDSi CCDS43420.2. [O75521-1 ]
RefSeqi NP_001159482.1. NM_001166010.1.
NP_006108.2. NM_006117.2.
NP_996667.2. NM_206836.2. [O75521-1 ]
UniGenei Hs.15250.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQU NMR - A 31-133 [» ]
2F6Q X-ray 1.95 A/B/C 138-394 [» ]
ProteinModelPortali O75521.
SMRi O75521. Positions 31-133, 139-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115718. 16 interactions.
IntActi O75521. 7 interactions.
MINTi MINT-3001383.

PTM databases

PhosphoSitei O75521.

2D gel databases

REPRODUCTION-2DPAGE IPI00419263.
UCD-2DPAGE O75521.

Proteomic databases

MaxQBi O75521.
PaxDbi O75521.
PRIDEi O75521.

Protocols and materials databases

DNASUi 10455.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361538 ; ENSP00000354737 ; ENSG00000198721 .
ENST00000380118 ; ENSP00000369461 ; ENSG00000198721 . [O75521-1 ]
ENST00000380125 ; ENSP00000369468 ; ENSG00000198721 .
ENST00000465828 ; ENSP00000420309 ; ENSG00000198721 .
GeneIDi 10455.
KEGGi hsa:10455.
UCSCi uc003mwc.3. human. [O75521-1 ]

Organism-specific databases

CTDi 10455.
GeneCardsi GC06M004115.
H-InvDB HIX0025043.
HGNCi HGNC:14601. ECI2.
HPAi HPA022130.
HPA031626.
MIMi 608024. gene.
neXtProti NX_O75521.
PharmGKBi PA33168.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4281.
GeneTreei ENSGT00760000119100.
HOVERGENi HBG006723.
InParanoidi O75521.
KOi K13239.
OMAi RWLSDEC.
OrthoDBi EOG72RN06.
PhylomeDBi O75521.
TreeFami TF313375.

Miscellaneous databases

EvolutionaryTracei O75521.
GeneWikii PECI_(gene).
GenomeRNAii 10455.
NextBioi 39633.
PROi O75521.
SOURCEi Search...

Gene expression databases

Bgeei O75521.
ExpressionAtlasi O75521. baseline and differential.
Genevestigatori O75521.

Family and domain databases

Gene3Di 1.20.80.10. 1 hit.
3.90.226.10. 1 hit.
InterProi IPR022408. Acyl-CoA-binding_prot_CS.
IPR000582. Acyl-CoA-binding_protein.
IPR029045. ClpP/crotonase-like_dom.
IPR001753. Crotonase_core_superfam.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
[Graphical view ]
Pfami PF00887. ACBP. 1 hit.
PF00378. ECH. 1 hit.
[Graphical view ]
PRINTSi PR00689. ACOABINDINGP.
SUPFAMi SSF47027. SSF47027. 1 hit.
SSF52096. SSF52096. 1 hit.
PROSITEi PS00880. ACB_1. 1 hit.
PS51228. ACB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of a novel human cDNA related to the diazepam binding inhibitor."
    Suk K., Kim Y.-H., Hwang D.-Y., Ihm S.-H., Yoo H.J., Lee M.-S.
    Biochim. Biophys. Acta 1454:126-131(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-344.
    Tissue: Pancreatic islet.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  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 2).
    Tissue: Placenta.
  4. "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].
  5. "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).
    Tissue: Bone marrow, Skin and Uterus.
  6. "Characterization of PECI, a novel monofunctional D3,D2-enoyl-CoA isomerase of mammalian peroxisomes."
    Geisbrecht B.V., Zhang D., Schulz H., Gould S.J.
    J. Biol. Chem. 274:21797-21803(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), SUBCELLULAR LOCATION.
  7. "Large scale identification of human hepatocellular carcinoma-associated antigens by autoantibodies."
    Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., Chen W.-F.
    J. Immunol. 169:1102-1109(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-394 (ISOFORM 1), VARIANT VAL-344.
    Tissue: Hepatoma.
  8. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  9. "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing."
    Simpson J.C., Wellenreuther R., Poustka A., Pepperkok R., Wiemann S.
    EMBO Rep. 1:287-292(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "Diazepam-binding inhibitor-related protein 1: a candidate autoantigen in acquired aplastic anemia patients harboring a minor population of paroxysmal nocturnal hemoglobinuria-type cells."
    Feng X., Chuhjo T., Sugimori C., Kotani T., Lu X., Takami A., Takamatsu H., Yamazaki H., Nakao S.
    Blood 104:2425-2431(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-92, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of RSGI RUH-045, a human acyl-CoA binding protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 36-133.
  14. "The crystal structure of human peroxisomal delta3, delta2 enoyl-CoA isomerase (pECI)."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 138-394.

Entry informationi

Entry nameiECI2_HUMAN
AccessioniPrimary (citable) accession number: O75521
Secondary accession number(s): Q5JYK5
, Q5JYK7, Q7L124, Q8N0X0, Q9BUE9, Q9H0T9, Q9NQH1, Q9NYH7, Q9UN55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: September 1, 2009
Last modified: October 29, 2014
This is version 151 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

Caution

It is uncertain whether Met-1 or Met-3 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, 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

External Data

Dasty 3