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Protein

DNA repair protein complementing XP-C cells homolog

Gene

Xpc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by Rad23b and Rad23a. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity.
The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, Xpa, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the Xpc:Rad23b dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. Xpc:Rad23b induces a bend in DNA upon binding. Xpc:Rad23b stimulates the activity of DNA glycosylases Tdg and Smug1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • DNA repair Source: MGI
  • intra-S DNA damage checkpoint Source: MGI
  • mismatch repair Source: GO_Central
  • nucleotide-excision repair Source: MGI
  • nucleotide-excision repair, DNA damage recognition Source: MGI
  • regulation of mitotic cell cycle phase transition Source: MGI
  • response to drug Source: Ensembl
  • response to UV-B Source: MGI
  • UV-damage excision repair Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_290376. DNA Damage Recognition in GG-NER.
REACT_296832. Dual incision reaction in GG-NER.
REACT_314261. Formation of incision complex in GG-NER.
REACT_360954. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein complementing XP-C cells homolog
Alternative name(s):
Xeroderma pigmentosum group C-complementing protein homolog
p125
Gene namesi
Name:Xpc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103557. Xpc.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 930929DNA repair protein complementing XP-C cells homologPRO_0000218294Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931PhosphoserineBy similarity
Modified residuei126 – 1261PhosphoserineBy similarity
Modified residuei165 – 1651PhosphothreonineBy similarity
Modified residuei395 – 3951PhosphoserineBy similarity
Modified residuei397 – 3971PhosphoserineBy similarity
Modified residuei875 – 8751Phosphoserine2 Publications
Modified residuei876 – 8761Phosphoserine2 Publications
Modified residuei883 – 8831PhosphoserineBy similarity
Modified residuei895 – 8951PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated upon UV irradiation; the ubiquitination requires the UV-DDB complex, appears to be reversible and does not serve as a signal for degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP51612.
PaxDbiP51612.
PRIDEiP51612.

PTM databases

PhosphoSiteiP51612.

Expressioni

Gene expression databases

BgeeiP51612.
CleanExiMM_XPC.
GenevisibleiP51612. MM.

Interactioni

Subunit structurei

Component of the XPC complex composed of XPC, RAD23B and CETN2. Interacts with RAD23A; the interaction is suggesting the existence of a functional equivalent variant XPC complex. Interacts with TDG; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with SMUG1; the interaction is demonstrated using the XPC:RAD23B dimer. Interacts with DDB2. Interacts with CCNH, GTF2H1 and ERCC3 (By similarity).By similarity

Protein-protein interaction databases

BioGridi204605. 1 interaction.
IntActiP51612. 3 interactions.
MINTiMINT-4122377.
STRINGi10090.ENSMUSP00000032182.

Structurei

3D structure databases

ProteinModelPortaliP51612.
SMRiP51612. Positions 524-817.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni489 – 727239Interaction with RAD23BBy similarityAdd
BLAST
Regioni600 – 759160Minimal sensor domain involved in damage recognitionBy similarityAdd
BLAST
Regioni600 – 734135DNA-binding; preference for heteroduplex DNABy similarityAdd
BLAST
Regioni760 – 82465DNA-binding; preference for single stranded DNA; required for formation of stable nucleoprotein complexBy similarityAdd
BLAST
Regioni809 – 930122Interaction with ERCC2 and GTF2H1By similarityAdd
BLAST
Regioni840 – 85920Interaction with CETN2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi388 – 3936Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 173147Glu-rich (acidic)Add
BLAST
Compositional biasi355 – 39339Lys-rich (basic)Add
BLAST
Compositional biasi401 – 42424Arg/Lys-rich (basic)Add
BLAST
Compositional biasi425 – 45430Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi459 – 48628Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Belongs to the XPC family.Curated

Phylogenomic databases

eggNOGiCOG5535.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiP51612.
KOiK10838.
OMAiPQRTKAG.
OrthoDBiEOG7BW0J2.
PhylomeDBiP51612.
TreeFamiTF101242.

Family and domain databases

InterProiIPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018327. Rad4_beta-hairpin_dom2.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERiPTHR12135. PTHR12135. 1 hit.
PfamiPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00605. rad4. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P51612-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV
60 70 80 90 100
SQGKRKRGCS DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD
110 120 130 140 150
SPADCKKAKK HPKSKVVDQG TDEDDSEDDW EEVEELTEPV LDMGENSATS
160 170 180 190 200
PSDMPVKAVE IEIETPQQAK ERERSEKIKM EFETYLRRMM KRFNKEVQEN
210 220 230 240 250
MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV PLQDRDAYYL
260 270 280 290 300
SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL
310 320 330 340 350
ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP
360 370 380 390 400
ESHNKPTTSR RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE
410 420 430 440 450
EAEQKVQGRP HARKRRVAAK VSYKEESESD GAGSGSDFEP SSGEGQHSSD
460 470 480 490 500
EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ RGSQCEPSSF PEASSSSSGC
510 520 530 540 550
KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC VHGVVGQPVA
560 570 580 590 600
CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL
610 620 630 640 650
RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ
660 670 680 690 700
AIYPETAAVL GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV
710 720 730 740 750
KGFSNRARKA RLSEPQLHDH NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG
760 770 780 790 800
NVYLFLPSMM PVGCVQMTLP NLNRVARKLG IDCVQAITGF DFHGGYCHPV
810 820 830 840 850
TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN WKLLVRGLLI
860 870 880 890 900
RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR
910 920 930
EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL
Length:930
Mass (Da):104,522
Last modified:August 16, 2004 - v2
Checksum:i0C469AB21B4E4EE9
GO

Sequence cautioni

The sequence AAC52500.1 differs from that shown. Reason: Frameshift at positions 50, 52 and 61. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131K → N in BAB64540 (Ref. 2) Curated
Sequence conflicti84 – 841L → S in AAC52500 (PubMed:8604333).Curated
Sequence conflicti98 – 981F → L in AAC52500 (PubMed:8604333).Curated
Sequence conflicti101 – 1011S → L in AAC52500 (PubMed:8604333).Curated
Sequence conflicti148 – 1492AT → CP in BAB64540 (Ref. 2) Curated
Sequence conflicti165 – 1662TP → RG in AAC52500 (PubMed:8604333).Curated
Sequence conflicti196 – 2016EVQENM → GVHEDT in AAA82720 (PubMed:7675084).Curated
Sequence conflicti212 – 2121S → N in AAA82720 (PubMed:7675084).Curated
Sequence conflicti218 – 2181S → N in AAA82720 (PubMed:7675084).Curated
Sequence conflicti221 – 2233RQP → SQL in AAA82720 (PubMed:7675084).Curated
Sequence conflicti373 – 3753GKA → AKP in AAA82720 (PubMed:7675084).Curated
Sequence conflicti373 – 3731G → GS in AAC52500 (PubMed:8604333).Curated
Sequence conflicti397 – 3971S → R in AAC52500 (PubMed:8604333).Curated
Sequence conflicti454 – 4541E → K in BAB64540 (Ref. 2) Curated
Sequence conflicti458 – 4581R → C in AAA82720 (PubMed:7675084).Curated
Sequence conflicti497 – 4971S → C in AAC52500 (PubMed:8604333).Curated
Sequence conflicti614 – 6141E → K in AAC52500 (PubMed:8604333).Curated
Sequence conflicti621 – 6222KH → ND in AAC52500 (PubMed:8604333).Curated
Sequence conflicti683 – 6831W → R in AAC52500 (PubMed:8604333).Curated
Sequence conflicti712 – 7154LSEP → HLGA in AAC52500 (PubMed:8604333).Curated
Sequence conflicti751 – 7511N → K in AAC52500 (PubMed:8604333).Curated
Sequence conflicti777 – 7771R → H in AAC52500 (PubMed:8604333).Curated
Sequence conflicti797 – 7971C → S in AAC52500 (PubMed:8604333).Curated
Sequence conflicti921 – 9211A → P in AAC52500 (PubMed:8604333).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27398 mRNA. Translation: AAC52500.1. Frameshift.
AB071144 mRNA. Translation: BAB64540.1.
AK004713 mRNA. Translation: BAB23497.1.
AK028595 mRNA. Translation: BAC26023.1.
AK166981 mRNA. Translation: BAE39163.1.
U40005 mRNA. Translation: AAA82720.1.
CCDSiCCDS39569.1.
PIRiS70630.
RefSeqiNP_033557.2. NM_009531.2.
UniGeneiMm.2806.

Genome annotation databases

EnsembliENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
GeneIDi22591.
KEGGimmu:22591.
UCSCiuc009cyd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27398 mRNA. Translation: AAC52500.1. Frameshift.
AB071144 mRNA. Translation: BAB64540.1.
AK004713 mRNA. Translation: BAB23497.1.
AK028595 mRNA. Translation: BAC26023.1.
AK166981 mRNA. Translation: BAE39163.1.
U40005 mRNA. Translation: AAA82720.1.
CCDSiCCDS39569.1.
PIRiS70630.
RefSeqiNP_033557.2. NM_009531.2.
UniGeneiMm.2806.

3D structure databases

ProteinModelPortaliP51612.
SMRiP51612. Positions 524-817.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204605. 1 interaction.
IntActiP51612. 3 interactions.
MINTiMINT-4122377.
STRINGi10090.ENSMUSP00000032182.

PTM databases

PhosphoSiteiP51612.

Proteomic databases

MaxQBiP51612.
PaxDbiP51612.
PRIDEiP51612.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
GeneIDi22591.
KEGGimmu:22591.
UCSCiuc009cyd.2. mouse.

Organism-specific databases

CTDi7508.
MGIiMGI:103557. Xpc.

Phylogenomic databases

eggNOGiCOG5535.
GeneTreeiENSGT00390000005194.
HOGENOMiHOG000124671.
HOVERGENiHBG000407.
InParanoidiP51612.
KOiK10838.
OMAiPQRTKAG.
OrthoDBiEOG7BW0J2.
PhylomeDBiP51612.
TreeFamiTF101242.

Enzyme and pathway databases

ReactomeiREACT_290376. DNA Damage Recognition in GG-NER.
REACT_296832. Dual incision reaction in GG-NER.
REACT_314261. Formation of incision complex in GG-NER.
REACT_360954. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiXpc. mouse.
NextBioi302933.
PROiP51612.
SOURCEiSearch...

Gene expression databases

BgeeiP51612.
CleanExiMM_XPC.
GenevisibleiP51612. MM.

Family and domain databases

InterProiIPR004583. DNA_repair_Rad4.
IPR018026. DNA_repair_Rad4_subgr.
IPR018325. Rad4/PNGase_transGLS-fold.
IPR018326. Rad4_beta-hairpin_dom1.
IPR018327. Rad4_beta-hairpin_dom2.
IPR018328. Rad4_beta-hairpin_dom3.
[Graphical view]
PANTHERiPTHR12135. PTHR12135. 1 hit.
PfamiPF10403. BHD_1. 1 hit.
PF10404. BHD_2. 1 hit.
PF10405. BHD_3. 1 hit.
PF03835. Rad4. 1 hit.
[Graphical view]
SMARTiSM01030. BHD_1. 1 hit.
SM01031. BHD_2. 1 hit.
SM01032. BHD_3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00605. rad4. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the mouse XPC cDNA and genomic structure of the human XPC gene."
    Li L., Peterson C., Legerski R.
    Nucleic Acids Res. 24:1026-1028(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-930.
  2. "Molecular cloning of mouse XPC."
    Yokoi M., Hanaoka F.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Skin.
  4. "High susceptibility to ultraviolet-induced carcinogenesis in mice lacking XPC."
    Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.
    Nature 377:162-165(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 59-617.
    Strain: 129/Sv.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiXPC_MOUSE
AccessioniPrimary (citable) accession number: P51612
Secondary accession number(s): P54732
, Q3TKI2, Q920M1, Q9DBW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 16, 2004
Last modified: June 24, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.