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Protein

Transcription elongation factor B polypeptide 3

Gene

TCEB3

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

Functioni

SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription elongation factor B polypeptide 3
Alternative name(s):
Elongin 110 kDa subunit
Elongin-A
Short name:
EloA
RNA polymerase II transcription factor SIII subunit A1
SIII p110
Gene namesi
Name:TCEB3
ORF Names:MSTP059
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11620. TCEB3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36379.

Polymorphism and mutation databases

BioMutaiTCEB3.
DMDMi294862430.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 798798Transcription elongation factor B polypeptide 3PRO_0000086960Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei410 – 4101Phosphoserine2 Publications
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei420 – 4201Phosphothreonine1 Publication
Modified residuei460 – 4601N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ14241.
PaxDbiQ14241.
PeptideAtlasiQ14241.
PRIDEiQ14241.

PTM databases

PhosphoSiteiQ14241.

Expressioni

Gene expression databases

BgeeiQ14241.
ExpressionAtlasiQ14241. baseline and differential.
GenevisibleiQ14241. HS.

Organism-specific databases

HPAiHPA005910.
HPA052418.

Interactioni

Subunit structurei

Heterotrimer of an A (A1, A2 or A3), B and C subunit. The C subunit mediates the binding of the elongin BC complex to subunit A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP57L1Q8IYX8-23EBI-742350,EBI-10181988
CEP70Q8NHQ13EBI-742350,EBI-739624
FAM9BQ8IZU03EBI-742350,EBI-10175124
FLJ13057Q53SE73EBI-742350,EBI-10172181
HOMEZQ8IX15-33EBI-742350,EBI-10172004
JAKMIP2Q96AA83EBI-742350,EBI-752007
KRT40Q6A1623EBI-742350,EBI-10171697
MDFIQ997503EBI-742350,EBI-724076
MID2Q9UJV3-23EBI-742350,EBI-10172526
PLK4O004443EBI-742350,EBI-746202
SPERTQ8NA613EBI-742350,EBI-741724
TRIM54Q9BYV23EBI-742350,EBI-2130429

Protein-protein interaction databases

BioGridi112786. 45 interactions.
IntActiQ14241. 16 interactions.
MINTiMINT-1462212.
STRINGi9606.ENSP00000395574.

Structurei

Secondary structure

1
798
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi607 – 6093Combined sources
Helixi612 – 6198Combined sources
Helixi623 – 6253Combined sources
Helixi630 – 6367Combined sources
Beta strandi648 – 6503Combined sources
Helixi652 – 67120Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HFXX-ray2.54A/B/C/D597-682[»]
ProteinModelPortaliQ14241.
SMRiQ14241. Positions 600-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 10576TFIIS N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini592 – 63645F-boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni548 – 707160Activation domainBy similarityAdd
BLAST
Regioni576 – 58510Interacting with Elongin BC complex

Domaini

The elongin BC complex binding domain is also known as BC-box with the consensus [APST]-L-x(3)-C-x(3)-[AILV].

Sequence similaritiesi

Contains 1 F-box domain.PROSITE-ProRule annotation
Contains 1 TFIIS N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG114994.
GeneTreeiENSGT00390000002428.
HOGENOMiHOG000059565.
HOVERGENiHBG051467.
InParanoidiQ14241.
KOiK15076.
OMAiWKVHCHR.
OrthoDBiEOG7P2XSR.
PhylomeDBiQ14241.
TreeFamiTF317259.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR010684. RNA_pol_II_trans_fac_SIII_A.
IPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
[Graphical view]
PfamiPF06881. Elongin_A. 1 hit.
PF08711. Med26. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS51319. TFIIS_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14241-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHGGRSCGPR TRREPSSGEE AAPVTAMAAE SALQVVEKLQ ARLAANPDPK
60 70 80 90 100
KLLKYLKKLS TLPITVDILA ETGVGKTVNS LRKHEHVGSF ARDLVAQWKK
110 120 130 140 150
LVPVERNAEP DEQDFEKSNS RKRPRDALQK EEEMEGDYQE TWKATGSRSY
160 170 180 190 200
SPDHRQKKHR KLSELERPHK VSHGHERRDE RKRCHRMSPT YSSDPESSDY
210 220 230 240 250
GHVQSPPSCT SPHQMYVDHY RSLEEDQEPI VSHQKPGKGH SNAFQDRLGA
260 270 280 290 300
SQERHLGEPH GKGVVSQNKE HKSSHKDKRP VDAKSDEKAS VVSREKSHKA
310 320 330 340 350
LSKEENRRPP SGDNAREKPP SSGVKKEKDR EGSSLKKKCL PPSEAASDNH
360 370 380 390 400
LKKPKHRDPE KAKLDKSKQG LDSFDTGKGA GDLLPKVKEK GSNNLKTPEG
410 420 430 440 450
KVKTNLDRKS LGSLPKVEET DMEDEFEQPT MSFESYLSYD QPRKKKKKIV
460 470 480 490 500
KTSATALGDK GLKKNDSKST GKNLDSVQKL PKVNKTKSEK PAGADLAKLR
510 520 530 540 550
KVPDVLPVLP DLPLPAIQAN YRPLPSLELI SSFQPKRKAF SSPQEEEEAG
560 570 580 590 600
FTGRRMNSKM QVYSGSKCAY LPKMMTLHQQ CIRVLKNNID SIFEVGGVPY
610 620 630 640 650
SVLEPVLERC TPDQLYRIEE YNHVLIEETD QLWKVHCHRD FKEERPEEYE
660 670 680 690 700
SWREMYLRLQ DAREQRLRVL TKNIQFAHAN KPKGRQAKMA FVNSVAKPPR
710 720 730 740 750
DVRRRQEKFG TGGAAVPEKI KIKPAPYPMG SSHASASSIS FNPSPEEPAY
760 770 780 790
DGPSTSSAHL APVVSSTVSY DPRKPTVKKI APMMAKTIKA FKNRFSRR
Length:798
Mass (Da):89,909
Last modified:April 20, 2010 - v2
Checksum:i2C8FD8710E27EE46
GO

Sequence cautioni

The sequence AAA75492.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH02883.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO15305.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG35905.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAB40157.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAW95070.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451T → M.
Corresponds to variant rs2235541 [ dbSNP | Ensembl ].
VAR_020104
Natural varianti324 – 3241V → I.
Corresponds to variant rs520713 [ dbSNP | Ensembl ].
VAR_033850
Natural varianti516 – 5161A → V.
Corresponds to variant rs550252 [ dbSNP | Ensembl ].
VAR_033851

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313079 mRNA. Translation: BAG35905.1. Different initiation.
DA333869 mRNA. No translation available.
AL031295 Genomic DNA. Translation: CAB40157.1. Different initiation.
CH471134 Genomic DNA. Translation: EAW95070.1. Different initiation.
L47345 mRNA. Translation: AAA75492.1. Different initiation.
BC002883 mRNA. Translation: AAH02883.1. Different initiation.
AF116729 mRNA. Translation: AAO15305.1. Different initiation.
CCDSiCCDS239.2.
PIRiJC4636.
RefSeqiNP_003189.2. NM_003198.2.
UniGeneiHs.15535.

Genome annotation databases

EnsembliENST00000418390; ENSP00000395574; ENSG00000011007.
ENST00000613537; ENSP00000484196; ENSG00000011007.
GeneIDi6924.
KEGGihsa:6924.
UCSCiuc001bho.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313079 mRNA. Translation: BAG35905.1. Different initiation.
DA333869 mRNA. No translation available.
AL031295 Genomic DNA. Translation: CAB40157.1. Different initiation.
CH471134 Genomic DNA. Translation: EAW95070.1. Different initiation.
L47345 mRNA. Translation: AAA75492.1. Different initiation.
BC002883 mRNA. Translation: AAH02883.1. Different initiation.
AF116729 mRNA. Translation: AAO15305.1. Different initiation.
CCDSiCCDS239.2.
PIRiJC4636.
RefSeqiNP_003189.2. NM_003198.2.
UniGeneiHs.15535.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4HFXX-ray2.54A/B/C/D597-682[»]
ProteinModelPortaliQ14241.
SMRiQ14241. Positions 600-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112786. 45 interactions.
IntActiQ14241. 16 interactions.
MINTiMINT-1462212.
STRINGi9606.ENSP00000395574.

PTM databases

PhosphoSiteiQ14241.

Polymorphism and mutation databases

BioMutaiTCEB3.
DMDMi294862430.

Proteomic databases

MaxQBiQ14241.
PaxDbiQ14241.
PeptideAtlasiQ14241.
PRIDEiQ14241.

Protocols and materials databases

DNASUi6924.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418390; ENSP00000395574; ENSG00000011007.
ENST00000613537; ENSP00000484196; ENSG00000011007.
GeneIDi6924.
KEGGihsa:6924.
UCSCiuc001bho.3. human.

Organism-specific databases

CTDi6924.
GeneCardsiGC01P024069.
H-InvDBHIX0000251.
HGNCiHGNC:11620. TCEB3.
HPAiHPA005910.
HPA052418.
MIMi600786. gene.
neXtProtiNX_Q14241.
PharmGKBiPA36379.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG114994.
GeneTreeiENSGT00390000002428.
HOGENOMiHOG000059565.
HOVERGENiHBG051467.
InParanoidiQ14241.
KOiK15076.
OMAiWKVHCHR.
OrthoDBiEOG7P2XSR.
PhylomeDBiQ14241.
TreeFamiTF317259.

Enzyme and pathway databases

ReactomeiREACT_1845. Formation of RNA Pol II elongation complex.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6244. Pausing and recovery of HIV elongation.
REACT_6259. HIV elongation arrest and recovery.
REACT_6344. Tat-mediated HIV elongation arrest and recovery.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.

Miscellaneous databases

GeneWikiiTCEB3.
GenomeRNAii6924.
NextBioi27089.
PROiQ14241.
SOURCEiSearch...

Gene expression databases

BgeeiQ14241.
ExpressionAtlasiQ14241. baseline and differential.
GenevisibleiQ14241. HS.

Family and domain databases

Gene3Di1.20.930.10. 1 hit.
InterProiIPR001810. F-box_dom.
IPR010684. RNA_pol_II_trans_fac_SIII_A.
IPR003617. TFIIS/CRSP70_N_sub.
IPR017923. TFIIS_N.
[Graphical view]
PfamiPF06881. Elongin_A. 1 hit.
PF08711. Med26. 1 hit.
[Graphical view]
SMARTiSM00509. TFS2N. 1 hit.
[Graphical view]
SUPFAMiSSF47676. SSF47676. 1 hit.
PROSITEiPS50181. FBOX. 1 hit.
PS51319. TFIIS_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "A human cDNA encoding the 110-kDa A subunit of RNA polymerase II transcription factor elongin."
    Aso T., Haque D., Fukudome K., Brower C.S., Conaway J.W., Conaway R.C.
    Gene 168:277-278(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-798.
    Tissue: Umbilical vein.
  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] OF 20-798.
    Tissue: Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-798.
    Tissue: Heart.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND THR-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELOA1_HUMAN
AccessioniPrimary (citable) accession number: Q14241
Secondary accession number(s): B2R7Q8, Q8IXH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: April 20, 2010
Last modified: June 24, 2015
This is version 142 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

Caution

It is uncertain whether Met-1 or Met-27 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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.