wanglab/gogpt-training-data huggingface dataset:
Protein: Clathrin coat assembly protein AP180 (91 kDa synaptosomal-associated protein) (Clathrin coat-associated protein AP180) (Phosphoprotein F1-20) (Q61548)
Organism: Mus musculus (Mouse)
Function: Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats.
Subcellular location: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Interaction partners:
- Epsin-1
- Epidermal growth factor receptor substrate 15
- Clathrin heavy chain 1
- Epsin-3
- Vesicle-associated membrane protein 2
- Intersectin-2
- AP-2 complex subunit alpha-2
- Synaptojanin-1
- Intersectin-1
- Clathrin interactor 1
Sequence:
MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGAAAGAAAPVVPPSGGATAWGDLLGEDSLAALSSVPCEAPISDPFAPEPSPPTTTTEPASASASTTTAVTAVTTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAAPKPDAAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSGASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPSFEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPSGQPAPVSMVPPSPAMAASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGFGMPPSGTGMTMMSQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL
Protein: Mitogen-activated protein kinase, putative (EC 2.7.1.-) (Q580Z7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSKGEELMQELIVELREMNSRYTVHRFLSSGSYGAVFAGVDESDLPVAIKRVFNTISEGRTINILSDPFLCKRVLREIMLLNHFHHPNILGLKNMFIHLQPPGQHKLYLVTDLMRTDLAQVIHDKRIDISPQHIRFFMYHIILGLHVLHEAGVVHRDLHPGNVLVSENNDITICDFNLAREDTQDPNKTHYVTHRWYRAPELVMQFKGFTKLVDMWSAGCVMGELFNRRALFRGSTFYNQLDKIVEVVGAPTEEDHLDMFSSSQARNYLRNALSHCKPRPWCDVVPTADAEAIDLLSRMLEFNPARRISAEQALQHPYFASLYDPLDLTEACSGPFHFPEVSDIFSMHQMFLAEVRGFEARRLKRENIIQQRLALSNGTTNAKEVLGCDHMLRTHSLMEVSDLPTSMP
Protein: Gap junction alpha-1 protein (Connexin-43) (Cx43) (Q29101)
Organism: Sus scrofa (Pig)
Function: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract. May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD is dependent on TMEM65. {ECO:0000250|UniProtKB:P23242}.
Interaction partners:
- Zona occludens protein 1
- Tyrosine-protein kinase
- Mitogen-activated protein kinase
- Tubulin beta chain
- Cell division cycle 2
- Gap junction protein
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Tubulin alpha-1B chain
- Tubulin beta chain
Sequence:
MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVEMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYAFFKGVKDRVKGKSDPYHATTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRMGQAGSTISNSHAQPFDFPDDNQNSKKLDAGHELQPLAIVDQRPSSRASSRASSRPRPDDLEI
Protein: HUWE1-associated protein modifying stress responses (Telomere attrition and p53 response 1 protein) (A2BE76)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as a central player within a network of stress response pathways promoting cellular adaptability. Functions as a negative regulator of TP53/P53 in the cellular response to telomere erosion and probably also DNA damage.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q14CZ0}. Cytoplasm {ECO:0000250|UniProtKB:Q14CZ0}.
Interaction partners:
- Protein LSM12 homolog A
- Protein LSM12 homolog B
- MOB-like protein phocein
- Translocon-associated protein subunit beta
Sequence:
MEEKKEEGEAEIQEHGPEHWFSKWERQCLAEAEQEEPAEEETDQSQQKLWHLFQNSATAVAQLYKDRVCQQQQGLSLWVPFQNAATAVTNLYKESVDAHQRSYELGIQIGHQRRNKDVLAWVKKRRRTIRREDLISFLCGKAPPPRSSRAPPRLAMVSPSRSTPSETSSSVETDLQPFREAIALHGLSGAMASISMRSGAPGSPTHLSASSAPSRRRNGLHDVDLNTFIAEEMALHLDNGTRKRSSAQCNDVITDSPTHKRNRMI
Protein: LLGL scribble cell polarity complex component 2 (Lethal(2) giant larvae protein homolog 2) (Protein penner) (Q7SZE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Essential for hemidesmosome formation and maintenance of the cytoskeleton elements as well as cellular morphology in the basal epidermis during development. Also involved in regulating growth of the basal epidermis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Protein kinase C iota type
- Protein kinase C
- Protein scribble homolog
- Discs large homolog 1-like protein
- LLGL scribble cell polarity complex component 1.
- Par-6 family cell polarity regulator gamma b
- Par-6 partitioning defective 6 homolog beta
- Par-6 family cell polarity regulator alpha.
- Par-6 family cell polarity regulator gamma a.
Sequence:
MKRFRRHGHESQRDKHKQDLYQFNKTVEHGFPHQPSALGFSPSLELLAIGTRSGAIKLYGAPGVEFMGLHDENAAVTQVHFLPNQVELVTLLEDNSLHMWTLRAHNSMCELLEIGRFTLSGPPGAIPSVTRVTAVLAHSSGELLLLGTEGGHVFVVEVPGFRELEENNISVEDVQNRVPEDYVGRRNLESVETLHENPLNPRQVLIGYSRGLMVLWDLDRQRPVQHFLGTQQLESVWWMEDGESILSSHSDGSYCQWTVTGEDPQTEPEKQETPYGAFPCKAISKIIQLPSKQGPPFLIFSGGMPRASYGDRHCISVIHSKTHEALDFTSRIIDFFVIREGENHKGEPSALVVLVEEELVVVDLQTEGWPVIQTPYLVPLHCSAITCSHHVSSIPLKLWERVQAAGAHQNTHYSRKPWPINGGKNLAPDPPQRDLLLTGHEDGTVRFWDASGVCLYPMYKLSTAGVFHTDADPNDNMNQGSEGEWPPFRKVGCFDPYSDDPRLGIQKIHLCKYSGYLTVAGTAGQILVLELNDEAAEQMVEATVVDLLQGQEGFRWKGQARLDVREEPVLFPPGFQPFALVQCQPPAVVTAIALHSEWKLVGFGTSHGFGLYDYNQRNNIMVKCTLNPSDQMAMEGPLSRVKSIKKSLRQSFRRIRRSRVSMRKHHTNNAAKLQEINARLEAEALQEMELAPVQRKIEARSSDDSFTGLVRTLYFADTFVSDSSHSTPSLWAGTNGGAVFAYVLRVPPQERRAEDPVTAHAAKEIQLMHRAPVVGLVVLDGKGAPLPEPLEVAHDLARSPEMHGSHHLLVVSEEQFKLFTLPKVSSKSKLKLTAVDGSRVRRVGVAWFGSRTDEQLESCLVVLTNQGELHVISLPSIKMLVHYPCIRREDVSGIASCVFTKYGQGFYLISPSEFERFSLSTRWVVQPHCLVEPPLQMRSKSPSSPVHRDLPDGVPTEHRNFKGDSEGYENSARQVMEHALLNDESVLQEIQKSLEGDQTTFLENNLKTKPKAGNVLSNGD
Protein: alpha-amylase (EC 3.2.1.1) (Q8N0R0)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGLLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYRMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAKL
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (P13051)
Organism: Homo sapiens (Human)
Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:15967827, ECO:0000269|PubMed:17101234, ECO:0000269|PubMed:9016624, ECO:0000269|PubMed:9753728}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:15967827, ECO:0000269|PubMed:17101234, ECO:0000269|PubMed:22521144, ECO:0000269|PubMed:9016624, ECO:0000269|PubMed:9753728}. Note=Localizes to S-phase replication foci. {ECO:0000269|PubMed:22521144}.
Interaction partners:
- Replication protein A 32 kDa subunit
- DDB1- and CUL4-associated factor 1
- DNA repair nuclease/redox regulator APEX1
- Single-strand selective monofunctional uracil DNA glycosylase
- DNA damage-binding protein 1
- DNA ligase 1
- Single-stranded DNA cytosine deaminase
- G/T mismatch-specific thymine DNA glycosylase
- DNA repair protein REV1
- DNA repair protein XRCC1
Sequence:
MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL
Protein: Androglobin (G3UZ78)
Organism: Mus musculus (Mouse)
Function: Required for sperm flagellum formation and maturation of elongating spermatids, thus playing an essential role in male fertility. Contributes to in vitro proteolytic cleavage of SEPT10 in a calmodulin-dependent manner.
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:35700329}. Note=Expressed within the midpiece and along the whole sperm flagellum (PubMed:35700329). Detected in the annulus of the sperm flagellum in S12 and S15 spermatids and mature sperm (PubMed:35700329). {ECO:0000269|PubMed:35700329}.
Interaction partners:
- Neuroglobin
- Cytoglobin
- Myoglobin
Sequence:
MASKQAKRKEVHRINSAHGSDKSKDLYHFGSNVPPGSFEQKKGKFPIWPEWSEADINAEKWDAGKGGKEKDKTAKSPIFHFFEDPEGKIELPQSLKVFSWKRPQDFIFSRTPVVVKNEITFDLFSPNEHLLCSELMRWIISEIYAVWKIFNGGILSNYHKGNLGELPILPWKPWEHIYSLCKAVKGHVPLFNSYGKYVVKLYWMGCWRKITVDDFLPFDEENNLLLPATSYEFELWPMLLSKAIIKLANVDVHVAHRRELGELTVIHALTGWLPEVIPLHPAYVDRVWELLKEILPEFKLTEEPSSESKITTIDNKLKEATKENKDGKDGKNGKDLKDGKDMKDGKDGKDGKDGKDGKDGKDEKADARDLGKKNKKDGEKEKEKFKFSLHGSRPSSDVQYSMQSLSECSSAIQLPHMVVYATFTPLYLFENKIFSLEKMANSAEKLREYGLSHICSHPVLVTRSRSCPLVSPPKPPPLPAWKLIRHKKETVITDEAQDAVPKKPEQFLEISSPFLNYRMTPFTIPTETHFVQSVIKKGTPLGSSLPPLVENDLVASTSQGEMSIVNGNQSQGNIALQITLGKDEPSEPALADFHQLEATSLDRDLISLTTATLDKSQEELAINEGVAKEIWLDFEDFCVCFHHIYIFHKPHSYCLNFQKSEFKFVEERVPYYLFVDSLKPIELLVCFSALVRWGESGALTKDSPPVEPGLLTAEAITWKSLKPLSVVLRIHTYATKASVVRLPAGRHMLLFNAYSPVGHAIHVCSMTTFVIGDEDIVLPNFEPESYRFTEQSIIIMKAIGNVIANFKDKGKLPAALRDLQAAHYPIPLNNKELTAQHFRVFHISLWRLMKKSQVAKPPSNFKFAFRAMVFDTDLLDSFSEDVSLAEWVDLKYSTPINEKEYTSEEIAAAVKIQSMWKGCYVRLLMKARKPETKENVTVADTLQKIWAVLEMNLEQYALSLLRLMFKSKCKSMESYPCYQDEETKLAFADHTVNYADQPPNSWFIVFREIFLVPQDMIILPKVYTTLPICILHVINNDTLEQVPKVFQKVVPFLYTKNKKGYTFVAEAYTGDTFVSGARWKLRLIGSYNPLPFLARDSPCNTFSIKEIRDYYIPNDRKILFRYSIKVTVAQSITIQVRTSKPDTFIKLQVLESEEVITSTVGKGQAVIPAFYFLGNEKALSSQSSKQVLLSHPSPKKDPEVLTKKKSGQPGQKSFKGRSGGGLTDTGMPLLEEEILNIPTLEENSSTPQQCYKYIIQCLVLFNSWPLNETQLTFVQALKDMEKMDIKEKHEEPAPMGSPDSHAVSEGQKSVGVPKTTRKGKEKSAEKEKLAKEKQAPRFEPQQVQMPTAVHSQQEDPNKPYWILRLVSEHTDSDYVDVKKDTERADEIRAMKQAWETTEPGRAIKAAQARLKYLTQFIKKPVTTDTTTSAPSPETLSVSQSQTKSSEEGELDTGKYADIKELPPNAAGSVLWKKWQMTKTITSLTKFTSSESVPKEEPPQKEIPVVRQRSPTILETSPQQIRKALEFLDFSHYVRKTAAEAVLQTEELNKQQAMQKAEEIHQFRQHRSRILSIRDIDQEERFKQKDEVLEMYGEMRDSVDEARQKILDIREVYRNKLLEAERLRMEALAAQEAAVKIEIEKKSPASDSQKKKKVGKKK
Protein: ADP-ribosylation factor-like protein 6 (A0A0B4LFW0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGMLHNLADLIKIKKDKMTILVLGLNNSGKSSIINHFKKSSEQTSIVVPTVGFMVEQFYSMSGVSIKAIDMSGATRYRNLWEHQFKNCHGIIYVIDSSDRMRFVVVKDELDLVLQHPDLCNRIVPILFYGNKMDMEDSLSSVKIAAALRLENIKDKPWHICSSSAISGEGLGEGVQWLIQQMRFAMLNNKNAAKSRSKHSK
Protein: Probable mitochondrial-processing peptidase subunit alpha (Alpha-MPP) (Inactive zinc metalloprotease alpha) (O94745)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable mitochondrial-processing peptidase subunit beta
- Cytochrome b-c1 complex subunit 7
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- Mitochondrial intermediate peptidase
- Intermediate cleaving peptidase 55
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
Sequence:
MSFLTTPKMLSEYQCLKNIGFSHKTVLKRRLFRKECTPALKSFYSTQDPALNEVRTEKLKNGVTYVCDPRPGHFSGLGVYVKAGSRYETKKFSGVSHFMDRLAFQATERTPVGEMKAKLENLGGNYMCSTSRESMIYQAAVFNDDVKSMSKLLAETVLAPKIQEDDLVHYRDSIIYENSELWTKPDALLGEFAHVTAFQNNTLGNCLLCTPDKVNGITATSIREYLKYFYRPEHLTLAYAGIPQEIAKEITKELYGHLPSSSLPPLEAIPSHYTGGFMGIKKSEAPPVPYQQEFTHVVIAMEGLPVTDPDIYALACLQFLLGGGGSFSAGGPGKGMYSRLYLNVLNQYPWVETCMAFNHSYTDSGLFGMFVTILDDAAHLAAPLIIRELCNTVLSVTSEETERAKNQLKSSLLMNLESRMISLEDLGRQIQTQNGLYITPKEMIEKIDALTPSDLSRVARRVLTGNVSNPGNGTGKPTVLIHGNVDEVGDVFALCKKAGIGH
Protein: Small G protein signaling modulator 1 (RUN and TBC1 domain-containing protein 2) (Q8BPQ7)
Organism: Mus musculus (Mouse)
Function: Interacts with numerous Rab family members, functioning as Rab effector for some, and as GTPase activator for others. Promotes GTP hydrolysis by RAB34 and RAB36. Probably functions as GTPase effector with RAB9A and RAB9B; does not stimulate GTP hydrolysis with RAB9A and RAB9B.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:17509819}. Cytoplasm {ECO:0000269|PubMed:25220469}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25220469}; Peripheral membrane protein {ECO:0000269|PubMed:25220469}. Note=Recruited to cytoplasmic vesicle membranes via its interaction with Rab family members, such as RAB9A. {ECO:0000269|PubMed:25220469}.
Interaction partners:
- Ras-related protein Rab-9A
Sequence:
MASVPAEAETRQRLLRTVKKEVKQIMEEAVTRKFVHEDSSHIISFCAAVEACVLHGLRRRAAGFLRSNKIAALFMKVGKGFPPAEELSRKVQELEQLIESARNQIQGLQENVRKLPKLPNLSPLAIKHLWIRTALFGRVLDKIVHYLVENSSKYYEKEALLMDPVDGPILASLLVGPCALEYTKMKTADHFWTDPSADELVQRHRIHSSHLRQDSPTKRPALCIQKRHSSGSMDDRPSISARDYVESLHQDSRATLLYGKNNVLVQPRDDMEAVPGYLSLHQTADVMTLKWTPNQLMNGSVGDLDYEKSVYWDYAVTIRLEEIVYLHCHQQVDSGGTVVLVSQDGIQRPPFRFPKGGHLLQFLSCLENGLLPHGQLDPPLWSQRGKGKVFPKLRKRSPQGSSESTSSDKEDDEATDYVFRIIYPGTQSEFVPQDLMDVSMNNLPPLWQPSPRKSSCSSCSQSGSADGGSTNGCNHERAPLKLLCDNMKYQILSRAFYGWLAYCRHLSTVRTHLSALVNHMIVSPDLPCDAGQGLTASIWEKYIQDSTTYPEQELLRLIYYGGVQPEIRRAVWPFLLGHYQFGMTEMERKEVDEQIHACYAQTMSEWLGCEAIVRQRERESHAAALAKCSSGASLDSHLHRMLHRDSTISNESSQSCSSGRQNLRLQSDSSSSTQVFESVDEVEQTEAEGRSEEKHPKIPNGNPANGTCSPDSGHPSSHNFSSGLSEHSEPSLSTEDSVLDAQRSLPAVFRPGDSSVEDGQSSEATTSRDEAPREELAVQDSLESDLLANESLEEFMSIPGSLDVALPEKDGAVMDGWPGEADKPSRADSEDNLSEEPEMESLFPALASLAVTSSANNEASPVSSSGVTYSPELLDLYTVNLHRIEKDVQRCDRSYWYFTAANLEKLRNIMCSYIWQHIEIGYVQGMCDLLAPLLVILDDEALAFSCFTELMKRMNQNFPHGGAMDTHFANMRSLIQILDSELFELMHQNGDYTHFYFCYRWFLLDFKRELVYDDVFSVWETIWAAKHVSSAHYVLFIALALVEVYRDIILENNMDFTDIIKFFNEMAERHNAKQILQLARDLVHKVQILIENK
Protein: Uracil-DNA glycosylase, mitochondrial (AtUNG) (UDG) (EC 3.2.2.27) (Q9LIH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. More active on U:G, U:T and U:C mispairs than on U:A pairs. Highly specific for uracil and no activity with 5-substituted uracil or cytosine derivatives. Required for initiation of base excision repair (BER) of uracil.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19625491}.
Interaction partners:
- DNA-
- N-glycosylase/DNA lyase OGG1
- DDB1- and CUL4-associated factor homolog 1
- Formamidopyrimidine-DNA glycosylase
- DNA-
- Endonuclease III homolog 1, chloroplastic
- Cytidine deaminase 2
- Cytidine deaminase 5
- Cytidine deaminase 7
- Cytidine deaminase 6
Sequence:
MASSTPKTLMDFFQPAKRLKASPSSSSFPAVSVAGGSRDLGSVANSPPRVTVTTSVADDSSGLTPEQIARAEFNKFVAKSKRNLAVCSERVTKAKSEGNCYVPLSELLVEESWLKALPGEFHKPYAKSLSDFLEREIITDSKSPLIYPPQHLIFNALNTTPFDRVKTVIIGQDPYHGPGQAMGLSFSVPEGEKLPSSLLNIFKELHKDVGCSIPRHGNLQKWAVQGVLLLNAVLTVRSKQPNSHAKKGWEQFTDAVIQSISQQKEGVVFLLWGRYAQEKSKLIDATKHHILTAAHPSGLSANRGFFDCRHFSRANQLLEEMGIPPIDWQL
Protein: Spore membrane assembly protein 2 (Q04658)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore and ascus formation. Required for the efficient assembly of the precursors of the prospore membrane to a continuous prospore membrane.
Subcellular location: Prospore membrane {ECO:0000269|PubMed:17298976}; Multi-pass membrane protein {ECO:0000269|PubMed:17298976}. Endoplasmic reticulum {ECO:0000269|PubMed:17298976}. Note=Localizes to prospore membrane, and accumulates in the endoplasmic reticulum in vegetative and sporulating ERV14-deleted cells.
Interaction partners:
- Sporulation-specific protein 77
- ER-derived vesicles protein ERV15
- Subtilase-type proteinase RRT12
- Uncharacterized protein YOR376W-A
Sequence:
MLFPKRLIVWGVLLILSLSQFVLYLPATTCTNSKGLRLCAPQFTITVIGGSSTANEFIASVREFLRLISYLTIDMGWSNEFTDPSVYEDENLVDTFQPDKVFELNYFGFCKRSNKSKVYCTSNENYGMDVLEVLVRDVGIQLGNISTTRSNETKKFGDSLVLTYRLALTSIRDFLKHDKHTGNALSKALIGSPDPNVKGVSPTKNYLKGVNLAFILMMFNGMVFYFAVLEIIVGFLSICVVSAFGGALSVGKRHRLFPMLLKSSSSILVVIATLTILCNIVYLIALKTLEPEEVTDVGSDNAAVHTTGWELLKVNVGSGFIMGLARYAIQWVLLVLAFLAANHYKAKPKKSDKYTEDTSNSPSPDLMEK
Protein: C2H2-type domain-containing protein (Q584W8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDLEKLRACCRAVVRRQRNNATLDFPCVICQQVIRGQHGSMEHYRVSHGICTSHFDDVADLNGFLSHLRSLLLPAGDTKFHCPVCGVSCDGEASLVAHAGQLGHTFWDARAIPTLAPFCITAVSSGNDELQHEEDDEVTGKVIDQAFYDEDEDEDEDEEWEEEPAMCLLCDTTSHNCLLHMKEAHSFDFVAAVQQHEGVNDVYDVIRIVNIIRGCVADGTCPHHYGEDSPEAESCRHEIASSSLLSHLRYEPLHALPRAIPTGDKELIPRLVGDTFISSIVVGGNIKFGETKCQTGGDEGEDYPMVPTMMELAAKRLAKGGA
Protein: Cellular tumor antigen p53 (G1K2L5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}.
Interaction partners:
Sequence:
MAQNDSQEFAELWEKNLISIQPPGGGSCWDIINDEEYLPGSFDPNFFENVLEEQPQPSTLPPTSTVPETSDYPGDHGFRLRFPQSGTAKSVTCTYSPDLNKLFCQLAKTCPVQMVVDVAPPQGSVVRATAIYKKSEHVAEVVRRCPHHERTPDGDNLAPAGHLIRVEGNQRANYREDNITLRHSVFVPYEAPQLGAEWTTVLLNYMCNSSCMGGMNRRPILTIITLETQEGQLLGRRSFEVRVCACPGRDRKTEESNFKKDQETKTMAKTTTGTKRSLVKESSSATLRPEGSKKAKGSSSDEEIFTLQVRGRERYEILKKLNDSLELSDVVPASDAEKYRQKFMTKNKKENRESSEPKQGKKLMVKDEGRSDSD
Protein: Miranda, isoform A (Q9VDR7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Maternal effect protein staufen
- Inscuteable
- Worniu
- Homeobox protein prospero
- Protein brain tumor
- Atypical protein kinase C
- Protein numb
Sequence:
MSFSKAKLKRFNDVDVAICGSPAASNSSAGSAGSATPTASSAAAAPPTVQPERKEQIEKFFKDAVRFASSSKEAKEFAIPKEDKKSKGLRLFRTPSLPQRLRFRPTPSHTDTATGSGSGASTAASTPLHSAATTPVKEAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDELLDKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEREKSYWRAELDKRQKLAENELIKIELEKQDVMVLLETTNDMLRMRDEKLQKCEEQLRNGIDYYIQLSDALQQQLVQLKQDMAKTITEKYNYQLTLTNTRATVNILMERLKKSDADVEQYRAELESVQLAKGALEQSYLVLQADAEQLRQQLTESQDALNALRSSSQTLQSEVSLKESLLHELLAGEAETLAKFNQIANSFQERIDGDAQLAHYHELRRKDETREAYMVDMKKALDEFATVLQFAQLELDNKEQMLVKVREECEQLKLENIALKSKQPGSASLLGTPGKANRSNTTDLEKIEDLLCDSELRSDCEKITTWLLNSSDKCVRQDTTSEINELLSAGKSSPRPAPRTPKAPHTPRSPRTPHTPRTPRSAASTPKKTVLFAGKENVPSPPQKQVLKARNI
Protein: DNA repair protein REV1 (EC 2.7.7.-) (Alpha integrin-binding protein 80) (AIBP80) (Rev1-like terminal deoxycytidyl transferase) (Q9UBZ9)
Organism: Homo sapiens (Human)
Function: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA polymerase zeta catalytic subunit
- Mitotic spindle assembly checkpoint protein MAD2B
- DNA polymerase eta
- DNA-directed DNA/RNA polymerase mu
- DNA polymerase delta subunit 3
- DNA polymerase iota
- DNA polymerase kappa
- Proliferating cell nuclear antigen
- Polyubiquitin-C
- Polyubiquitin-B
Sequence:
MRRGGWRKRAENDGWETWGGYMAAKVQKLEEQFRSDAAMQKDGTSSTIFSGVAIYVNGYTDPSAEELRKLMMLHGGQYHVYYSRSKTTHIIATNLPNAKIKELKGEKVIRPEWIVESIKAGRLLSYIPYQLYTKQSSVQKGLSFNPVCRPEDPLPGPSNIAKQLNNRVNHIVKKIETENEVKVNGMNSWNEEDENNDFSFVDLEQTSPGRKQNGIPHPRGSTAIFNGHTPSSNGALKTQDCLVPMVNSVASRLSPAFSQEEDKAEKSSTDFRDCTLQQLQQSTRNTDALRNPHRTNSFSLSPLHSNTKINGAHHSTVQGPSSTKSTSSVSTFSKAAPSVPSKPSDCNFISNFYSHSRLHHISMWKCELTEFVNTLQRQSNGIFPGREKLKKMKTGRSALVVTDTGDMSVLNSPRHQSCIMHVDMDCFFVSVGIRNRPDLKGKPVAVTSNRGTGRAPLRPGANPQLEWQYYQNKILKGKAADIPDSSLWENPDSAQANGIDSVLSRAEIASCSYEARQLGIKNGMFFGHAKQLCPNLQAVPYDFHAYKEVAQTLYETLASYTHNIEAVSCDEALVDITEILAETKLTPDEFANAVRMEIKDQTKCAASVGIGSNILLARMATRKAKPDGQYHLKPEEVDDFIRGQLVTNLPGVGHSMESKLASLGIKTCGDLQYMTMAKLQKEFGPKTGQMLYRFCRGLDDRPVRTEKERKSVSAEINYGIRFTQPKEAEAFLLSLSEEIQRRLEATGMKGKRLTLKIMVRKPGAPVETAKFGGHGICDNIARTVTLDQATDNAKIIGKAMLNMFHTMKLNISDMRGVGIHVNQLVPTNLNPSTCPSRPSVQSSHFPSGSYSVRDVFQVQKAKKSTEEEHKEVFRAAVDLEISSASRTCTFLPPFPAHLPTSPDTNKAESSGKWNGLHTPVSVQSRLNLSIEVPSPSQLDQSVLEALPPDLREQVEQVCAVQQAESHGDKKKEPVNGCNTGILPQPVGTVLLQIPEPQESNSDAGINLIALPAFSQVDPEVFAALPAELQRELKAAYDQRQRQGENSTHQQSASASVPKNPLLHLKAAVKEKKRNKKKKTIGSPKRIQSPLNNKLLNSPAKTLPGACGSPQKLIDGFLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT
Protein: DNA dC->dU-editing enzyme APOBEC-3Ca (EC 3.5.4.38) (Antiviral cytidine deaminase A3Ca) (Q4VDN5)
Organism: Felis catus (Cat) (Felis silvestris catus)
Function: DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (By similarity). Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (By similarity). Does not reduce infectivity of foamy feline virus, feline immunodeficiency virus or feline leukemia virus.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NRW3}. Cytoplasm {ECO:0000250|UniProtKB:Q9NRW3}.
Interaction partners:
Sequence:
MEPWRPSPRNPMDRIDPNTFRFHFPNLLYASGRKLCYLCFQVETEDYFSCDDSDRGVFRNKVHPWARCHAEQCFLSWFRDQYPYRDEYYNVTWFLSWSPCPTCAEEVVEFLEEYRNLTLSIFTSRLYYFWDPNYQEGLCKLWDAGVQLDIMSCDDFKHCWDNFVDHKGMRFQRRNLLKDYDFLAAELQEILR
Protein: Chromodomain helicase DNA binding protein 1 like (A0A0A0MSH9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFENETAKKVKLQNILSQLRKCVDHPYLFDGVEPEPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDEIDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMAWWESNNYQSFCLPSEESEPEDLENGEESSAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHSQSSSSSSRQLVP