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Protein

Very long-chain acyl-CoA synthetase

Gene

SLC27A2

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

Functioni

Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity).By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication
ATP + a very-long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 23312AMPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: UniProtKB
  3. fatty acid transporter activity Source: Ensembl
  4. long-chain fatty acid-CoA ligase activity Source: UniProtKB
  5. phytanate-CoA ligase activity Source: UniProtKB
  6. pristanate-CoA ligase activity Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. bile acid biosynthetic process Source: UniProtKB
  2. bile acid metabolic process Source: Reactome
  3. cellular lipid metabolic process Source: Reactome
  4. fatty acid alpha-oxidation Source: UniProtKB
  5. fatty acid beta-oxidation Source: UniProtKB
  6. long-chain fatty acid import Source: UniProtKB
  7. long-chain fatty acid metabolic process Source: UniProtKB
  8. methyl-branched fatty acid metabolic process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
  10. very long-chain fatty acid catabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06695-MONOMER.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_17003. Alpha-oxidation of phytanate.

Protein family/group databases

TCDBi4.C.1.1.5. the proposed fatty acid transporter (fat) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain acyl-CoA synthetase (EC:6.2.1.-)
Short name:
VLACS
Short name:
VLCS
Alternative name(s):
Fatty acid transport protein 2
Short name:
FATP-2
Fatty-acid-coenzyme A ligase, very long-chain 1
Long-chain-fatty-acid--CoA ligase (EC:6.2.1.3)
Solute carrier family 27 member 2
THCA-CoA ligase
Very long-chain-fatty-acid-CoA ligase
Gene namesi
Name:SLC27A2
Synonyms:ACSVL1, FACVL1, FATP2, VLACS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:10996. SLC27A2.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Multi-pass membrane protein
Note: Peripheral membrane associated with the lumenal side of peroxisomes.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Lumenal1 Publication
Transmembranei5 – 2723HelicalSequence AnalysisAdd
BLAST
Topological domaini28 – 10679CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence AnalysisAdd
BLAST
Topological domaini128 – 261134LumenalSequence AnalysisAdd
BLAST
Transmembranei262 – 28221HelicalSequence AnalysisAdd
BLAST
Topological domaini283 – 620338CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
  2. endoplasmic reticulum membrane Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. integral component of peroxisomal membrane Source: UniProtKB
  6. mitochondrion Source: Ensembl
  7. peroxisomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27971.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Very long-chain acyl-CoA synthetasePRO_0000193204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-acetyllysineBy similarity
Modified residuei577 – 5771Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14975.
PaxDbiO14975.
PRIDEiO14975.

PTM databases

PhosphoSiteiO14975.

Expressioni

Tissue specificityi

Expressed in liver, kidney, placenta and pancreas.1 Publication

Gene expression databases

BgeeiO14975.
CleanExiHS_SLC27A2.
ExpressionAtlasiO14975. baseline and differential.
GenevestigatoriO14975.

Organism-specific databases

HPAiHPA026089.

Interactioni

Protein-protein interaction databases

BioGridi116194. 19 interactions.
IntActiO14975. 2 interactions.
MINTiMINT-2998454.
STRINGi9606.ENSP00000267842.

Structurei

3D structure databases

SMRiO14975. Positions 60-555.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00550000074420.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiO14975.
KOiK08746.
OMAiITHQRIW.
OrthoDBiEOG7W6WKB.
PhylomeDBiO14975.
TreeFamiTF313430.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030305. FATP2.
[Graphical view]
PANTHERiPTHR24096:SF127. PTHR24096:SF127. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 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: O14975-1) [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
MLSAIYTVLA GLLFLPLLVN LCCPYFFQDI GYFLKVAAVG RRVRSYGKRR
60 70 80 90 100
PARTILRAFL EKARQTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG
110 120 130 140 150
LRQGDCVALL MGNEPAYVWL WLGLVKLGCA MACLNYNIRA KSLLHCFQCC
160 170 180 190 200
GAKVLLVSPE LQAAVEEILP SLKKDDVSIY YVSRTSNTDG IDSFLDKVDE
210 220 230 240 250
VSTEPIPESW RSEVTFSTPA LYIYTSGTTG LPKAAMITHQ RIWYGTGLTF
260 270 280 290 300
VSGLKADDVI YITLPFYHSA ALLIGIHGCI VAGATLALRT KFSASQFWDD
310 320 330 340 350
CRKYNVTVIQ YIGELLRYLC NSPQKPNDRD HKVRLALGNG LRGDVWRQFV
360 370 380 390 400
KRFGDICIYE FYAATEGNIG FMNYARKVGA VGRVNYLQKK IITYDLIKYD
410 420 430 440 450
VEKDEPVRDE NGYCVRVPKG EVGLLVCKIT QLTPFNGYAG AKAQTEKKKL
460 470 480 490 500
RDVFKKGDLY FNSGDLLMVD HENFIYFHDR VGDTFRWKGE NVATTEVADT
510 520 530 540 550
VGLVDFVQEV NVYGVHVPDH EGRIGMASIK MKENHEFDGK KLFQHIADYL
560 570 580 590 600
PSYARPRFLR IQDTIEITGT FKHRKMTLVE EGFNPAVIKD ALYFLDDTAK
610 620
MYVPMTEDIY NAISAKTLKL
Length:620
Mass (Da):70,312
Last modified:October 5, 2010 - v2
Checksum:i752E2FFBB2E47C26
GO
Isoform 2 (identifier: O14975-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-282: Missing.

Note: No experimental confirmation available.

Show »
Length:567
Mass (Da):64,616
Checksum:iFF3A2B0FD68177B0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti48 – 481K → Q.4 Publications
Corresponds to variant rs1648348 [ dbSNP | Ensembl ].
VAR_046533

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei230 – 28253Missing in isoform 2. 1 PublicationVSP_042726Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88308 mRNA. Translation: BAA23644.1.
AF096290 mRNA. Translation: AAC64973.1.
AK223145 mRNA. Translation: BAD96865.1.
AK290262 mRNA. Translation: BAF82951.1.
AC009753 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77386.1.
BC057770 mRNA. Translation: AAH57770.1.
CCDSiCCDS10133.1. [O14975-1]
CCDS53943.1. [O14975-2]
RefSeqiNP_001153101.1. NM_001159629.1. [O14975-2]
NP_003636.2. NM_003645.3. [O14975-1]
UniGeneiHs.11729.

Genome annotation databases

EnsembliENST00000267842; ENSP00000267842; ENSG00000140284. [O14975-1]
ENST00000380902; ENSP00000370289; ENSG00000140284. [O14975-2]
GeneIDi11001.
KEGGihsa:11001.
UCSCiuc001zxw.3. human. [O14975-1]
uc010bes.3. human. [O14975-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88308 mRNA. Translation: BAA23644.1.
AF096290 mRNA. Translation: AAC64973.1.
AK223145 mRNA. Translation: BAD96865.1.
AK290262 mRNA. Translation: BAF82951.1.
AC009753 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77386.1.
BC057770 mRNA. Translation: AAH57770.1.
CCDSiCCDS10133.1. [O14975-1]
CCDS53943.1. [O14975-2]
RefSeqiNP_001153101.1. NM_001159629.1. [O14975-2]
NP_003636.2. NM_003645.3. [O14975-1]
UniGeneiHs.11729.

3D structure databases

SMRiO14975. Positions 60-555.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116194. 19 interactions.
IntActiO14975. 2 interactions.
MINTiMINT-2998454.
STRINGi9606.ENSP00000267842.

Chemistry

ChEMBLiCHEMBL4326.

Protein family/group databases

TCDBi4.C.1.1.5. the proposed fatty acid transporter (fat) family.

PTM databases

PhosphoSiteiO14975.

Proteomic databases

MaxQBiO14975.
PaxDbiO14975.
PRIDEiO14975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267842; ENSP00000267842; ENSG00000140284. [O14975-1]
ENST00000380902; ENSP00000370289; ENSG00000140284. [O14975-2]
GeneIDi11001.
KEGGihsa:11001.
UCSCiuc001zxw.3. human. [O14975-1]
uc010bes.3. human. [O14975-2]

Organism-specific databases

CTDi11001.
GeneCardsiGC15P050474.
HGNCiHGNC:10996. SLC27A2.
HPAiHPA026089.
MIMi603247. gene.
neXtProtiNX_O14975.
PharmGKBiPA27971.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00550000074420.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiO14975.
KOiK08746.
OMAiITHQRIW.
OrthoDBiEOG7W6WKB.
PhylomeDBiO14975.
TreeFamiTF313430.

Enzyme and pathway databases

BioCyciMetaCyc:HS06695-MONOMER.
ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
REACT_17003. Alpha-oxidation of phytanate.

Miscellaneous databases

ChiTaRSiSLC27A2. human.
GeneWikiiSLC27A2.
GenomeRNAii11001.
NextBioi41795.
PROiO14975.
SOURCEiSearch...

Gene expression databases

BgeeiO14975.
CleanExiHS_SLC27A2.
ExpressionAtlasiO14975. baseline and differential.
GenevestigatoriO14975.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030305. FATP2.
[Graphical view]
PANTHERiPTHR24096:SF127. PTHR24096:SF127. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a possible human homolog of the rat very-long-chain acyl-CoA synthetase cDNA and its chromosomal localization."
    Uchiyama A., Aoyama T., Kamijo K., Wakui K., Fukushima Y., Shimozawa N., Suzuki Y., Kondo N., Orii T., Hashimoto T.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-48.
    Tissue: Liver.
  2. "Human very-long-chain acyl-CoA synthetase: cloning, topography, and relevance to branched-chain fatty acid metabolism."
    Steinberg S.J., Wang S.J., Kim D.G., Mihalik S.J., Watkins P.A.
    Biochem. Biophys. Res. Commun. 257:615-621(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT GLN-48.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-48.
    Tissue: Colon.
  4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-48.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  8. "Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling."
    Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.
    J. Biol. Chem. 277:24771-24779(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiS27A2_HUMAN
AccessioniPrimary (citable) accession number: O14975
Secondary accession number(s): A8K2J7, Q53FY6, Q6PF09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 5, 2010
Last modified: April 1, 2015
This is version 128 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 15
    Human chromosome 15: 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. 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.