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P51612

- XPC_MOUSE

UniProt

P51612 - XPC_MOUSE

Protein

DNA repair protein complementing XP-C cells homolog

Gene

Xpc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    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

    1. damaged DNA binding Source: Ensembl
    2. single-stranded DNA binding Source: Ensembl

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. DNA repair Source: MGI
    3. intra-S DNA damage checkpoint Source: MGI
    4. nucleotide-excision repair Source: MGI
    5. nucleotide-excision repair, DNA damage recognition Source: Ensembl
    6. response to drug Source: Ensembl
    7. response to UV-B Source: MGI

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_210532. DNA Damage Recognition in GG-NER.

    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: 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

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: MGI
    3. XPC complex Source: UniProtKB

    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 residuei875 – 8751Phosphoserine2 Publications
    Modified residuei876 – 8761Phosphoserine2 Publications
    Modified residuei883 – 8831PhosphoserineBy 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

    PaxDbiP51612.
    PRIDEiP51612.

    PTM databases

    PhosphoSiteiP51612.

    Expressioni

    Gene expression databases

    BgeeiP51612.
    CleanExiMM_XPC.
    GenevestigatoriP51612.

    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.

    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

    MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV    50
    SQGKRKRGCS DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD 100
    SPADCKKAKK HPKSKVVDQG TDEDDSEDDW EEVEELTEPV LDMGENSATS 150
    PSDMPVKAVE IEIETPQQAK ERERSEKIKM EFETYLRRMM KRFNKEVQEN 200
    MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV PLQDRDAYYL 250
    SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL 300
    ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP 350
    ESHNKPTTSR RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE 400
    EAEQKVQGRP HARKRRVAAK VSYKEESESD GAGSGSDFEP SSGEGQHSSD 450
    EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ RGSQCEPSSF PEASSSSSGC 500
    KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC VHGVVGQPVA 550
    CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL 600
    RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ 650
    AIYPETAAVL GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV 700
    KGFSNRARKA RLSEPQLHDH NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG 750
    NVYLFLPSMM PVGCVQMTLP NLNRVARKLG IDCVQAITGF DFHGGYCHPV 800
    TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN WKLLVRGLLI 850
    RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR 900
    EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL 930
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131K → N in BAB64540. 1 PublicationCurated
    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. 1 PublicationCurated
    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. 1 PublicationCurated
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS39569.1.
    PIRi S70630.
    RefSeqi NP_033557.2. NM_009531.2.
    UniGenei Mm.2806.

    3D structure databases

    ProteinModelPortali P51612.
    SMRi P51612. Positions 524-817.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204605. 1 interaction.
    IntActi P51612. 3 interactions.
    MINTi MINT-4122377.

    PTM databases

    PhosphoSitei P51612.

    Proteomic databases

    PaxDbi P51612.
    PRIDEi P51612.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032182 ; ENSMUSP00000032182 ; ENSMUSG00000030094 .
    GeneIDi 22591.
    KEGGi mmu:22591.
    UCSCi uc009cyd.2. mouse.

    Organism-specific databases

    CTDi 7508.
    MGIi MGI:103557. Xpc.

    Phylogenomic databases

    eggNOGi COG5535.
    GeneTreei ENSGT00390000005194.
    HOGENOMi HOG000124671.
    HOVERGENi HBG000407.
    InParanoidi P51612.
    KOi K10838.
    OMAi PQRTKAG.
    OrthoDBi EOG7BW0J2.
    PhylomeDBi P51612.
    TreeFami TF101242.

    Enzyme and pathway databases

    Reactomei REACT_210532. DNA Damage Recognition in GG-NER.

    Miscellaneous databases

    ChiTaRSi XPC. mouse.
    NextBioi 302933.
    PROi P51612.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51612.
    CleanExi MM_XPC.
    Genevestigatori P51612.

    Family and domain databases

    InterProi IPR004583. 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 ]
    PANTHERi PTHR12135. PTHR12135. 1 hit.
    Pfami PF10403. BHD_1. 1 hit.
    PF10404. BHD_2. 1 hit.
    PF10405. BHD_3. 1 hit.
    PF03835. Rad4. 1 hit.
    [Graphical view ]
    SMARTi SM01030. BHD_1. 1 hit.
    SM01031. BHD_2. 1 hit.
    SM01032. BHD_3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00605. rad4. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 112 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