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Protein

DNA-directed RNA polymerases I and III subunit RPAC1

Gene

POLR1C

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

Functioni

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: InterPro
  • DNA-directed RNA polymerase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_1074. RNA Polymerase I Transcription Termination.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.
REACT_953. RNA Polymerase I Transcription Initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I and III subunit RPAC1
Short name:
DNA-directed RNA polymerase I subunit C
Short name:
RNA polymerases I and III subunit AC1
Alternative name(s):
AC40
DNA-directed RNA polymerases I and III 40 kDa polypeptide
Short name:
RPA40
RPA39
RPC40
Gene namesi
Name:POLR1C
Synonyms:POLR1E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:20194. POLR1C.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase I complex Source: ProtInc
  • DNA-directed RNA polymerase III complex Source: MGI
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Involvement in diseasei

Treacher Collins syndrome 3 (TCS3)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of Treacher Collins syndrome, a disorder of craniofacial development. Treacher Collins syndrome is characterized by a combination of bilateral downward slanting of the palpebral fissures, colobomas of the lower eyelids with a paucity of eyelashes medial to the defect, hypoplasia of the facial bones, cleft palate, malformation of the external ears, atresia of the external auditory canals, and bilateral conductive hearing loss.

See also OMIM:248390
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti279 – 2791R → Q in TCS3. 1 Publication
Corresponds to variant rs191582628 [ dbSNP | Ensembl ].
VAR_064899
Natural varianti279 – 2791R → W in TCS3. 1 Publication
VAR_064900

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi248390. phenotype.
Orphaneti861. Treacher-Collins syndrome.
PharmGKBiPA134882004.

Polymorphism and mutation databases

BioMutaiPOLR1C.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 346345DNA-directed RNA polymerases I and III subunit RPAC1PRO_0000132739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO15160.
PaxDbiO15160.
PRIDEiO15160.

2D gel databases

REPRODUCTION-2DPAGEIPI00217386.
SWISS-2DPAGEO15160.

PTM databases

PhosphoSiteiO15160.

Expressioni

Gene expression databases

BgeeiO15160.
CleanExiHS_POLR1C.
HS_POLR1E.
ExpressionAtlasiO15160. baseline and differential.
GenevestigatoriO15160.

Organism-specific databases

HPAiHPA031010.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I) and RNA polymerase III (Pol III) complexes consisting of at least 13 and 17 subunits, respectively.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ATRIPQ8WXE13EBI-1055079,EBI-747353
BIRC7Q96CA53EBI-1055079,EBI-517623
C9orf138A8K8803EBI-1055079,EBI-10174528
CCDC36Q8IYA83EBI-1055079,EBI-8638439
FAM208BQ5VWN6-23EBI-1055079,EBI-10172380
IKZF3Q9UKT93EBI-1055079,EBI-747204
KCTD1Q719H93EBI-1055079,EBI-9027502
KRT19P087273EBI-1055079,EBI-742756
LZTS2Q9BRK43EBI-1055079,EBI-741037
MBIPQ9NS73-53EBI-1055079,EBI-10182361
NME1P155315EBI-1055079,EBI-741141
POLR1DQ9Y2S07EBI-1055079,EBI-359498
POLR2JP524354EBI-1055079,EBI-394753
PPP2R3CQ969Q65EBI-1055079,EBI-2561661
RIMBP3Q9UFD93EBI-1055079,EBI-10182375
SMN2Q166373EBI-1055079,EBI-395421
TCF4P158843EBI-1055079,EBI-533224
TNFAIP1Q138294EBI-1055079,EBI-2505861
TRIM27P143733EBI-1055079,EBI-719493
TSC22D4Q9Y3Q83EBI-1055079,EBI-739485

Protein-protein interaction databases

BioGridi114909. 67 interactions.
DIPiDIP-27587N.
IntActiO15160. 38 interactions.
MINTiMINT-1137932.
STRINGi9606.ENSP00000361465.

Structurei

3D structure databases

ProteinModelPortaliO15160.
SMRiO15160. Positions 40-332.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0202.
GeneTreeiENSGT00550000075060.
HOGENOMiHOG000230845.
HOVERGENiHBG017743.
InParanoidiO15160.
KOiK03027.
OMAiGKCQRFL.
PhylomeDBiO15160.
TreeFamiTF103034.

Family and domain databases

Gene3Di2.170.120.12. 1 hit.
InterProiIPR001514. DNA-dir_RNA_pol_30-40kDasu_CS.
IPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR009025. RBP11-like_dimer.
[Graphical view]
PfamiPF01000. RNA_pol_A_bac. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
SMARTiSM00662. RPOLD. 1 hit.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
PROSITEiPS00446. RNA_POL_D_30KD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: O15160-1) [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
MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR
60 70 80 90 100
VDVVHMDENS LEFDMVGIDA AIANAFRRIL LAEVPTMAVE KVLVYNNTSI
110 120 130 140 150
VQDEILAHRL GLIPIHADPR LFEYRNQGDE EGTEIDTLQF RLQVRCTRNP
160 170 180 190 200
HAAKDSSDPN ELYVNHKVYT RHMTWIPLGN QADLFPEGTI RPVHDDILIA
210 220 230 240 250
QLRPGQEIDL LMHCVKGIGK DHAKFSPVAT ASYRLLPDIT LLEPVEGEAA
260 270 280 290 300
EELSRCFSPG VIEVQEVQGK KVARVANPRL DTFSREIFRN EKLKKVVRLA
310 320 330 340
RVRDHYIFSV ESTGVLPPDV LVSEAIKVLM GKCRRFLDEL DAVQMD
Length:346
Mass (Da):39,250
Last modified:January 1, 1998 - v1
Checksum:iB7D558BC8F33D92E
GO
Isoform 2 (identifier: O15160-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-346: FSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD → CKKDLLAAVAHTCNPSTLGGQGEWITGSRERDHPG

Note: No experimental confirmation available.

Show »
Length:342
Mass (Da):38,647
Checksum:i9E2785123BB74D8B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti279 – 2791R → Q in TCS3. 1 Publication
Corresponds to variant rs191582628 [ dbSNP | Ensembl ].
VAR_064899
Natural varianti279 – 2791R → W in TCS3. 1 Publication
VAR_064900

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 34639FSVES…AVQMD → CKKDLLAAVAHTCNPSTLGG QGEWITGSRERDHPG in isoform 2. 1 PublicationVSP_005913Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008442 mRNA. Translation: AAC14354.1.
AF047441 mRNA. Translation: AAC39892.1.
AL355802 Genomic DNA. Translation: CAI42629.1.
BC008863 mRNA. Translation: AAH08863.1.
CCDSiCCDS4901.1. [O15160-1]
RefSeqiNP_976035.1. NM_203290.2. [O15160-1]
XP_005249548.1. XM_005249491.1. [O15160-2]
UniGeneiHs.743509.

Genome annotation databases

EnsembliENST00000304004; ENSP00000307212; ENSG00000171453. [O15160-2]
ENST00000372389; ENSP00000361465; ENSG00000171453. [O15160-1]
GeneIDi9533.
KEGGihsa:9533.
UCSCiuc003ovn.3. human. [O15160-1]
uc003ovo.2. human. [O15160-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008442 mRNA. Translation: AAC14354.1.
AF047441 mRNA. Translation: AAC39892.1.
AL355802 Genomic DNA. Translation: CAI42629.1.
BC008863 mRNA. Translation: AAH08863.1.
CCDSiCCDS4901.1. [O15160-1]
RefSeqiNP_976035.1. NM_203290.2. [O15160-1]
XP_005249548.1. XM_005249491.1. [O15160-2]
UniGeneiHs.743509.

3D structure databases

ProteinModelPortaliO15160.
SMRiO15160. Positions 40-332.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114909. 67 interactions.
DIPiDIP-27587N.
IntActiO15160. 38 interactions.
MINTiMINT-1137932.
STRINGi9606.ENSP00000361465.

PTM databases

PhosphoSiteiO15160.

Polymorphism and mutation databases

BioMutaiPOLR1C.

2D gel databases

REPRODUCTION-2DPAGEIPI00217386.
SWISS-2DPAGEO15160.

Proteomic databases

MaxQBiO15160.
PaxDbiO15160.
PRIDEiO15160.

Protocols and materials databases

DNASUi9533.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000304004; ENSP00000307212; ENSG00000171453. [O15160-2]
ENST00000372389; ENSP00000361465; ENSG00000171453. [O15160-1]
GeneIDi9533.
KEGGihsa:9533.
UCSCiuc003ovn.3. human. [O15160-1]
uc003ovo.2. human. [O15160-2]

Organism-specific databases

CTDi9533.
GeneCardsiGC06P043484.
GeneReviewsiPOLR1C.
H-InvDBHIX0005907.
HGNCiHGNC:20194. POLR1C.
HPAiHPA031010.
MIMi248390. phenotype.
610060. gene.
neXtProtiNX_O15160.
Orphaneti861. Treacher-Collins syndrome.
PharmGKBiPA134882004.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0202.
GeneTreeiENSGT00550000075060.
HOGENOMiHOG000230845.
HOVERGENiHBG017743.
InParanoidiO15160.
KOiK03027.
OMAiGKCQRFL.
PhylomeDBiO15160.
TreeFamiTF103034.

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_1074. RNA Polymerase I Transcription Termination.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.
REACT_953. RNA Polymerase I Transcription Initiation.

Miscellaneous databases

GeneWikiiPOLR1C.
GenomeRNAii9533.
NextBioi35740.
PROiO15160.
SOURCEiSearch...

Gene expression databases

BgeeiO15160.
CleanExiHS_POLR1C.
HS_POLR1E.
ExpressionAtlasiO15160. baseline and differential.
GenevestigatoriO15160.

Family and domain databases

Gene3Di2.170.120.12. 1 hit.
InterProiIPR001514. DNA-dir_RNA_pol_30-40kDasu_CS.
IPR011262. DNA-dir_RNA_pol_insert.
IPR011263. DNA-dir_RNA_pol_RpoA/D/Rpb3.
IPR009025. RBP11-like_dimer.
[Graphical view]
PfamiPF01000. RNA_pol_A_bac. 1 hit.
PF01193. RNA_pol_L. 1 hit.
[Graphical view]
SMARTiSM00662. RPOLD. 1 hit.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 2 hits.
SSF56553. SSF56553. 1 hit.
PROSITEiPS00446. RNA_POL_D_30KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human RNA polymerase I subunit hRPA40."
    Dammann R., Pfeifer G.P.
    Biochim. Biophys. Acta 1396:153-157(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Umbilical cord blood.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain.
  5. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 14-22; 79-91; 110-120; 155-167 AND 225-255, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  6. "Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits."
    Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.
    Mol. Cell. Biol. 22:8044-8055(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: VARIANTS TCS3 GLN-279 AND TRP-279.

Entry informationi

Entry nameiRPAC1_HUMAN
AccessioniPrimary (citable) accession number: O15160
Secondary accession number(s): O75395, Q5JTE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 158 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.