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Protein

Diphthine methyl ester synthase

Gene

DPH5

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

Functioni

S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.By similarity1 Publication

Catalytic activityi

4 S-adenosyl-L-methionine + 2-((3S)-3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] = 4 S-adenosyl-L-homocysteine + diphthine methyl ester-[translation elongation factor 2].By similarity

Pathway: peptidyl-diphthamide biosynthesis

This protein is involved in the pathway peptidyl-diphthamide biosynthesis, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway peptidyl-diphthamide biosynthesis and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei84 – 841S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei87 – 871S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei163 – 1631S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei225 – 2251S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei250 – 2501S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

  • diphthine synthase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_268628. Synthesis of diphthamide-EEF2.
UniPathwayiUPA00559.

Names & Taxonomyi

Protein namesi
Recommended name:
Diphthine methyl ester synthase (EC:2.1.1.314)
Alternative name(s):
Diphthamide biosynthesis methyltransferase
Gene namesi
Name:DPH5
ORF Names:AD-018, CGI-30, HSPC143, NPD015
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24270. DPH5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671956.

Polymorphism and mutation databases

BioMutaiDPH5.
DMDMi46397414.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Diphthine methyl ester synthasePRO_0000156133Add
BLAST

Proteomic databases

MaxQBiQ9H2P9.
PaxDbiQ9H2P9.
PRIDEiQ9H2P9.

PTM databases

PhosphoSiteiQ9H2P9.

Expressioni

Gene expression databases

BgeeiQ9H2P9.
CleanExiHS_DPH5.
ExpressionAtlasiQ9H2P9. baseline and differential.
GenevisibleiQ9H2P9. HS.

Organism-specific databases

HPAiHPA046439.

Interactioni

Protein-protein interaction databases

BioGridi119637. 4 interactions.
STRINGi9606.ENSP00000359127.

Structurei

3D structure databases

ProteinModelPortaliQ9H2P9.
SMRiQ9H2P9. Positions 1-270.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni112 – 1132S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the diphthine synthase family.Curated

Phylogenomic databases

eggNOGiCOG1798.
GeneTreeiENSGT00390000010568.
HOGENOMiHOG000205302.
HOVERGENiHBG044879.
InParanoidiQ9H2P9.
KOiK00586.
OMAiTLQQMCT.
OrthoDBiEOG7Q2N64.
PhylomeDBiQ9H2P9.
TreeFamiTF105603.

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPiMF_01084. Diphthine_synth.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036432. Diphthine_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR00522. dph5. 1 hit.

Sequences (6)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9H2P9-1) [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
MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG
60 70 80 90 100
RKLVVADREE VEQEADNILK DADISDVAFL VVGDPFGATT HSDLVLRATK
110 120 130 140 150
LGIPYRVIHN ASIMNAVGCC GLQLYKFGET VSIVFWTDTW RPESFFDKVK
160 170 180 190 200
KNRQNGMHTL CLLDIKVKEQ SLENLIKGRK IYEPPRYMSV NQAAQQLLEI
210 220 230 240 250
VQNQRIRGEE PAVTEETLCV GLARVGADDQ KIAAGTLRQM CTVDLGEPLH
260 270 280
SLIITGGSIH PMEMEMLSLF SIPENSSESQ SINGL
Length:285
Mass (Da):31,651
Last modified:October 10, 2003 - v2
Checksum:i1348631C25BC624E
GO
Isoform 2 (identifier: Q9H2P9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-137: PFGATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWT → HL

Note: No experimental confirmation available.
Show »
Length:234
Mass (Da):26,122
Checksum:iCAA1ABE0A11AF714
GO
Isoform 3 (identifier: Q9H2P9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     88-143: ATTHSDLVLRATKLGIPYRVIHNASIMNAVGCCGLQLYKFGETVSIVFWTDTWRPE → HLETR

Note: No experimental confirmation available.
Show »
Length:234
Mass (Da):26,025
Checksum:i86A9E6761145DFBA
GO
Isoform 4 (identifier: Q9H2P9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-141: VGCCGLQLYKFGETVSIVFWTDTWR → EAAGGYRYISLERQVLLVFGQTLGG

Note: No experimental confirmation available.
Show »
Length:285
Mass (Da):31,440
Checksum:i2784D835EB96EFC2
GO
Isoform 5 (identifier: Q9H2P9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-137: VFWT → MLISVMLHSLWLVIHL

Note: No experimental confirmation available.
Show »
Length:297
Mass (Da):33,005
Checksum:iE0D27EEEF0B9849D
GO
Isoform 6 (identifier: Q9H2P9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     212-212: Missing.

Note: No experimental confirmation available.
Show »
Length:284
Mass (Da):31,580
Checksum:i862A9762E32AA574
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071V → G in AAG44563 (Ref. 4) Curated
Sequence conflicti285 – 2851L → FEHRYFHCLM in AAF67485 (PubMed:10931946).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 13753PFGAT…IVFWT → HL in isoform 2. 1 PublicationVSP_008508Add
BLAST
Alternative sequencei88 – 14356ATTHS…TWRPE → HLETR in isoform 3. 1 PublicationVSP_008509Add
BLAST
Alternative sequencei117 – 14125VGCCG…TDTWR → EAAGGYRYISLERQVLLVFG QTLGG in isoform 4. 1 PublicationVSP_008510Add
BLAST
Alternative sequencei134 – 1374VFWT → MLISVMLHSLWLVIHL in isoform 5. 1 PublicationVSP_008511
Alternative sequencei212 – 2121Missing in isoform 6. 1 PublicationVSP_043444

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132964 mRNA. Translation: AAD27739.1.
AF157319 mRNA. Translation: AAF67485.1.
AF161492 mRNA. Translation: AAF29107.1.
AF248965 mRNA. Translation: AAG44563.1.
AK289351 mRNA. Translation: BAF82040.1.
AC093157 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW72933.1.
CH471097 Genomic DNA. Translation: EAW72937.1.
CH471097 Genomic DNA. Translation: EAW72938.1.
CH471097 Genomic DNA. Translation: EAW72940.1.
BC053857 mRNA. Translation: AAH53857.1.
CCDSiCCDS41358.1. [Q9H2P9-1]
CCDS41359.1. [Q9H2P9-6]
RefSeqiNP_001070862.1. NM_001077394.1. [Q9H2P9-1]
NP_001070863.1. NM_001077395.1. [Q9H2P9-6]
NP_057042.2. NM_015958.2. [Q9H2P9-1]
UniGeneiHs.440776.

Genome annotation databases

EnsembliENST00000342173; ENSP00000339630; ENSG00000117543. [Q9H2P9-6]
ENST00000370109; ENSP00000359127; ENSG00000117543. [Q9H2P9-1]
ENST00000488176; ENSP00000418282; ENSG00000117543. [Q9H2P9-1]
GeneIDi51611.
KEGGihsa:51611.
UCSCiuc001dtr.2. human. [Q9H2P9-6]
uc001dts.2. human. [Q9H2P9-1]
uc001dty.2. human. [Q9H2P9-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF132964 mRNA. Translation: AAD27739.1.
AF157319 mRNA. Translation: AAF67485.1.
AF161492 mRNA. Translation: AAF29107.1.
AF248965 mRNA. Translation: AAG44563.1.
AK289351 mRNA. Translation: BAF82040.1.
AC093157 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW72933.1.
CH471097 Genomic DNA. Translation: EAW72937.1.
CH471097 Genomic DNA. Translation: EAW72938.1.
CH471097 Genomic DNA. Translation: EAW72940.1.
BC053857 mRNA. Translation: AAH53857.1.
CCDSiCCDS41358.1. [Q9H2P9-1]
CCDS41359.1. [Q9H2P9-6]
RefSeqiNP_001070862.1. NM_001077394.1. [Q9H2P9-1]
NP_001070863.1. NM_001077395.1. [Q9H2P9-6]
NP_057042.2. NM_015958.2. [Q9H2P9-1]
UniGeneiHs.440776.

3D structure databases

ProteinModelPortaliQ9H2P9.
SMRiQ9H2P9. Positions 1-270.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119637. 4 interactions.
STRINGi9606.ENSP00000359127.

PTM databases

PhosphoSiteiQ9H2P9.

Polymorphism and mutation databases

BioMutaiDPH5.
DMDMi46397414.

Proteomic databases

MaxQBiQ9H2P9.
PaxDbiQ9H2P9.
PRIDEiQ9H2P9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342173; ENSP00000339630; ENSG00000117543. [Q9H2P9-6]
ENST00000370109; ENSP00000359127; ENSG00000117543. [Q9H2P9-1]
ENST00000488176; ENSP00000418282; ENSG00000117543. [Q9H2P9-1]
GeneIDi51611.
KEGGihsa:51611.
UCSCiuc001dtr.2. human. [Q9H2P9-6]
uc001dts.2. human. [Q9H2P9-1]
uc001dty.2. human. [Q9H2P9-5]

Organism-specific databases

CTDi51611.
GeneCardsiGC01M101455.
H-InvDBHIX0023161.
HGNCiHGNC:24270. DPH5.
HPAiHPA046439.
MIMi611075. gene.
neXtProtiNX_Q9H2P9.
PharmGKBiPA142671956.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1798.
GeneTreeiENSGT00390000010568.
HOGENOMiHOG000205302.
HOVERGENiHBG044879.
InParanoidiQ9H2P9.
KOiK00586.
OMAiTLQQMCT.
OrthoDBiEOG7Q2N64.
PhylomeDBiQ9H2P9.
TreeFamiTF105603.

Enzyme and pathway databases

UniPathwayiUPA00559.
ReactomeiREACT_268628. Synthesis of diphthamide-EEF2.

Miscellaneous databases

ChiTaRSiDPH5. human.
GeneWikiiDPH5.
GenomeRNAii51611.
NextBioi55510.
PROiQ9H2P9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2P9.
CleanExiHS_DPH5.
ExpressionAtlasiQ9H2P9. baseline and differential.
GenevisibleiQ9H2P9. HS.

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPiMF_01084. Diphthine_synth.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFiPIRSF036432. Diphthine_synth. 1 hit.
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR00522. dph5. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Adrenal gland.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Umbilical cord blood.
  4. Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Pituitary.
  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 6).
  6. "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].
  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] (ISOFORM 1).
    Tissue: Eye.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A modified form of diphthamide causes immunotoxin resistance in a lymphoma cell line with a deletion of the WDR85 gene."
    Wei H., Bera T.K., Wayne A.S., Xiang L., Colantonio S., Chertov O., Pastan I.
    J. Biol. Chem. 288:12305-12312(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.

Entry informationi

Entry nameiDPH5_HUMAN
AccessioniPrimary (citable) accession number: Q9H2P9
Secondary accession number(s): A8JZY6
, D3DT62, Q9P017, Q9P0I4, Q9Y319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 10, 2003
Last modified: June 24, 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 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. 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.