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Q9Y617

- SERC_HUMAN

UniProt

Q9Y617 - SERC_HUMAN

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Protein

Phosphoserine aminotransferase

Gene
PSAT1, PSA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity.UniRule annotation

Catalytic activityi

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.UniRule annotation
4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.UniRule annotation

Cofactori

Binds 1 pyridoxal phosphate per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451L-glutamate By similarity
Binding sitei107 – 1071Pyridoxal phosphate By similarity
Binding sitei156 – 1561Pyridoxal phosphate By similarity
Binding sitei176 – 1761Pyridoxal phosphate By similarity
Binding sitei199 – 1991Pyridoxal phosphate By similarity

GO - Molecular functioni

  1. O-phospho-L-serine:2-oxoglutarate aminotransferase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: Reactome
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. L-serine biosynthetic process Source: UniProtKB
  4. pyridoxine biosynthetic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS05946-MONOMER.
ReactomeiREACT_115789. Serine biosynthesis.
UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine aminotransferase (EC:2.6.1.52)
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name:
PSAT
Gene namesi
Name:PSAT1
Synonyms:PSA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:19129. PSAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Phosphoserine aminotransferase deficiency (PSATD) [MIM:610992]: Characterized biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001D → A in PSATD; reduced Vmax. 1 Publication
VAR_037252

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610992. phenotype.
Orphaneti284417. Phosphoserine aminotransferase deficiency.
PharmGKBiPA128395782.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Phosphoserine aminotransferaseUniRule annotationPRO_0000150135Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei51 – 511N6-acetyllysine1 Publication
Modified residuei127 – 1271N6-acetyllysine By similarity
Modified residuei200 – 2001N6-(pyridoxal phosphate)lysine By similarity
Modified residuei269 – 2691N6-acetyllysine1 Publication
Modified residuei318 – 3181N6-acetyllysine1 Publication
Modified residuei323 – 3231N6-acetyllysine1 Publication
Modified residuei333 – 3331N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y617.
PaxDbiQ9Y617.
PeptideAtlasiQ9Y617.
PRIDEiQ9Y617.

2D gel databases

REPRODUCTION-2DPAGEIPI00001734.

PTM databases

PhosphoSiteiQ9Y617.

Expressioni

Tissue specificityi

Expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon.

Gene expression databases

ArrayExpressiQ9Y617.
BgeeiQ9Y617.
CleanExiHS_PSAT1.
GenevestigatoriQ9Y617.

Organism-specific databases

HPAiCAB014882.
CAB040567.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi119001. 24 interactions.
IntActiQ9Y617. 3 interactions.
MINTiMINT-1490243.
STRINGi9606.ENSP00000365773.

Structurei

Secondary structure

1
370
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 279
Beta strandi29 – 313
Helixi32 – 343
Beta strandi35 – 373
Turni39 – 413
Helixi47 – 6418
Beta strandi70 – 778
Helixi78 – 9013
Helixi91 – 933
Beta strandi98 – 1014
Helixi106 – 11510
Turni116 – 1183
Beta strandi119 – 1235
Beta strandi129 – 1313
Helixi137 – 1393
Beta strandi149 – 1557
Turni156 – 1594
Beta strandi173 – 1764
Turni178 – 1825
Helixi188 – 1903
Beta strandi192 – 1976
Turni198 – 2025
Beta strandi208 – 2136
Helixi226 – 2283
Helixi230 – 2345
Turni235 – 2384
Helixi245 – 26016
Helixi263 – 28321
Beta strandi288 – 2903
Helixi295 – 2973
Beta strandi300 – 30910
Helixi314 – 32613
Beta strandi329 – 3313
Turni336 – 3383
Beta strandi340 – 3445
Helixi351 – 36818

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3E77X-ray2.50A/B/C17-370[»]
ProteinModelPortaliQ9Y617.
SMRiQ9Y617. Positions 17-370.

Miscellaneous databases

EvolutionaryTraceiQ9Y617.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 802Pyridoxal phosphate binding By similarity
Regioni241 – 2422Pyridoxal phosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1932.
HOGENOMiHOG000088965.
HOVERGENiHBG001218.
InParanoidiQ9Y617.
KOiK00831.
OMAiVFFGAQK.
OrthoDBiEOG7KQ220.
PhylomeDBiQ9Y617.
TreeFamiTF312975.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
InterProiIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01364. serC_1. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y617-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha

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

MDAPRQVVNF GPGPAKLPHS VLLEIQKELL DYKGVGISVL EMSHRSSDFA    50
KIINNTENLV RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKAGRCAD 100
YVVTGAWSAK AAEEAKKFGT INIVHPKLGS YTKIPDPSTW NLNPDASYVY 150
YCANETVHGV EFDFIPDVKG AVLVCDMSSN FLSKPVDVSK FGVIFAGAQK 200
NVGSAGVTVV IVRDDLLGFA LRECPSVLEY KVQAGNSSLY NTPPCFSIYV 250
MGLVLEWIKN NGGAAAMEKL SSIKSQTIYE IIDNSQGFYV CPVEPQNRSK 300
MNIPFRIGNA KGDDALEKRF LDKALELNML SLKGHRSVGG IRASLYNAVT 350
IEDVQKLAAF MKKFLEMHQL 370
Length:370
Mass (Da):40,423
Last modified:January 23, 2002 - v2
Checksum:iBAF9A10E71B165B4
GO
Isoform 2 (identifier: Q9Y617-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     291-336: Missing.

Show »
Length:324
Mass (Da):35,189
Checksum:i4F83811D3593DDA1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871P → A.
Corresponds to variant rs11540974 [ dbSNP | Ensembl ].
VAR_048235
Natural varianti100 – 1001D → A in PSATD; reduced Vmax. 1 Publication
VAR_037252

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei291 – 33646Missing in isoform 2. VSP_000237Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401L → V in AAH16645. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113132 mRNA. Translation: AAD42052.1.
AY131232 mRNA. Translation: AAN71736.1.
BT006840 mRNA. Translation: AAP35486.1.
AL353594 Genomic DNA. Translation: CAI16882.1.
AL353594 Genomic DNA. Translation: CAI16883.1.
CH471089 Genomic DNA. Translation: EAW62621.1.
CH471089 Genomic DNA. Translation: EAW62617.1.
BC000971 mRNA. Translation: AAH00971.1.
BC004863 mRNA. Translation: AAH04863.1.
BC016645 mRNA. Translation: AAH16645.1.
BC018129 mRNA. Translation: AAH18129.1.
CCDSiCCDS6659.1. [Q9Y617-2]
CCDS6660.1. [Q9Y617-1]
RefSeqiNP_066977.1. NM_021154.4. [Q9Y617-2]
NP_478059.1. NM_058179.3. [Q9Y617-1]
UniGeneiHs.494261.

Genome annotation databases

EnsembliENST00000347159; ENSP00000317606; ENSG00000135069. [Q9Y617-2]
ENST00000376588; ENSP00000365773; ENSG00000135069. [Q9Y617-1]
GeneIDi29968.
KEGGihsa:29968.
UCSCiuc004ala.3. human. [Q9Y617-1]
uc004alb.3. human. [Q9Y617-2]

Polymorphism databases

DMDMi20141815.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF113132 mRNA. Translation: AAD42052.1 .
AY131232 mRNA. Translation: AAN71736.1 .
BT006840 mRNA. Translation: AAP35486.1 .
AL353594 Genomic DNA. Translation: CAI16882.1 .
AL353594 Genomic DNA. Translation: CAI16883.1 .
CH471089 Genomic DNA. Translation: EAW62621.1 .
CH471089 Genomic DNA. Translation: EAW62617.1 .
BC000971 mRNA. Translation: AAH00971.1 .
BC004863 mRNA. Translation: AAH04863.1 .
BC016645 mRNA. Translation: AAH16645.1 .
BC018129 mRNA. Translation: AAH18129.1 .
CCDSi CCDS6659.1. [Q9Y617-2 ]
CCDS6660.1. [Q9Y617-1 ]
RefSeqi NP_066977.1. NM_021154.4. [Q9Y617-2 ]
NP_478059.1. NM_058179.3. [Q9Y617-1 ]
UniGenei Hs.494261.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3E77 X-ray 2.50 A/B/C 17-370 [» ]
ProteinModelPortali Q9Y617.
SMRi Q9Y617. Positions 17-370.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119001. 24 interactions.
IntActi Q9Y617. 3 interactions.
MINTi MINT-1490243.
STRINGi 9606.ENSP00000365773.

Chemistry

DrugBanki DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.
DB00165. Pyridoxine.

PTM databases

PhosphoSitei Q9Y617.

Polymorphism databases

DMDMi 20141815.

2D gel databases

REPRODUCTION-2DPAGE IPI00001734.

Proteomic databases

MaxQBi Q9Y617.
PaxDbi Q9Y617.
PeptideAtlasi Q9Y617.
PRIDEi Q9Y617.

Protocols and materials databases

DNASUi 29968.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000347159 ; ENSP00000317606 ; ENSG00000135069 . [Q9Y617-2 ]
ENST00000376588 ; ENSP00000365773 ; ENSG00000135069 . [Q9Y617-1 ]
GeneIDi 29968.
KEGGi hsa:29968.
UCSCi uc004ala.3. human. [Q9Y617-1 ]
uc004alb.3. human. [Q9Y617-2 ]

Organism-specific databases

CTDi 29968.
GeneCardsi GC09P080911.
HGNCi HGNC:19129. PSAT1.
HPAi CAB014882.
CAB040567.
MIMi 610936. gene.
610992. phenotype.
neXtProti NX_Q9Y617.
Orphaneti 284417. Phosphoserine aminotransferase deficiency.
PharmGKBi PA128395782.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1932.
HOGENOMi HOG000088965.
HOVERGENi HBG001218.
InParanoidi Q9Y617.
KOi K00831.
OMAi VFFGAQK.
OrthoDBi EOG7KQ220.
PhylomeDBi Q9Y617.
TreeFami TF312975.

Enzyme and pathway databases

UniPathwayi UPA00135 ; UER00197 .
UPA00244 ; UER00311 .
BioCyci MetaCyc:HS05946-MONOMER.
Reactomei REACT_115789. Serine biosynthesis.

Miscellaneous databases

ChiTaRSi PSAT1. human.
EvolutionaryTracei Q9Y617.
GeneWikii PSAT1.
GenomeRNAii 29968.
NextBioi 52705.
PROi Q9Y617.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y617.
Bgeei Q9Y617.
CleanExi HS_PSAT1.
Genevestigatori Q9Y617.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPi MF_00160. SerC_aminotrans_5.
InterProi IPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00266. Aminotran_5. 1 hit.
[Graphical view ]
PIRSFi PIRSF000525. SerC. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01364. serC_1. 1 hit.
PROSITEi PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis."
    Baek J.Y., Jun Y.D., Taub D., Kim Y.H.
    Biochem. J. 373:191-200(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "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] (ISOFORM 1).
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] (ISOFORMS 1 AND 2).
    Tissue: Lung, Lymph and Placenta.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-51; LYS-269; LYS-318; LYS-323 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway."
    Hart C.E., Race V., Achouri Y., Wiame E., Sharrard M., Olpin S.E., Watkinson J., Bonham J.R., Jaeken J., Matthijs G., Van Schaftingen E.
    Am. J. Hum. Genet. 80:931-937(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PSATD ALA-100, CHARACTERIZATION OF VARIANT PSATD ALA-100.

Entry informationi

Entry nameiSERC_HUMAN
AccessioniPrimary (citable) accession number: Q9Y617
Secondary accession number(s): Q5T7G5
, Q5T7G6, Q96AW2, Q9BQ12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2002
Last modified: September 3, 2014
This is version 151 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 9
    Human chromosome 9: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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