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Protein

Elongation of very long chain fatty acids protein 1

Gene

ELOVL1

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

Functioni

Catalyzes the first and rate-limiting reaction of the four that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. Indirectly inhibits RPE65 via production of VLCFAs.UniRule annotation2 Publications

Catalytic activityi

A very-long-chain acyl-CoA + malonyl-CoA = CoA + a very-long-chain 3-oxoacyl-CoA + CO2.UniRule annotation2 Publications

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.UniRule annotation2 Publications
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • fatty acid elongase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-HSA-2046105. Linoleic acid (LA) metabolism.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-75876. Synthesis of very long-chain fatty acyl-CoAs.
UniPathwayiUPA00094.

Chemistry

SwissLipidsiSLP:000000249.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation of very long chain fatty acids protein 1UniRule annotationCurated (EC:2.3.1.199UniRule annotation2 Publications)
Alternative name(s):
3-keto acyl-CoA synthase ELOVL1UniRule annotation
ELOVL fatty acid elongase 1UniRule annotation
Short name:
ELOVL FA elongase 1UniRule annotation
Very long chain 3-ketoacyl-CoA synthase 1UniRule annotation
Very long chain 3-oxoacyl-CoA synthase 1UniRule annotation
Gene namesi
Name:ELOVL1UniRule annotation
Synonyms:SSC1
ORF Names:CGI-88
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:14418. ELOVL1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei23 – 4321HelicalUniRule annotationAdd
BLAST
Transmembranei61 – 8121HelicalUniRule annotationAdd
BLAST
Transmembranei110 – 13021HelicalUniRule annotationAdd
BLAST
Transmembranei137 – 15418HelicalUniRule annotationAdd
BLAST
Transmembranei176 – 19621HelicalUniRule annotationAdd
BLAST
Transmembranei201 – 22121HelicalUniRule annotationAdd
BLAST
Transmembranei231 – 25121HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27760.

Chemistry

ChEMBLiCHEMBL6001.

Polymorphism and mutation databases

BioMutaiELOVL1.
DMDMi20137931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Elongation of very long chain fatty acids protein 1PRO_0000207536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9BW60.
MaxQBiQ9BW60.
PaxDbiQ9BW60.
PRIDEiQ9BW60.
TopDownProteomicsiQ9BW60-1. [Q9BW60-1]

PTM databases

iPTMnetiQ9BW60.
PhosphoSiteiQ9BW60.
SwissPalmiQ9BW60.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9BW60.
CleanExiHS_ELOVL1.
GenevisibleiQ9BW60. HS.

Organism-specific databases

HPAiCAB033426.
HPA056557.

Interactioni

Subunit structurei

Interacts with LASS2, TECR and HSD17B12.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi122312. 11 interactions.
IntActiQ9BW60. 3 interactions.
STRINGi9606.ENSP00000361536.

Chemistry

BindingDBiQ9BW60.

Structurei

3D structure databases

ProteinModelPortaliQ9BW60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi275 – 2795Di-lysine motifUniRule annotation

Domaini

The C-terminal di-lysine motif may confer endoplasmic reticulum localization.UniRule annotation

Sequence similaritiesi

Belongs to the ELO family. ELOVL1 subfamily.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9BW60.
KOiK10247.
OMAiLYQEMMK.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9BW60.
TreeFamiTF323454.

Family and domain databases

HAMAPiMF_03201. VLCF_elongase_1.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9BW60-1) [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
MEAVVNLYQE VMKHADPRIQ GYPLMGSPLL MTSILLTYVY FVLSLGPRIM
60 70 80 90 100
ANRKPFQLRG FMIVYNFSLV ALSLYIVYEF LMSGWLSTYT WRCDPVDYSN
110 120 130 140 150
SPEALRMVRV AWLFLFSKFI ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW
160 170 180 190 200
SWWWGVKIAP GGMGSFHAMI NSSVHVIMYL YYGLSAFGPV AQPYLWWKKH
210 220 230 240 250
MTAIQLIQFV LVSLHISQYY FMSSCNYQYP VIIHLIWMYG TIFFMLFSNF
260 270
WYHSYTKGKR LPRALQQNGA PGIAKVKAN
Length:279
Mass (Da):32,663
Last modified:June 1, 2001 - v1
Checksum:iB168EE4C7EAF92A6
GO
Isoform 2 (identifier: Q9BW60-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     80-106: Missing.

Show »
Length:252
Mass (Da):29,485
Checksum:i027A10BA1FC68054
GO

Sequence cautioni

The sequence AAD34083.1 differs from that shown. Reason: Frameshift at position 189. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681S → P in BAA91813 (PubMed:14702039).Curated
Sequence conflicti75 – 751Y → H in AAL71993 (Ref. 1) Curated
Sequence conflicti201 – 2011M → T in BAD96218 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei80 – 10627Missing in isoform 2. 1 PublicationVSP_045436Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336793 mRNA. Translation: AAL71993.1.
AF151846 mRNA. Translation: AAD34083.1. Frameshift.
AK001653 mRNA. Translation: BAA91813.1.
AK222498 mRNA. Translation: BAD96218.1.
AK298163 mRNA. Translation: BAG60436.1.
AL139289 Genomic DNA. Translation: CAB92758.1.
BC000618 mRNA. Translation: AAH00618.1.
CCDSiCCDS485.1. [Q9BW60-1]
CCDS57987.1. [Q9BW60-2]
RefSeqiNP_001243328.1. NM_001256399.1. [Q9BW60-1]
NP_001243330.1. NM_001256401.1. [Q9BW60-2]
NP_001243331.1. NM_001256402.1.
NP_073732.1. NM_022821.3. [Q9BW60-1]
UniGeneiHs.25597.

Genome annotation databases

EnsembliENST00000372458; ENSP00000361536; ENSG00000066322. [Q9BW60-1]
ENST00000413844; ENSP00000416024; ENSG00000066322. [Q9BW60-2]
ENST00000621943; ENSP00000477602; ENSG00000066322. [Q9BW60-1]
GeneIDi64834.
KEGGihsa:64834.
UCSCiuc001cjb.5. human. [Q9BW60-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF336793 mRNA. Translation: AAL71993.1.
AF151846 mRNA. Translation: AAD34083.1. Frameshift.
AK001653 mRNA. Translation: BAA91813.1.
AK222498 mRNA. Translation: BAD96218.1.
AK298163 mRNA. Translation: BAG60436.1.
AL139289 Genomic DNA. Translation: CAB92758.1.
BC000618 mRNA. Translation: AAH00618.1.
CCDSiCCDS485.1. [Q9BW60-1]
CCDS57987.1. [Q9BW60-2]
RefSeqiNP_001243328.1. NM_001256399.1. [Q9BW60-1]
NP_001243330.1. NM_001256401.1. [Q9BW60-2]
NP_001243331.1. NM_001256402.1.
NP_073732.1. NM_022821.3. [Q9BW60-1]
UniGeneiHs.25597.

3D structure databases

ProteinModelPortaliQ9BW60.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122312. 11 interactions.
IntActiQ9BW60. 3 interactions.
STRINGi9606.ENSP00000361536.

Chemistry

BindingDBiQ9BW60.
ChEMBLiCHEMBL6001.
SwissLipidsiSLP:000000249.

PTM databases

iPTMnetiQ9BW60.
PhosphoSiteiQ9BW60.
SwissPalmiQ9BW60.

Polymorphism and mutation databases

BioMutaiELOVL1.
DMDMi20137931.

Proteomic databases

EPDiQ9BW60.
MaxQBiQ9BW60.
PaxDbiQ9BW60.
PRIDEiQ9BW60.
TopDownProteomicsiQ9BW60-1. [Q9BW60-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372458; ENSP00000361536; ENSG00000066322. [Q9BW60-1]
ENST00000413844; ENSP00000416024; ENSG00000066322. [Q9BW60-2]
ENST00000621943; ENSP00000477602; ENSG00000066322. [Q9BW60-1]
GeneIDi64834.
KEGGihsa:64834.
UCSCiuc001cjb.5. human. [Q9BW60-1]

Organism-specific databases

CTDi64834.
GeneCardsiELOVL1.
H-InvDBHIX0000507.
HGNCiHGNC:14418. ELOVL1.
HPAiCAB033426.
HPA056557.
MIMi611813. gene.
neXtProtiNX_Q9BW60.
PharmGKBiPA27760.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3071. Eukaryota.
ENOG410XRWT. LUCA.
GeneTreeiENSGT00760000119122.
HOGENOMiHOG000038120.
HOVERGENiHBG051468.
InParanoidiQ9BW60.
KOiK10247.
OMAiLYQEMMK.
OrthoDBiEOG7Z3F4V.
PhylomeDBiQ9BW60.
TreeFamiTF323454.

Enzyme and pathway databases

UniPathwayiUPA00094.
ReactomeiR-HSA-2046105. Linoleic acid (LA) metabolism.
R-HSA-2046106. alpha-linolenic acid (ALA) metabolism.
R-HSA-75876. Synthesis of very long-chain fatty acyl-CoAs.

Miscellaneous databases

ChiTaRSiELOVL1. human.
GenomeRNAii64834.
NextBioi66916.
PROiQ9BW60.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BW60.
CleanExiHS_ELOVL1.
GenevisibleiQ9BW60. HS.

Family and domain databases

HAMAPiMF_03201. VLCF_elongase_1.
InterProiIPR030457. ELO_CS.
IPR002076. ELO_fam.
[Graphical view]
PANTHERiPTHR11157. PTHR11157. 1 hit.
PfamiPF01151. ELO. 1 hit.
[Graphical view]
PROSITEiPS01188. ELO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Description of the human SSC1/ELOVL1 gene. Relocation of the CDC20 gene to human chromosome 1 support a bi-directional transcription of the human SSC1/ELOVL1 and CDC20 genes."
    Asadi A., Jacobsson A.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Adipose tissue.
  4. "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].
  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] (ISOFORM 1).
    Tissue: Kidney.
  6. "Fatty acid elongases in mammals: their regulation and roles in metabolism."
    Jakobsson A., Westerberg R., Jacobsson A.
    Prog. Lipid Res. 45:237-249(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  7. "The role of ELOVL1 in very long-chain fatty acid homeostasis and X-linked adrenoleukodystrophy."
    Ofman R., Dijkstra I.M.E., van Roermund C.W.T., Burger N., Turkenburg M., van Cruchten A., van Engen C.E., Wanders R.J.A., Kemp S.
    EMBO Mol. Med. 2:90-97(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
  8. Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH LASS2; HSD17B12 AND TECR.
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiELOV1_HUMAN
AccessioniPrimary (citable) accession number: Q9BW60
Secondary accession number(s): B4DP24
, Q53HT2, Q5JUY3, Q8WXU3, Q9NVD9, Q9Y396
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 130 of the entry and version 1 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

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.