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Protein

DNA-directed RNA polymerases I and III subunit RPAC2

Gene

POLR1D

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 core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.

GO - Molecular functioni

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 RPAC2
Short name:
RNA polymerases I and III subunit AC2
Alternative name(s):
AC19
DNA-directed RNA polymerase I subunit D
RNA polymerase I 16 kDa subunit
Short name:
RPA16
RPC16
hRPA19
Gene namesi
Name:POLR1D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:20422. POLR1D.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Involvement in diseasei

Treacher Collins syndrome 2 (TCS2)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:613717
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471E → K in TCS2. 1 Publication
VAR_064892
Natural varianti50 – 501T → I in TCS2. 1 Publication
VAR_064893
Natural varianti51 – 511L → R in TCS2. 1 Publication
VAR_064894
Natural varianti52 – 521G → E in TCS2. 1 Publication
VAR_064895
Natural varianti56 – 561R → C in TCS2. 1 Publication
VAR_064896
Natural varianti82 – 821L → S in TCS2. 1 Publication
VAR_064897
Natural varianti99 – 991G → S in TCS2. 1 Publication
VAR_064898

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613717. phenotype.
Orphaneti861. Treacher-Collins syndrome.
PharmGKBiPA134914527.

Polymorphism and mutation databases

BioMutaiPOLR1D.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133DNA-directed RNA polymerases I and III subunit RPAC2PRO_0000149316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Isoform 2 (identifier: Q9Y2S0-2)
Modified residuei104 – 1041Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2S0.
PaxDbiQ9Y2S0.
PeptideAtlasiQ9Y2S0.
PRIDEiQ9Y2S0.

2D gel databases

SWISS-2DPAGEQ9Y2S0.

PTM databases

PhosphoSiteiQ9Y2S0.

Expressioni

Gene expression databases

BgeeiQ9Y2S0.
CleanExiHS_POLR1D.
ExpressionAtlasiQ9Y2S0. baseline and differential.
GenevisibleiQ9Y2S0. HS.

Organism-specific databases

HPAiHPA039337.

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
POLR1CO151607EBI-359498,EBI-1055079

Protein-protein interaction databases

BioGridi119272. 26 interactions.
DIPiDIP-27598N.
IntActiQ9Y2S0. 15 interactions.
MINTiMINT-1149665.
STRINGi9606.ENSP00000302478.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2S0.
SMRiQ9Y2S0. Positions 22-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1761.
GeneTreeiENSGT00550000075160.
HOGENOMiHOG000179862.
HOVERGENiHBG001176.
InParanoidiQ9Y2S0.
KOiK03020.
OMAiSSFSIME.
OrthoDBiEOG7J9VRX.
PhylomeDBiQ9Y2S0.
TreeFamiTF103035.

Family and domain databases

InterProiIPR009025. RBP11-like_dimer.
IPR008193. RNA_pol_Rpb11_13-16kDa_CS.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 1 hit.
PROSITEiPS01154. RNA_POL_L_13KD. 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: Q9Y2S0-1) [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
MEEDQELERK ISGLKTSMAE GERKTALEMV QAAGTDRHCV TFVLHEEDHT
60 70 80 90 100
LGNSLRYMIM KNPEVEFCGY TTTHPSESKI NLRIQTRGTL PAVEPFQRGL
110 120 130
NELMNVCQHV LDKFEASIKD YKDQKASRNE STF
Length:133
Mass (Da):15,237
Last modified:November 1, 1999 - v1
Checksum:i715DAEF2B22B1C76
GO
Isoform 2 (identifier: Q9Y2S0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     11-133: ISGLKTSMAE...QKASRNESTF → AIEELLKEAK...DKYEKRSNRR

Show »
Length:122
Mass (Da):14,332
Checksum:iF6F1FAF28BB89E3A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471E → K in TCS2. 1 Publication
VAR_064892
Natural varianti50 – 501T → I in TCS2. 1 Publication
VAR_064893
Natural varianti51 – 511L → R in TCS2. 1 Publication
VAR_064894
Natural varianti52 – 521G → E in TCS2. 1 Publication
VAR_064895
Natural varianti56 – 561R → C in TCS2. 1 Publication
VAR_064896
Natural varianti82 – 821L → S in TCS2. 1 Publication
VAR_064897
Natural varianti99 – 991G → S in TCS2. 1 Publication
VAR_064898

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei11 – 133123ISGLK…NESTF → AIEELLKEAKRGKTRAETMG PMGWMKCPLASTNKRFLINT IKNTLPSHKEQDHEQKEGDK EPAKSQAQKEENPKKHRSHP YKHSFRARGSASYSPPRKRS SQDKYEKRSNRR in isoform 2. 2 PublicationsVSP_035416Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077044 mRNA. Translation: AAD27777.1.
AK311833 mRNA. Translation: BAG34775.1.
AL136439 Genomic DNA. Translation: CAI16933.1.
AL136439 Genomic DNA. Translation: CAI16934.1.
CH471075 Genomic DNA. Translation: EAX08416.1.
BC000889 mRNA. Translation: AAH00889.1.
BC015319 mRNA. Translation: AAH15319.1.
BC018528 mRNA. Translation: AAH18528.1.
CCDSiCCDS9324.1. [Q9Y2S0-2]
CCDS9325.1. [Q9Y2S0-1]
RefSeqiNP_001193488.1. NM_001206559.1.
NP_057056.1. NM_015972.3. [Q9Y2S0-1]
NP_689918.1. NM_152705.2. [Q9Y2S0-2]
XP_005266469.1. XM_005266412.1. [Q9Y2S0-1]
XP_005266471.1. XM_005266414.1. [Q9Y2S0-2]
UniGeneiHs.507584.
Hs.735744.

Genome annotation databases

EnsembliENST00000302979; ENSP00000302478; ENSG00000186184.
ENST00000399697; ENSP00000382604; ENSG00000186184. [Q9Y2S0-2]
GeneIDi51082.
KEGGihsa:51082.
UCSCiuc001uro.3. human. [Q9Y2S0-1]
uc001urp.3. human. [Q9Y2S0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077044 mRNA. Translation: AAD27777.1.
AK311833 mRNA. Translation: BAG34775.1.
AL136439 Genomic DNA. Translation: CAI16933.1.
AL136439 Genomic DNA. Translation: CAI16934.1.
CH471075 Genomic DNA. Translation: EAX08416.1.
BC000889 mRNA. Translation: AAH00889.1.
BC015319 mRNA. Translation: AAH15319.1.
BC018528 mRNA. Translation: AAH18528.1.
CCDSiCCDS9324.1. [Q9Y2S0-2]
CCDS9325.1. [Q9Y2S0-1]
RefSeqiNP_001193488.1. NM_001206559.1.
NP_057056.1. NM_015972.3. [Q9Y2S0-1]
NP_689918.1. NM_152705.2. [Q9Y2S0-2]
XP_005266469.1. XM_005266412.1. [Q9Y2S0-1]
XP_005266471.1. XM_005266414.1. [Q9Y2S0-2]
UniGeneiHs.507584.
Hs.735744.

3D structure databases

ProteinModelPortaliQ9Y2S0.
SMRiQ9Y2S0. Positions 22-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119272. 26 interactions.
DIPiDIP-27598N.
IntActiQ9Y2S0. 15 interactions.
MINTiMINT-1149665.
STRINGi9606.ENSP00000302478.

PTM databases

PhosphoSiteiQ9Y2S0.

Polymorphism and mutation databases

BioMutaiPOLR1D.

2D gel databases

SWISS-2DPAGEQ9Y2S0.

Proteomic databases

MaxQBiQ9Y2S0.
PaxDbiQ9Y2S0.
PeptideAtlasiQ9Y2S0.
PRIDEiQ9Y2S0.

Protocols and materials databases

DNASUi51082.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302979; ENSP00000302478; ENSG00000186184.
ENST00000399697; ENSP00000382604; ENSG00000186184. [Q9Y2S0-2]
GeneIDi51082.
KEGGihsa:51082.
UCSCiuc001uro.3. human. [Q9Y2S0-1]
uc001urp.3. human. [Q9Y2S0-2]

Organism-specific databases

CTDi51082.
GeneCardsiGC13P028194.
GeneReviewsiPOLR1D.
HGNCiHGNC:20422. POLR1D.
HPAiHPA039337.
MIMi613715. gene.
613717. phenotype.
neXtProtiNX_Q9Y2S0.
Orphaneti861. Treacher-Collins syndrome.
PharmGKBiPA134914527.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1761.
GeneTreeiENSGT00550000075160.
HOGENOMiHOG000179862.
HOVERGENiHBG001176.
InParanoidiQ9Y2S0.
KOiK03020.
OMAiSSFSIME.
OrthoDBiEOG7J9VRX.
PhylomeDBiQ9Y2S0.
TreeFamiTF103035.

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

ChiTaRSiPOLR1D. human.
GeneWikiiPOLR1D.
GenomeRNAii51082.
NextBioi53727.
PROiQ9Y2S0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2S0.
CleanExiHS_POLR1D.
ExpressionAtlasiQ9Y2S0. baseline and differential.
GenevisibleiQ9Y2S0. HS.

Family and domain databases

InterProiIPR009025. RBP11-like_dimer.
IPR008193. RNA_pol_Rpb11_13-16kDa_CS.
[Graphical view]
SUPFAMiSSF55257. SSF55257. 1 hit.
PROSITEiPS01154. RNA_POL_L_13KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human RNA polymerase I 16-kDa subunit."
    Ye M., Zhang Q., Fu G., Zhou J., Yu Y., Shen Y., Wu J., He K., Chen S., Mao M., Chen Z.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] (ISOFORM 2).
    Tissue: Cerebellum.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(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: Cervix, Colon and Eye.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-9 AND 88-98, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: VARIANTS TCS2 LYS-47; ILE-50; ARG-51; GLU-52; CYS-56; SER-82 AND SER-99.

Entry informationi

Entry nameiRPAC2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2S0
Secondary accession number(s): Q5TBX2, Q96BR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 138 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 13
    Human chromosome 13: 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.