wanglab/gogpt-training-data huggingface dataset:
Protein: DNA-directed RNA polymerase III subunit RPC8 (RNA polymerase III subunit C8) (DNA-directed RNA polymerase III 25 kDa polypeptide) (RNA polymerase III subunit C25) (P35718)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA. The RPC25/RPC8-RPC17/RPC9 subcomplex may bind Pol III transcripts emerging from the adjacent exit pore during elongation.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MFILSKIADLVRIPPDQFHRDTISAITHQLNNKFANKIIPNVGLCITIYDLLTVEEGQLKPGDGSSYINVTFRAVVFKPFLGEIVTGWISKCTAEGIKVSLLGIFDDIFIPQNMLFEGCYYTPEESAWIWPMDEETKLYFDVNEKIRFRIEREVFVDVKPKSPKERELEERAQLENEIEGKNEETPQNEKPPAYALLGSCQTDGMGLVSWWE
Protein: Replication protein E1 (EC 3.6.4.12) (ATP-dependent helicase E1) (P06789)
Organism: Human papillomavirus type 18
Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000}.
Interaction partners:
Sequence:
MADPEGTDGEGTGCNGWFYVQAIVDKKTGDVISDDEDENATDTGSDMVDFIDTQGTFCEQAELETAQALFHAQEVHNDAQVLHVLKRKFAGGSTENSPLGERLEVDTELSPRLQEISLNSGQKKAKRRLFTISDSGYGCSEVEATQIQVTTNGEHGGNVCSGGSTEAIDNGGTEGNNSSVDGTSDNSNIENVNPQCTIAQLKDLLKVNNKQGAMLAVFKDTYGLSFTDLVRNFKSDKTTCTDWVTAIFGVNPTIAEGFKTLIQPFILYAHIQCLDCKWGVLILALLRYKCGKSRLTVAKGLSTLLHVPETCMLIQPPKLRSSVAALYWYRTGISNISEVMGDTPEWIQRLTIIQHGIDDSNFDLSEMVQWAFDNELTDESDMAFEYALLADSNSNAAAFLKSNCQAKYLKDCATMCKHYRRAQKRQMNMSQWIRFRCSKIDEGGDWRPIVQFLRYQQIEFITFLGALKSFLKGTPKKNCLVFCGPANTGKSYFGMSFIHFIQGAVISFVNSTSHFWLEPLTDTKVAMLDDATTTCWTYFDTYMRNALDGNPISIDRKHKPLIQLKCPPILLTTNIHPAKDNRWPYLESRITVFEFPNAFPFDKNGNPVYEINDKNWKCFFERTWSRLDLHEEEEDADTEGNPFGTFKLRAGQNHRPL
Protein: Peptide methionine sulfoxide reductase B7 (AtMSRB7) (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase) (Q8VY86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantiomer (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Peptide methionine sulfoxide reductase A3
- Peptide methionine sulfoxide reductase A2
- Peptide methionine sulfoxide reductase A4, chloroplastic
- Peptide methionine sulfoxide reductase A1
- Farnesoic acid carboxyl-O-methyltransferase
Sequence:
MAAMTAAAVPATGSFQKQDEEWRAVLSPEQFRVLRLKGTDKRGKGEFTKKFEEGTYSCAGCGTALYKSTTKFDSGCGWPAFFDAIPGAIKQTPEAGGRRMEITCAVCDGHLGHVFKGEGYSTPTDQRHCVNSVSLKFSSAGSSQ
Protein: Growth/differentiation factor 15 (GDF-15) (Macrophage inhibitory cytokine 1) (MIC-1) (G7PWZ3)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which constitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions. On hepatocytes, inhibits growth hormone signaling (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:29046435}. Note=Secreted in the plasma. {ECO:0000269|PubMed:29046435}.
Interaction partners:
- TGF-beta receptor type-2
- GDNF family receptor alpha like.
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Cyclin-J
- Macaca fascicularis brain cDNA clone: QflA-17230, similar to human twisted gastrulation homolog 1
- Adenosine receptor A1
- Neuromedin U receptor 1
- Zinc finger protein 300
- Heat shock protein beta-6
- NF-kappa-B-repressing factor
Sequence:
MPGQELKTLNGSQMLLVLLVLLWPPHGGAVSLAEASRASFPGPSDLHSEDSRFRELRKRYEDLLTRLRANQSWEDSNTDLIQAPEVRILTPEVRLGSGGHLHLRISRAVLPEGLPEACRIHRALFRLSPTASRSRDVTRPLRRQLRLARPQAPALHLRLSPPPSQSDQLLVKSSSSRPQLALHLRPRASRGRRRARARNGDRCPLGPGRCCRLHTVHASLEDLGWADWVLSPREVQVTMCIGACPSQFREANMHAQIKMNLHRLKPDTVPAPCCVPASYNPMVLIQKTDTGVSLQTYDDLLAKDCHCV
Protein: Striatin 4 (A0A0G2JX43)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMAAARAAQQRAQVAFLQGERKGQENLKTDLVRRIKMLEYALKQERAKYHKLKFGTDLNQGEKKADLSEQVSNGPVESVTLDNSPLVWKEGRQLLRQYLEEVGYTDTILDMRSKRVRSLLGRSLELNGAGEPVEGAPRASPGPGGLSGGESLLVKQIEEQIKRNAAGKDGKERLGGSVLEQIPFLQNCEDEDSDEDDELDSVQHKKQRVRLPSKALVPEMEDEDEEDDSEDAINEFDFLGSGEDGEGSPDPRRCASEGNPHELESRRVKLQGILADLRDVDGLPPKVTVPPPGTPQPRPHEDVFIMDTIGGGEVSLGDLADLTVTNDNDLSCDLSDSKDAFKKTWNPKFTLRSHYDGIRSLAFHHSQSALLTASEDGTLKLWNLQKAVTAKKNAALDVEPIHAFRAHRGPVLAVTMGSNSEYCYSGGADARIHSWKIPDLNMDPYDGYDPSVLSCVLEGHGDAVWGLAFSPTSQRLASCSADGTIRIWDPSSSGSSCLCTFPMAGEHGIPTSVAFTSTEPAHVVASFRSGDTVLYDLEAGGALLTLESRGSSGPTQINQVVSHPNQPLTITAHDDRGIRFLDNRTGKSVHSMVAHLDAVTCLAVDPNGVFLMSGSHDCSLRLWSLDNKTCVQEITAHRKKHEEAIHAVACHPSKALIASAGADALAKVFV
Protein: Keratin, type I cytoskeletal 18 (Cell proliferation-inducing gene 46 protein) (Cytokeratin-18) (CK-18) (Keratin-18) (K18) (P05783)
Organism: Homo sapiens (Human)
Function: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}.
Interaction partners:
- Keratin, type II cytoskeletal 8
- Desmoplakin
- Tumor necrosis factor receptor superfamily member 1B
- Keratin, type I cytoskeletal 19
- Cadherin-1
- Epidermal growth factor receptor
- 14-3-3 protein zeta/delta
- Protein LIAT1
- Epithelial cell adhesion molecule
- Plectin
Sequence:
MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASLENSLREVEARYALQMEQLNGILLHLESELAQTRAEGQRQAQEYEALLNIKVKLEAEIATYRRLLEDGEDFNLGDALDSSNSMQTIQKTTTRRIVDGKVVSETNDTKVLRH
Protein: Probable calcium-binding protein CML27 (Calmodulin-like protein 27) (Q9LE22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Obg-like ATPase 1
- Probable calcium-binding protein CML22
Sequence:
MASANPETAKPTPATVDMANPEELKKVFDQFDSNGDGKISVLELGGVFKAMGTSYTETELNRVLEEVDTDRDGYINLDEFSTLCRSSSSAAEIRDAFDLYDQDKNGLISASELHQVLNRLGMSCSVEDCTRMIGPVDADGDGNVNFEEFQKMMTSSSLLNSNGSAAPPST
Protein: Cytochrome c oxidase assembly factor 8 (COA8) (Apoptogenic protein 1, mitochondrial) (APOP-1) (Q96IL0)
Organism: Homo sapiens (Human)
Function: Required for cytochrome c complex (COX) IV assembly and function Protects COX assembly from oxidation-induced degradation, COX being the terminal component of the mitochondrial respiratory chain.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:25175347, ECO:0000269|PubMed:30552096}; Peripheral membrane protein {ECO:0000305|PubMed:30552096}; Matrix side {ECO:0000269|PubMed:30552096}.
Interaction partners:
Sequence:
MLPCAAGARGRGAMVVLRAGKKTFLPPLCRAFACRGCQLAPERGAERRDTAPSGVSRFCPPRKSCHDWIGPPDKYSNLRPVHFYIPENESPLEQKLRKLRQETQEWNQQFWANQNLTFSKEKEEFIHSRLKTKGLGLRTESGQKATLNAEEMADFYKEFLSKNFQKHMYYNRDWYKRNFAITFFMGKVALERIWNKLKQKQKKRSN
Protein: Putative galactosidae (Q8W4Z8)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
CTLGPLDEFGLQREPKWGHLKDVHRALSLCKRALFWGFPTTLKLGPDQQAIVWQQPGTSACAALLANNNTRLAQHVNFRGQDIRLPARSISVLPDCKTVVFNTQLVTTQHNSRNFVRSEIANKNFNWEMYREVPPVGLGFKFDVPRELFHLTKDTTDYAWYTTSLLLGRRDLPMKKNVRPVLRVASLGHGIHAYVNGEYAGSAHGSKVEKSFVCRELSSLKEGENHIALLGYLVGLPDSGAYMEKRFAGPRSITILGLNTGTLDISQNGWGHQVGTDGEKKKLFTEEGSKSVQWTKPDQGGPLTWYKGYFDAPEGDNPVAIVMTGMGKGMVWVNGRSIGRYWNNYLSPLKKPTQSEYHIPRAYLKPKNLIVLLEEEGGNPKDV
Protein: [Trp5]-bradykinin (P84774)
Organism: Lepisosteus osseus (Long-nosed gar) (Esox osseus)
Function: Induces smooth muscle dilation and contraction. May target bradykinin receptors (BDKRB).
Subcellular location: Secreted {ECO:0000269|PubMed:7651903}.
Interaction partners:
Sequence:
RPPGWSPFR
Protein: Cytochrome P450 2M1 (EC 1.14.14.1) (CYPIIM1) (LMC1) (Lauric acid omega-6-hydroxylase) (Q92088)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Has (omega-6)-hydroxylation activity toward lauric acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MDVLHILQTNFVSIIIGFVVIILLWMNRGKQSNSRLPPGPAPIPLLGNLLRMDVKAPYKLYMELSKKYGSVFTVWLGSKPVVVISGYQAIKDAFVTQGEEFSGRANYPVIMTVSKGYGVLVSSGKRSKDLRRFSLMTLKTFGMGRRSIEERVQEEAKMLVKAFGEYRDSVVNPKELLCNCVGNVICSIVFGHRFENDDPMFQLIQKAVDAYFNVLSSPIGAMYNMFPRIVWCFPGNHHEMFAIVNKAKVYIQEQAEIRLKTLNISEPQDFIEAFLVKMLEEKDDPNTEFNNGNMVMTAWSLFAAGTETTSSTLRQSFLMMIKYPHIQESVQKEIDEVIGSRVPTVDDRVKMPYTDAVIHEVQRYMDLSPTSVPHKVMRDTEFYNYHIPEGTMVLPLLSSVLVDPKLFKNPDEFDPENFLDENGVFKKNDGFFAFGVGKRACPGEALARVELFLFFTSVLQRFTFTGTKPPEEINIEPACSSFGRLPRSYDCYIKLRTEK
Protein: Mu-type opioid receptor (B8JHS2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Perikaryon {ECO:0000256|ARBA:ARBA00004484}.
Interaction partners:
- Pro-opiomelanocortin protein
- Proenkephalin a
- Prodynorphin.
Sequence:
MMENTGNISDLLYALSNPMVSNSSIFCRNFSNSSGLVNMNSSVCDRTPELDKSSTPVIVAIIITALYSIVCVMGLVGNVLVMYVIIRYTKMKTATNIYIFNLALADSLATSTLPFQSVNYLMGTWPFGDELCKIVMSIDYYNMFTSIFTLTTMSVDRYIAVCHPVKALDFRTPRNAKIVNVCNWILSSAIGLPVMVMASTTSDLHSNGIIDCTLLFPHPSWYWENLLKICVFIFAFIMPVLIITVCYGLMILRLKSVRMLSGSKEKDRNLRRITRMVLVVVAVFIVCWTPIHIFVIIKALVTIPNSLLQTITWHFCIALGYTNSCLNPVLYAFLDENFKRCFREFCVPSPSVLDLQNSTRSRNPQRDGQSSGHTVDRTNQQV
Protein: T-box transcription factor TBX6 (T-box protein 6) (O95947)
Organism: Homo sapiens (Human)
Function: T-box transcription factor that plays an essential role in the determination of the fate of axial stem cells: neural vs mesodermal. Acts in part by down-regulating, a specific enhancer (N1) of SOX2, to inhibit neural development. Seems to play also an essential role in left/right axis determination and acts through effects on Notch signaling around the node as well as through an effect on the morphology and motility of the nodal cilia (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- Mesoderm posterior protein 2
- Mesogenin-1
- Protein Wnt-3a
- Delta-like protein 1
- Fibroblast growth factor receptor 1
- T-box transcription factor T
- Homeobox protein MOX-1
- Protein ripply2
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Fibroblast growth factor 8
Sequence:
MYHPRELYPSLGAGYRLGPAQPGADSSFPPALAEGYRYPELDTPKLDCFLSGMEAAPRTLAAHPPLPLLPPAMGTEPAPSAPEALHSLPGVSLSLENRELWKEFSSVGTEMIITKAGRRMFPACRVSVTGLDPEARYLFLLDVIPVDGARYRWQGRRWEPSGKAEPRLPDRVYIHPDSPATGAHWMRQPVSFHRVKLTNSTLDPHGHLILHSMHKYQPRIHLVRAAQLCSQHWGGMASFRFPETTFISVTAYQNPQITQLKIAANPFAKGFRENGRNCKRERDARVKRKLRGPEPAATEAYGSGDTPGGPCDSTLGGDIRESDPEQAPAPGEATAAPAPLCGGPSAEAYLLHPAAFHGAPSHLPTRSPSFPEAPDSGRSAPYSAAFLELPHGSGGSGYPAAPPAVPFAPHFLQGGPFPLPYTAPGGYLDVGSKPMY
Protein: GATA zinc finger domain-containing protein 1 (Q1L8G7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of some chromatin complex recruited to chromatin sites methylated 'Lys-4' of histone H3 (H3K4me), with a preference for trimethylated form (H3K4me3).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8WUU5}.
Interaction partners:
- PHD finger protein 12
- PHD finger protein 12
- Mortality factor 4-like protein 1
- Transmembrane protein 101
- BRCA2-interacting transcriptional repressor EMSY
Sequence:
MPLGLKPCCAVCKTQSSSMWKKGNQGEILCNGCTGKAVSSGGSGASASSTIQQNNGGGKQSKQEIHRRSARLRSTKYKAPASEKKVSTKGKGRRHIFKLKNPIKAPESVSTIITSESMFYKGIYYQIGDVIKVIDEDDGKPYYAQIRGFVQDQYCEKSAALTWLIPTQASPRDRFDPSTYIVGPEEDLPRKMEYLEFVCHAPSEYFKSRSCPFPTLPVRPEKGYVWTHIGPTPAVAIKETVG
Protein: Possible osmoprotectant (Glycine betaine/carnitine/choline/L-proline) transport integral membrane protein ABC transporter ProW (O69723)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Possible osmoprotectant binding lipoprotein ProX
- ABC-type quaternary amine transporter
- Possible osmoprotectant transport integral membrane protein ABC transporter ProZ
- Conserved protein
- Probable lipoprotein LpqZ
- Uncharacterized membrane protein Rv3760
Sequence:
MHYLMTHPGAAWALTVVHLRLSLLPVLIGLMSAVPLGLLVQRAPLLRRLTTATASVIFTIPSLALFVVLPLIIGTRILDEANVIVALAAYTTALLVRAVLEALDAVPAQVHDAATAIGYSRIAQMLKVELPLSIPVLVAGLRVVAVTNIAMVSVGSVIGIGGLGTWFTAGYQTNKSDQIVAGVVAMFLLAIVVDVVINLAGRLATPWERAPRAARRRRQVAAPITGGAR
Protein: Cytochrome b-c1 complex subunit 2, mitochondrial (Complex III subunit 2) (Core protein II) (Ubiquinol-cytochrome-c reductase complex core protein 2) (P78761)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07257}; Matrix side {ECO:0000250|UniProtKB:P07257}.
Interaction partners:
- Cytochrome b-c1 complex subunit 6
- Cytochrome b
- Cytochrome b-c1 complex subunit 9
- Probable mitochondrial-processing peptidase subunit beta
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MKSFTRNLRRFQTPRRNLHGISYTPKKVEGVSFAGRETPTATGSLSVVINAGSRYQPDAGVSHLLEKFAFKTTEERSALRITRESELLGGQLSTQITREHIILTARFLNEYLEYYARLLAEVVDATKFLPFQLTEEVLPTARIESELFREDILRVAMAKLHEKAFHRGIGNEVYLPASASPSISEIKDFASKAYVKSNFSVISSGPDVQKASDLCAKYFAVIPDGSPLKSAPTKISSGESRVYSKGTNYFCLGFPAPAASPELFVLSSILGGDAAVKWSHGNTLLAKAAGTASEYKATAVADLTPYSDASLLSVVISGSCPKAIKATASESFKALKSLSSNIPNDVVKSGIAMAKTKYLSAFEPVTLNAISASSLVSASKGSDAFISGFDKVTPASISKVVSSLLAKPASTVAVGNLDVLPYYDEL
Protein: Probable uracil-DNA glycosylase (UDG) (EC 3.2.2.-) (Q5UPT2)
Organism: Acanthamoeba polyphaga mimivirus (APMV)
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.
Interaction partners:
Sequence:
MSKKNVDPFSDSDSSSEPPSIFSSDNEENSDVDNSVIINDKNTKSDEADIKYMDEDESSDSESESESKKKSKKSKKSKKSKKSVTKKKNNLLVGNRIITEYILIDANNYHFKSWIECFPDCKVNLKLLLFRPEWFDFFKYVESKTYFPQLESKLSSYLEKRQRIVPYPELLFNTMNVLPPGKIKVVILGQDPYPGSCISGVPYAMGCSFSVPLNCPVPKSLANIYTNLIKFNHMRKAPKHGCLASWILQGTFMINSAFTTVLNESGVHARTWESFTADLIDYLTDNYDDLIFVAWGAHAHKLCQRVDPKKHYIITSSHPSPYSVSNTMTSMSYGPNPKKVTYPSFNSVDHFGKINEHLKSRNKKPIFWDL
Protein: Cerebral cavernous malformations 2 protein (Malcavernin) (Q9BSQ5)
Organism: Homo sapiens (Human)
Function: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions (By similarity). May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Krev interaction trapped protein 1
- Programmed cell death protein 10
- Mitogen-activated protein kinase kinase kinase 3
- Integrin beta-1-binding protein 1
- Dual specificity mitogen-activated protein kinase kinase 3
- E3 ubiquitin-protein ligase SMURF1
- Krev interaction trapped protein 1
- RAC-alpha serine/threonine-protein kinase
- Serine/threonine-protein kinase 25
- Protein HEG homolog 1
Sequence:
MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (Q9I7H5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MLDRHCLYIGIFQLIIWVGVANGEFYSSVDSMQDLAQVEEELLNATRSYVESQQKQLDFYRRYVEQIKREHEWATSQLKLDDYLGHPLHAFRLIKRLVRDWDSLIFEPILANNAREEFRAFVEVLSRDLGYPDQSELQGAIKGLARLQKVYNLATSDLADGIIGGLNYGSDLRWRECYEIGVQLFDLGEYQRSLEWLQVAFILLRNSPREEKDADHYLSDIREYASMANFELGNPKKAARLLSQILESQPTHSAQQTQKYLESRVPGKNVQETKPSWFSNYTRLCQGRRLPEERSGDPLRCYLDGKRHAYFTLAPLQVEPVHLDPDINVYHGMLSSKQILSIFEEADKEEMVRSAVAGSGGEGTVRDLRVSQQTWLDYKSPVMNSVGRIIQFVSGFDMAGAEHMQVANYGVGGQYEPHPDYFEVNLPKNFEGDRISTSMFYLSDVEQGGYTVFTKLNVFLPPVKGALVMWHNLHRSLHVDARTLHAGCPVIVGSKRIGNIWMHSGYQEFRRPCNLTSDSYKSLAYRD
Protein: Probable E3 ubiquitin-protein ligase MARCHF10 (EC 2.3.2.27) (Membrane-associated RING finger protein 10) (Membrane-associated RING-CH protein X) (MARCH-X) (RING finger protein 190) (RING-type E3 ubiquitin transferase MARCHF10) (Q8NA82)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase (Probable). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates.
Interaction partners:
- E3 ubiquitin-protein ligase MARCHF11
Sequence:
MLHDARDRQKFFSDVQYLRDMQHKVDSEYQACLRRQEYRRDPNEKKRDQFWGQETSFERSRFSSRSSSKQSSSEEDALTEPRSSIKISAFKCDSKLPAIDQTSVKQKHKSTMTVRKAEKVDPSEPSPADQAPMVLLRKRKPNLRRFTVSPESHSPRASGDRSRQKQQWPAKVPVPRGADQVVQQEGLMCNTKLKRPNQERRNLVPSSQPMTENAPDRAKKGDPSAPSQSELHPALSQAFQGKNSPQVLSEFSGPPLTPTTVGGPRKASFRFRDEDFYSILSLNSRRESDDTEEETQSEECLWVGVRSPCSPSHHKRSRFGGTSTPQAKNKNFEENAENCRGHSSRRSEPSHGSLRISNAMEPATERPSAGQRLSQDPGLPDRESATEKDRGGSENAKKSPLSWDTKSEPRQEVGVNAENVWSDCISVEHRPGTHDSEGYWKDYLNSSQNSLDYFISGRPISPRSSVNSSYNPPASFMHSALRDDIPVDLSMSSTSVHSSDSEGNSGFHVCQPLSPIRNRTPFASAENHNYFPVNSAHEFAVREAEDTTLTSQPQGAPLYTDLLLNPQGNLSLVDSSSSSPSRMNSEGHLHVSGSLQENTPFTFFAVSHFPNQNDNGSRMAASGFTDEKETSKIKADPEKLKKLQESLLEEDSEEEGDLCRICQIAGGSPSNPLLEPCGCVGSLQFVHQECLKKWLKVKITSGADLGAVKTCEMCKQGLLVDLGDFNMIEFYQKHQQSQAQNELMNSGLYLVLLLHLYEQRFAELMRLNHNQVERERLSRNYPQPRTEENENSELGDGNEGSISQSQVV
Protein: Alpha glucosidase-like protein (At3g23640) (Heteroglycan glucosidase 1) (Q93Y12)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTLSGDSSETVEMTSTDMIFEPILEHGVFRFDCSVDHRKAAFPSVSFKNSKDREVPIVSHIVPAYIPTCGCLQDQQVVTFEFSPGTSFYGTGEVSGQLERTGKRVFTWNTDAWGYGSGTTSLYQSHPWVLVVLPTGETLGVLADTTRKCEIDLRKEGIIRIISPASYPIITFGPFSSPTAVLESLSHAIGTVFMPPKWALGYHQCRWSYMSDKRVAEIAQTFRDKKIPSDVIWMDIDYMDGFRCFTFDKERFPDPSALAKDLHSNGFKAIWMLDPGIKQEEGYYVYDSGSKNDVWISRADGKPFTGEVWPGPCVFPDYTNSKARSWWANLVKEFVSNGVDGIWNDMNEPAVFKVVTKTMPENNIHHGDDELGGVQNHSHYHNVYGMLMARSTYEGMELADKNKRPFVLTRAGFIGSQRYAATWTGDNLSNWEHLHMSISMVLQLGLSGQPLSGPDIGGFAGNATPRLFGRWMGVGAMFPFCRGHSEAGTDDHEPWSFGEECEEVCRAALKRRYQLLPHFYTLFYIAHTTGAPVAAPIFFADPIDSRLRAVENGFLLGPLLIYASTLSSQGSHELQHILPRGIWHRFDFADSHPDLPTLYLQGGSIISLAPPHLHVGEFSLSDDLTLLVSLDENGKAKGLLFEDDGDGYGYTKGRFLVTHYIAERDSSTVTVKVSKTEGDWQRPNRRVHVQLLLGGGAMLDAWGMDGEFIHIKVPSESGISELISTSNERFKLHMENTKLIPEKEVVPGQKGMELSKEPVELSSGDWKLNIVPWVGGRILSMTHVPSGIQWLHSRIDINGYEEYSGTEYRSAGCTEEYNVIERDLEHAGEEESLILEGDVGGGLVLRRKISIAKDNQRVFRIASSIEARSVGAGSGGFSRLVCLRVHPTFTLLHPTESFVSFTSIDGSKHEVWPDSGDQIYEGNNLPHGKWMLVDKSLNLRMVNRFDVSQVFKCIIHWDCGTVNLELWSKERPVSKESPLKIEHEYEVTSFP
Protein: Katanin p60 ATPase-containing subunit A1 (Katanin p60 subunit A1) (EC 5.6.1.1) (p60 katanin) (E1JJ62)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly cytoplasmic. Also localized to the interphase centrosome and the mitotic spindle poles. Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1. {ECO:0000256|HAMAP-Rule:MF_03023}.
Interaction partners:
Sequence:
MRVEEATYRRTTREKIVLRGNTTIRTVDSTSTYLPVMSPAGSSTPPTSLSHMARMMDSLILDSLSPFGFTKITATSRPSRNASLKKSSEGGHSSTAERHRPVNNLGSNAPGGLGIGGSVPLRSKQRLPTQVSAAEVAPQPRASQTAQMPFPSQQQDNRWVSSLRRRDPELQPTLPSINSNANSSSLSQSHHGSAGNVGLAGAGAPTPAASMGTMRLGRPARASAMTAALRKSRSVERLRARKLSTNTQLNLKHKPVKKNSLDENSNSDDQDATTSLEDNSHAQSLATSHNTPKCSPKTKAKHFSPLGYEVHLVDTLEKDILQRHPCIKWTDVAGLNEAKTILQEAVVLPVIMPEFFKGIRRPWRGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSSTLTSKYRGESEKLVRLLFEMARFYAPSTIFIDEIDALCASRGSDSEHEASRRFKAELLIQMDGLNASMQEEKVIMVLAATNHPWDIDEAFRRRFEKRIYIPLPNEGTRSALLKLCLKDVCLSPSLNTGIIGDELQGYSGSDISNVCRDASMMAMRRLISGRTPDQIKQIRREEVDQPITLQDFQDARLRTKKSVSADDVARFEKWMEEYGSC