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Protein

General transcription factor IIH subunit 3

Gene

GTF2H3

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

Functioni

Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Anchors XPB.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri268 – 28518C4-typeAdd
BLAST

GO - Molecular functioni

  • damaged DNA binding Source: ProtInc
  • metal ion binding Source: UniProtKB-KW
  • protein N-terminus binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: ProtInc
  • translation factor activity, RNA binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIH subunit 3
Alternative name(s):
Basic transcription factor 2 34 kDa subunit
Short name:
BTF2 p34
General transcription factor IIH polypeptide 3
TFIIH basal transcription factor complex p34 subunit
Gene namesi
Name:GTF2H3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:4657. GTF2H3.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: GO_Central
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29043.

Polymorphism and mutation databases

DMDMi50403772.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308General transcription factor IIH subunit 3PRO_0000119251Add
BLAST

Proteomic databases

MaxQBiQ13889.
PaxDbiQ13889.
PRIDEiQ13889.

PTM databases

PhosphoSiteiQ13889.

Expressioni

Gene expression databases

BgeeiQ13889.
CleanExiHS_GTF2H3.
ExpressionAtlasiQ13889. baseline and differential.
GenevisibleiQ13889. HS.

Organism-specific databases

HPAiHPA004844.
HPA053562.

Interactioni

Subunit structurei

One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with RARA; the interaction requires prior phosphorylation of RARA on 'Ser-369' which then enhances interaction of RARA with CDK7 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2H2C_2Q6P1K83EBI-6380459,EBI-8469755

Protein-protein interaction databases

BioGridi109222. 15 interactions.
DIPiDIP-787N.
IntActiQ13889. 2 interactions.
MINTiMINT-3028878.
STRINGi9606.ENSP00000445162.

Structurei

3D structure databases

ProteinModelPortaliQ13889.
SMRiQ13889. Positions 5-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TFB4 family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri268 – 28518C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5242.
GeneTreeiENSGT00390000013143.
HOGENOMiHOG000175900.
HOVERGENiHBG054271.
InParanoidiQ13889.
KOiK03143.
OMAiNAHLMQK.
PhylomeDBiQ13889.
TreeFamiTF314336.

Family and domain databases

InterProiIPR004600. TFIIH_Tfb4/p34.
[Graphical view]
PANTHERiPTHR12831. PTHR12831. 1 hit.
PfamiPF03850. Tfb4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00627. tfb4. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q13889-1) [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
MVSDEDELNL LVIVVDANPI WWGKQALKES QFTLSKCIDA VMVLGNSHLF
60 70 80 90 100
MNRSNKLAVI ASHIQESRFL YPGKNGRLGD FFGDPGNPPE FNPSGSKDGK
110 120 130 140 150
YELLTSANEV IVEEIKDLMT KSDIKGQHTE TLLAGSLAKA LCYIHRMNKE
160 170 180 190 200
VKDNQEMKSR ILVIKAAEDS ALQYMNFMNV IFAAQKQNIL IDACVLDSDS
210 220 230 240 250
GLLQQACDIT GGLYLKVPQM PSLLQYLLWV FLPDQDQRSQ LILPPPVHVD
260 270 280 290 300
YRAACFCHRN LIEIGYVCSV CLSIFCNFSP ICTTCETAFK ISLPPVLKAK

KKKLKVSA
Length:308
Mass (Da):34,378
Last modified:July 19, 2004 - v2
Checksum:iE739E2176CD6BAA5
GO
Isoform 2 (identifier: Q13889-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.

Note: No experimental confirmation available.
Show »
Length:267
Mass (Da):29,777
Checksum:i9415C0930FAADD34
GO

Sequence cautioni

The sequence CAA82909.1 differs from that shown. Reason: Frameshift at position 302. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 2. 1 PublicationVSP_055153Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298128 mRNA. Translation: BAG60408.1.
AK313200 mRNA. Translation: BAG36016.1.
AF548661 Genomic DNA. Translation: AAN40702.1.
AC117503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98426.1.
BC039726 mRNA. Translation: AAH39726.1.
BC047868 mRNA. Translation: AAH47868.2.
BC065250 mRNA. Translation: AAH65250.1.
Z30093 mRNA. Translation: CAA82909.1. Frameshift.
CCDSiCCDS61275.1. [Q13889-2]
CCDS9252.1. [Q13889-1]
PIRiS44455.
RefSeqiNP_001258795.1. NM_001271866.1.
NP_001258796.1. NM_001271867.1. [Q13889-2]
NP_001258797.1. NM_001271868.1.
NP_001507.2. NM_001516.4. [Q13889-1]
UniGeneiHs.355348.

Genome annotation databases

EnsembliENST00000228955; ENSP00000228955; ENSG00000111358. [Q13889-2]
ENST00000543341; ENSP00000445162; ENSG00000111358. [Q13889-1]
GeneIDi2967.
KEGGihsa:2967.
UCSCiuc001ufo.2. human. [Q13889-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK298128 mRNA. Translation: BAG60408.1.
AK313200 mRNA. Translation: BAG36016.1.
AF548661 Genomic DNA. Translation: AAN40702.1.
AC117503 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98426.1.
BC039726 mRNA. Translation: AAH39726.1.
BC047868 mRNA. Translation: AAH47868.2.
BC065250 mRNA. Translation: AAH65250.1.
Z30093 mRNA. Translation: CAA82909.1. Frameshift.
CCDSiCCDS61275.1. [Q13889-2]
CCDS9252.1. [Q13889-1]
PIRiS44455.
RefSeqiNP_001258795.1. NM_001271866.1.
NP_001258796.1. NM_001271867.1. [Q13889-2]
NP_001258797.1. NM_001271868.1.
NP_001507.2. NM_001516.4. [Q13889-1]
UniGeneiHs.355348.

3D structure databases

ProteinModelPortaliQ13889.
SMRiQ13889. Positions 5-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109222. 15 interactions.
DIPiDIP-787N.
IntActiQ13889. 2 interactions.
MINTiMINT-3028878.
STRINGi9606.ENSP00000445162.

PTM databases

PhosphoSiteiQ13889.

Polymorphism and mutation databases

DMDMi50403772.

Proteomic databases

MaxQBiQ13889.
PaxDbiQ13889.
PRIDEiQ13889.

Protocols and materials databases

DNASUi2967.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228955; ENSP00000228955; ENSG00000111358. [Q13889-2]
ENST00000543341; ENSP00000445162; ENSG00000111358. [Q13889-1]
GeneIDi2967.
KEGGihsa:2967.
UCSCiuc001ufo.2. human. [Q13889-1]

Organism-specific databases

CTDi2967.
GeneCardsiGC12P124118.
H-InvDBHIX0026378.
HGNCiHGNC:4657. GTF2H3.
HPAiHPA004844.
HPA053562.
MIMi601750. gene.
neXtProtiNX_Q13889.
PharmGKBiPA29043.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5242.
GeneTreeiENSGT00390000013143.
HOGENOMiHOG000175900.
HOVERGENiHBG054271.
InParanoidiQ13889.
KOiK03143.
OMAiNAHLMQK.
PhylomeDBiQ13889.
TreeFamiTF314336.

Enzyme and pathway databases

ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
REACT_1470. mRNA Capping.
REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
REACT_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
REACT_2089. RNA Polymerase II Promoter Escape.
REACT_2204. RNA Polymerase I Chain Elongation.
REACT_22107. RNA Polymerase II Pre-transcription Events.
REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
REACT_2222. Dual incision reaction in TC-NER.
REACT_257. Formation of incision complex in GG-NER.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_311. Dual incision reaction in GG-NER.
REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
REACT_6233. Transcription of the HIV genome.
REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
REACT_6253. RNA Polymerase II HIV Promoter Escape.
REACT_6319. Formation of the HIV-1 Early Elongation Complex.
REACT_6332. HIV Transcription Initiation.
REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
REACT_833. RNA Polymerase II Transcription Elongation.
REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
REACT_846. Formation of the Early Elongation Complex.
REACT_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiGTF2H3. human.
GenomeRNAii2967.
NextBioi11760.
PROiQ13889.
SOURCEiSearch...

Gene expression databases

BgeeiQ13889.
CleanExiHS_GTF2H3.
ExpressionAtlasiQ13889. baseline and differential.
GenevisibleiQ13889. HS.

Family and domain databases

InterProiIPR004600. TFIIH_Tfb4/p34.
[Graphical view]
PANTHERiPTHR12831. PTHR12831. 1 hit.
PfamiPF03850. Tfb4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00627. tfb4. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 1 AND 2).
  2. NIEHS SNPs program
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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] (ISOFORM 1).
    Tissue: Brain, Eye and Testis.
  6. "p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair."
    Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M., Moncollin V.
    EMBO J. 13:2393-2398(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-305 (ISOFORM 1), PROTEIN SEQUENCE OF 57-68; 78-97; 107-112; 127-132 AND 239-251 (ISOFORMS 1/2).
  7. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
    Kershnar E., Wu S.-Y., Chiang C.-M.
    J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.

Entry informationi

Entry nameiTF2H3_HUMAN
AccessioniPrimary (citable) accession number: Q13889
Secondary accession number(s): B2R819
, B4DNZ6, Q7L0G0, Q96AT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: July 19, 2004
Last modified: June 24, 2015
This is version 136 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. 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.