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P35610

- SOAT1_HUMAN

UniProt

P35610 - SOAT1_HUMAN

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Protein

Sterol O-acyltransferase 1

Gene

SOAT1

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

Functioni

Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase.

Catalytic activityi

Acyl-CoA + cholesterol = CoA + cholesterol ester.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei460 – 46011 Publication

GO - Molecular functioni

  1. cholesterol binding Source: BHF-UCL
  2. cholesterol O-acyltransferase activity Source: BHF-UCL
  3. fatty-acyl-CoA binding Source: BHF-UCL
  4. sterol O-acyltransferase activity Source: BHF-UCL

GO - Biological processi

  1. cholesterol efflux Source: BHF-UCL
  2. cholesterol esterification Source: BHF-UCL
  3. cholesterol homeostasis Source: BHF-UCL
  4. cholesterol metabolic process Source: BHF-UCL
  5. cholesterol storage Source: BHF-UCL
  6. macrophage derived foam cell differentiation Source: BHF-UCL
  7. positive regulation of amyloid precursor protein biosynthetic process Source: BHF-UCL
  8. very-low-density lipoprotein particle assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Enzyme and pathway databases

BRENDAi2.3.1.26. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Sterol O-acyltransferase 1 (EC:2.3.1.26)
Alternative name(s):
Acyl-coenzyme A:cholesterol acyltransferase 1
Short name:
ACAT-1
Cholesterol acyltransferase 1
Gene namesi
Name:SOAT1
Synonyms:ACACT, ACACT1, ACAT, ACAT1, SOAT, STAT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:11177. SOAT1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 140140CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei141 – 15919HelicalSequence AnalysisAdd
BLAST
Topological domaini160 – 18122LumenalSequence AnalysisAdd
BLAST
Transmembranei182 – 20120HelicalSequence AnalysisAdd
BLAST
Topological domaini202 – 22423CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei225 – 24319HelicalSequence AnalysisAdd
BLAST
Topological domaini244 – 2463LumenalSequence Analysis
Transmembranei247 – 26418HelicalSequence AnalysisAdd
BLAST
Topological domaini265 – 501237CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei502 – 51716HelicalSequence AnalysisAdd
BLAST
Topological domaini518 – 55033LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: BHF-UCL
  2. endoplasmic reticulum membrane Source: BHF-UCL
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi269 – 2691S → A or T: Nearly normal expression and enzyme activity. 1 Publication
Mutagenesisi269 – 2691S → L: No expression nor activity. 1 Publication
Mutagenesisi400 – 4001D → N: Low expression, loss of enzymatic activity. 1 Publication
Mutagenesisi456 – 4561S → A: Loss of enzymatic activity. 1 Publication
Mutagenesisi460 – 4601H → A, C or N: Loss of enzymatic activity. 1 Publication
Mutagenesisi518 – 5181Y → F: Loss of enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA36015.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 550550Sterol O-acyltransferase 1PRO_0000207640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Disulfide bondi528 ↔ 5461 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP35610.
PaxDbiP35610.
PRIDEiP35610.

PTM databases

PhosphoSiteiP35610.

Expressioni

Inductioni

Highly activated by the presence of cholesterol.

Gene expression databases

BgeeiP35610.
CleanExiHS_ACAT1.
HS_SOAT1.
ExpressionAtlasiP35610. baseline and differential.
GenevestigatoriP35610.

Organism-specific databases

HPAiCAB009533.
HPA047171.

Interactioni

Subunit structurei

May form homo- or heterodimers. Interacts with UBIAD1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
UBIAD1Q9Y5Z93EBI-6621997,EBI-2819725

Protein-protein interaction databases

BioGridi112529. 13 interactions.
IntActiP35610. 2 interactions.
STRINGi9606.ENSP00000356591.

Structurei

3D structure databases

ProteinModelPortaliP35610.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5056.
GeneTreeiENSGT00530000063122.
HOGENOMiHOG000020782.
HOVERGENiHBG058198.
InParanoidiP35610.
KOiK00637.
OMAiFNFILHD.
OrthoDBiEOG7ZPNJP.
PhylomeDBiP35610.
TreeFamiTF105767.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view]
PANTHERiPTHR10408. PTHR10408. 1 hit.
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
PIRSFiPIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35610-1) [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
MVGEEKMSLR NRLSKSRENP EEDEDQRNPA KESLETPSNG RIDIKQLIAK
60 70 80 90 100
KIKLTAEAEE LKPFFMKEVG SHFDDFVTNL IEKSASLDNG GCALTTFSVL
110 120 130 140 150
EGEKNNHRAK DLRAPPEQGK IFIARRSLLD ELLEVDHIRT IYHMFIALLI
160 170 180 190 200
LFILSTLVVD YIDEGRLVLE FSLLSYAFGK FPTVVWTWWI MFLSTFSVPY
210 220 230 240 250
FLFQHWATGY SKSSHPLIRS LFHGFLFMIF QIGVLGFGPT YVVLAYTLPP
260 270 280 290 300
ASRFIIIFEQ IRFVMKAHSF VRENVPRVLN SAKEKSSTVP IPTVNQYLYF
310 320 330 340 350
LFAPTLIYRD SYPRNPTVRW GYVAMKFAQV FGCFFYVYYI FERLCAPLFR
360 370 380 390 400
NIKQEPFSAR VLVLCVFNSI LPGVLILFLT FFAFLHCWLN AFAEMLRFGD
410 420 430 440 450
RMFYKDWWNS TSYSNYYRTW NVVVHDWLYY YAYKDFLWFF SKRFKSAAML
460 470 480 490 500
AVFAVSAVVH EYALAVCLSF FYPVLFVLFM FFGMAFNFIV NDSRKKPIWN
510 520 530 540 550
VLMWTSLFLG NGVLLCFYSQ EWYARQHCPL KNPTFLDYVR PRSWTCRYVF
Length:550
Mass (Da):64,735
Last modified:July 25, 2003 - v3
Checksum:i5F5ACD525D541DEE
GO
Isoform 2 (identifier: P35610-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MVGEEKMSLRNRLSKSRENPEEDEDQRNPAKESLETPSNGRIDIKQLIAKKIKLTAEAE → M

Show »
Length:492
Mass (Da):58,131
Checksum:i285EF79CC80BF5E8
GO
Isoform 3 (identifier: P35610-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: Missing.

Show »
Length:485
Mass (Da):57,238
Checksum:i9C0D0F331D69376A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti526 – 5261Q → R.1 Publication
Corresponds to variant rs13306731 [ dbSNP | Ensembl ].
VAR_052031

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6565Missing in isoform 3. 1 PublicationVSP_045330Add
BLAST
Alternative sequencei1 – 5959MVGEE…TAEAE → M in isoform 2. 1 PublicationVSP_045331Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21934 mRNA. Translation: AAC37532.2.
AK290659 mRNA. Translation: BAF83348.1.
AK300551 mRNA. Translation: BAG62257.1.
AL451075, AL512326 Genomic DNA. Translation: CAI12676.1.
AL512326, AL451075 Genomic DNA. Translation: CAI13574.1.
CH471067 Genomic DNA. Translation: EAW91043.1.
CH471067 Genomic DNA. Translation: EAW91044.1.
BC028940 mRNA. Translation: AAH28940.1.
CCDSiCCDS1330.1. [P35610-1]
CCDS58047.1. [P35610-2]
CCDS58048.1. [P35610-3]
PIRiA59038. A48026.
RefSeqiNP_001239440.1. NM_001252511.1. [P35610-2]
NP_001239441.1. NM_001252512.1. [P35610-3]
NP_003092.4. NM_003101.5. [P35610-1]
UniGeneiHs.445588.

Genome annotation databases

EnsembliENST00000367619; ENSP00000356591; ENSG00000057252. [P35610-1]
ENST00000539888; ENSP00000441356; ENSG00000057252. [P35610-3]
ENST00000540564; ENSP00000445315; ENSG00000057252. [P35610-2]
GeneIDi6646.
KEGGihsa:6646.
UCSCiuc001gml.3. human. [P35610-1]
uc001gmm.3. human.

Polymorphism databases

DMDMi33302623.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L21934 mRNA. Translation: AAC37532.2 .
AK290659 mRNA. Translation: BAF83348.1 .
AK300551 mRNA. Translation: BAG62257.1 .
AL451075 , AL512326 Genomic DNA. Translation: CAI12676.1 .
AL512326 , AL451075 Genomic DNA. Translation: CAI13574.1 .
CH471067 Genomic DNA. Translation: EAW91043.1 .
CH471067 Genomic DNA. Translation: EAW91044.1 .
BC028940 mRNA. Translation: AAH28940.1 .
CCDSi CCDS1330.1. [P35610-1 ]
CCDS58047.1. [P35610-2 ]
CCDS58048.1. [P35610-3 ]
PIRi A59038. A48026.
RefSeqi NP_001239440.1. NM_001252511.1. [P35610-2 ]
NP_001239441.1. NM_001252512.1. [P35610-3 ]
NP_003092.4. NM_003101.5. [P35610-1 ]
UniGenei Hs.445588.

3D structure databases

ProteinModelPortali P35610.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112529. 13 interactions.
IntActi P35610. 2 interactions.
STRINGi 9606.ENSP00000356591.

Chemistry

BindingDBi P35610.
ChEMBLi CHEMBL2782.
DrugBanki DB00973. Ezetimibe.
DB01094. Hesperetin.

PTM databases

PhosphoSitei P35610.

Polymorphism databases

DMDMi 33302623.

Proteomic databases

MaxQBi P35610.
PaxDbi P35610.
PRIDEi P35610.

Protocols and materials databases

DNASUi 6646.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367619 ; ENSP00000356591 ; ENSG00000057252 . [P35610-1 ]
ENST00000539888 ; ENSP00000441356 ; ENSG00000057252 . [P35610-3 ]
ENST00000540564 ; ENSP00000445315 ; ENSG00000057252 . [P35610-2 ]
GeneIDi 6646.
KEGGi hsa:6646.
UCSCi uc001gml.3. human. [P35610-1 ]
uc001gmm.3. human.

Organism-specific databases

CTDi 6646.
GeneCardsi GC01P179262.
HGNCi HGNC:11177. SOAT1.
HPAi CAB009533.
HPA047171.
MIMi 102642. gene.
neXtProti NX_P35610.
PharmGKBi PA36015.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5056.
GeneTreei ENSGT00530000063122.
HOGENOMi HOG000020782.
HOVERGENi HBG058198.
InParanoidi P35610.
KOi K00637.
OMAi FNFILHD.
OrthoDBi EOG7ZPNJP.
PhylomeDBi P35610.
TreeFami TF105767.

Enzyme and pathway databases

BRENDAi 2.3.1.26. 2681.

Miscellaneous databases

ChiTaRSi SOAT1. human.
GeneWikii SOAT1.
GenomeRNAii 6646.
NextBioi 25899.
PROi P35610.
SOURCEi Search...

Gene expression databases

Bgeei P35610.
CleanExi HS_ACAT1.
HS_SOAT1.
ExpressionAtlasi P35610. baseline and differential.
Genevestigatori P35610.

Family and domain databases

InterProi IPR004299. MBOAT_fam.
IPR014371. Oat_ACAT_DAG_ARE.
[Graphical view ]
PANTHERi PTHR10408. PTHR10408. 1 hit.
Pfami PF03062. MBOAT. 1 hit.
[Graphical view ]
PIRSFi PIRSF000439. Oat_ACAT_DAG_ARE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of human acyl-coenzyme A:cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells."
    Chang C.C.Y., Huh H.Y., Cadigan K.M., Chang T.-Y.
    J. Biol. Chem. 268:20747-20755(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-526.
    Tissue: Macrophage.
  2. Chang C.C.Y., Chang T.-Y.
    Submitted (MAY-1999) to UniProtKB
    Cited for: SEQUENCE REVISION TO 207.
  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 2 AND 3).
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Placenta.
  7. "Human acyl-CoA:cholesterol acyltransferase-1 in the endoplasmic reticulum contains seven transmembrane domains."
    Lin S., Cheng D., Liu M.S., Chen J., Chang T.-Y.
    J. Biol. Chem. 274:23276-23285(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY TOPOLOGY.
  8. "The active site His-460 of human acyl-coenzyme A:cholesterol acyltransferase 1 resides in a hitherto undisclosed transmembrane domain."
    Guo Z.Y., Lin S., Heinen J.A., Chang C.C., Chang T.Y.
    J. Biol. Chem. 280:37814-37826(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, ACTIVE SITE, DISULFIDE BOND, MUTAGENESIS OF SER-269 AND HIS-460.
  9. "Identification of putative active site residues of ACAT enzymes."
    Das A., Davis M.A., Rudel L.L.
    J. Lipid Res. 49:1770-1781(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF ASP-400; SER-456; HIS-460 AND TYR-518.
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: INTERACTION WITH UBIAD1.

Entry informationi

Entry nameiSOAT1_HUMAN
AccessioniPrimary (citable) accession number: P35610
Secondary accession number(s): A6NC40
, A8K3P4, A9Z1V7, B4DU95, Q5T0X4, Q8N1E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: July 25, 2003
Last modified: November 26, 2014
This is version 142 of the entry and version 3 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. 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