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Q01581

- HMCS1_HUMAN

UniProt

Q01581 - HMCS1_HUMAN

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Protein

Hydroxymethylglutaryl-CoA synthase, cytoplasmic

Gene

HMGCS1

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

Functioni

This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.

Catalytic activityi

Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Proton donor/acceptorPROSITE-ProRule annotation
Active sitei129 – 1291Acyl-thioester intermediate
Active sitei264 – 2641Proton donor/acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. drug binding Source: Ensembl
  2. hydroxymethylglutaryl-CoA synthase activity Source: ProtInc
  3. isomerase activity Source: Ensembl
  4. organic acid binding Source: Ensembl

GO - Biological processi

  1. brain development Source: Ensembl
  2. cellular lipid metabolic process Source: Reactome
  3. cellular response to cholesterol Source: Ensembl
  4. cellular response to follicle-stimulating hormone stimulus Source: Ensembl
  5. cholesterol biosynthetic process Source: Reactome
  6. isoprenoid biosynthetic process Source: InterPro
  7. lipid metabolic process Source: ProtInc
  8. liver development Source: Ensembl
  9. male gonad development Source: Ensembl
  10. response to acid chemical Source: Ensembl
  11. response to drug Source: Ensembl
  12. response to lipoprotein particle Source: Ensembl
  13. response to low light intensity stimulus Source: Ensembl
  14. response to purine-containing compound Source: Ensembl
  15. response to tellurium ion Source: Ensembl
  16. response to vitamin E Source: Ensembl
  17. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000112972-MONOMER.
BRENDAi2.3.3.10. 2681.
ReactomeiREACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
UniPathwayiUPA00058; UER00102.

Names & Taxonomyi

Protein namesi
Recommended name:
Hydroxymethylglutaryl-CoA synthase, cytoplasmic (EC:2.3.3.10)
Short name:
HMG-CoA synthase
Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase
Gene namesi
Name:HMGCS1
Synonyms:HMGCS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:5007. HMGCS1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleus Source: HPA
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291C → A or S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA29337.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Hydroxymethylglutaryl-CoA synthase, cytoplasmicPRO_0000213747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41Phosphoserine1 Publication
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei273 – 2731N6-acetyllysine1 Publication
Modified residuei476 – 4761Phosphothreonine1 Publication
Modified residuei495 – 4951Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ01581.
PaxDbiQ01581.
PeptideAtlasiQ01581.
PRIDEiQ01581.

PTM databases

PhosphoSiteiQ01581.

Expressioni

Gene expression databases

BgeeiQ01581.
CleanExiHS_HMGCS1.
ExpressionAtlasiQ01581. baseline and differential.
GenevestigatoriQ01581.

Organism-specific databases

HPAiCAB032907.
HPA036913.
HPA036914.

Interactioni

Protein-protein interaction databases

BioGridi109400. 17 interactions.
IntActiQ01581. 2 interactions.
STRINGi9606.ENSP00000322706.

Structurei

Secondary structure

1
520
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258
Beta strandi28 – 325
Helixi33 – 408
Helixi46 – 516
Beta strandi55 – 573
Helixi65 – 7915
Helixi84 – 863
Beta strandi87 – 937
Beta strandi100 – 1023
Helixi104 – 1085
Helixi109 – 1113
Turni112 – 1165
Beta strandi124 – 1274
Helixi128 – 1303
Helixi131 – 14313
Beta strandi152 – 16110
Helixi169 – 1713
Beta strandi173 – 18412
Beta strandi186 – 1894
Beta strandi195 – 1984
Beta strandi203 – 2053
Helixi218 – 24730
Helixi255 – 2573
Beta strandi259 – 2635
Helixi268 – 28518
Helixi289 – 2913
Helixi293 – 2953
Helixi299 – 3013
Helixi306 – 3083
Helixi313 – 32210
Helixi324 – 3307
Helixi333 – 3353
Helixi336 – 3416
Helixi345 – 3473
Helixi348 – 35912
Helixi362 – 3654
Beta strandi369 – 3768
Turni377 – 3793
Beta strandi380 – 3889
Helixi397 – 4037
Turni404 – 4074
Helixi408 – 4136
Beta strandi415 – 4173
Helixi420 – 43314
Beta strandi453 – 4586
Beta strandi464 – 4685

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P8UX-ray2.00A/B16-470[»]
ProteinModelPortaliQ01581.
SMRiQ01581. Positions 16-470.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01581.

Family & Domainsi

Sequence similaritiesi

Belongs to the HMG-CoA synthase family.Curated

Phylogenomic databases

eggNOGiCOG3425.
GeneTreeiENSGT00390000006096.
HOGENOMiHOG000012351.
HOVERGENiHBG051912.
InParanoidiQ01581.
KOiK01641.
OMAiRDFTLND.
OrthoDBiEOG741Z1W.
PhylomeDBiQ01581.
TreeFamiTF105361.

Family and domain databases

Gene3Di3.40.47.10. 1 hit.
InterProiIPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF53901. SSF53901. 3 hits.
TIGRFAMsiTIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEiPS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01581-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG
60 70 80 90 100
LGQAKMGFCT DREDINSLCM TVVQNLMERN NLSYDCIGRL EVGTETIIDK
110 120 130 140 150
SKSVKTNLMQ LFEESGNTDI EGIDTTNACY GGTAAVFNAV NWIESSSWDG
160 170 180 190 200
RYALVVAGDI AVYATGNARP TGGVGAVALL IGPNAPLIFE RGLRGTHMQH
210 220 230 240 250
AYDFYKPDML SEYPIVDGKL SIQCYLSALD RCYSVYCKKI HAQWQKEGND
260 270 280 290 300
KDFTLNDFGF MIFHSPYCKL VQKSLARMLL NDFLNDQNRD KNSIYSGLEA
310 320 330 340 350
FGDVKLEDTY FDRDVEKAFM KASSELFSQK TKASLLVSNQ NGNMYTSSVY
360 370 380 390 400
GSLASVLAQY SPQQLAGKRI GVFSYGSGLA ATLYSLKVTQ DATPGSALDK
410 420 430 440 450
ITASLCDLKS RLDSRTGVAP DVFAENMKLR EDTHHLVNYI PQGSIDSLFE
460 470 480 490 500
GTWYLVRVDE KHRRTYARRP TPNDDTLDEG VGLVHSNIAT EHIPSPAKKV
510 520
PRLPATAAEP EAAVISNGEH
Length:520
Mass (Da):57,294
Last modified:October 1, 1996 - v2
Checksum:iC669212BF86CFF9B
GO

Sequence cautioni

The sequence AAH00297.2 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti248 – 2481G → A in CAA47061. (PubMed:1358203)Curated
Sequence conflicti251 – 2511K → N in CAA47061. (PubMed:1358203)Curated
Sequence conflicti299 – 2991E → K in CAA47061. (PubMed:1358203)Curated
Sequence conflicti364 – 3641Q → H in CAA47061. (PubMed:1358203)Curated
Sequence conflicti420 – 4201P → Q in CAA47061. (PubMed:1358203)Curated
Sequence conflicti519 – 5202EH → VW in CAA47061. (PubMed:1358203)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66435 mRNA. Translation: CAA47061.1.
L25798 mRNA. Translation: AAA62411.1.
BT007302 mRNA. Translation: AAP35966.1.
AK315593 mRNA. Translation: BAG37965.1.
CH471119 Genomic DNA. Translation: EAW56054.1.
BC000297 mRNA. Translation: AAH00297.2. Different initiation.
CCDSiCCDS34154.1.
PIRiS27197.
S45497.
RefSeqiNP_001091742.1. NM_001098272.2.
NP_002121.4. NM_002130.7.
UniGeneiHs.397729.
Hs.741287.

Genome annotation databases

EnsembliENST00000325110; ENSP00000322706; ENSG00000112972.
ENST00000433297; ENSP00000399402; ENSG00000112972.
GeneIDi3157.
KEGGihsa:3157.
UCSCiuc003jnq.5. human.

Polymorphism databases

DMDMi1708239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66435 mRNA. Translation: CAA47061.1 .
L25798 mRNA. Translation: AAA62411.1 .
BT007302 mRNA. Translation: AAP35966.1 .
AK315593 mRNA. Translation: BAG37965.1 .
CH471119 Genomic DNA. Translation: EAW56054.1 .
BC000297 mRNA. Translation: AAH00297.2 . Different initiation.
CCDSi CCDS34154.1.
PIRi S27197.
S45497.
RefSeqi NP_001091742.1. NM_001098272.2.
NP_002121.4. NM_002130.7.
UniGenei Hs.397729.
Hs.741287.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P8U X-ray 2.00 A/B 16-470 [» ]
ProteinModelPortali Q01581.
SMRi Q01581. Positions 16-470.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109400. 17 interactions.
IntActi Q01581. 2 interactions.
STRINGi 9606.ENSP00000322706.

Chemistry

GuidetoPHARMACOLOGYi 638.

PTM databases

PhosphoSitei Q01581.

Polymorphism databases

DMDMi 1708239.

Proteomic databases

MaxQBi Q01581.
PaxDbi Q01581.
PeptideAtlasi Q01581.
PRIDEi Q01581.

Protocols and materials databases

DNASUi 3157.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000325110 ; ENSP00000322706 ; ENSG00000112972 .
ENST00000433297 ; ENSP00000399402 ; ENSG00000112972 .
GeneIDi 3157.
KEGGi hsa:3157.
UCSCi uc003jnq.5. human.

Organism-specific databases

CTDi 3157.
GeneCardsi GC05M043326.
HGNCi HGNC:5007. HMGCS1.
HPAi CAB032907.
HPA036913.
HPA036914.
MIMi 142940. gene.
neXtProti NX_Q01581.
PharmGKBi PA29337.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3425.
GeneTreei ENSGT00390000006096.
HOGENOMi HOG000012351.
HOVERGENi HBG051912.
InParanoidi Q01581.
KOi K01641.
OMAi RDFTLND.
OrthoDBi EOG741Z1W.
PhylomeDBi Q01581.
TreeFami TF105361.

Enzyme and pathway databases

UniPathwayi UPA00058 ; UER00102 .
BioCyci MetaCyc:ENSG00000112972-MONOMER.
BRENDAi 2.3.3.10. 2681.
Reactomei REACT_116145. PPARA activates gene expression.
REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.

Miscellaneous databases

ChiTaRSi HMGCS1. human.
EvolutionaryTracei Q01581.
GenomeRNAii 3157.
NextBioi 12504.
PROi Q01581.
SOURCEi Search...

Gene expression databases

Bgeei Q01581.
CleanExi HS_HMGCS1.
ExpressionAtlasi Q01581. baseline and differential.
Genevestigatori Q01581.

Family and domain databases

Gene3Di 3.40.47.10. 1 hit.
InterProi IPR000590. HMG_CoA_synt_AS.
IPR013746. HMG_CoA_synt_C_dom.
IPR013528. HMG_CoA_synth_N.
IPR010122. HMG_CoA_synthase_euk.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF08540. HMG_CoA_synt_C. 1 hit.
PF01154. HMG_CoA_synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53901. SSF53901. 3 hits.
TIGRFAMsi TIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITEi PS01226. HMG_COA_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Amplification and direct sequencing of a cDNA encoding human cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase."
    Russ A.P., Ruzicka V., Maerz W., Appelhans H., Gross W.
    Biochim. Biophys. Acta 1132:329-331(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fibroblast.
  2. "Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes."
    Rokosz L.L., Boulton D.A., Butkiewicz E.A., Sanyal G., Cueto M.A., Lachance P.A., Hermes J.D.
    Arch. Biochem. Biophys. 312:1-13(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, MUTAGENESIS.
    Tissue: Fetal adrenal gland.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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: Placenta.
  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].
    Tissue: Lung.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-476 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46 AND LYS-273, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHMCS1_HUMAN
AccessioniPrimary (citable) accession number: Q01581
Secondary accession number(s): B2RDL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 161 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3