wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3 (Transducin beta chain 3) (Q61011)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MGEMEQLRQEAEQLKKQIADARKACADITLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLIVWDTYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDYKLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEAICTGSDDASCRLFDLRADQELTAYSQESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSLKCERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKIWN
Protein: Splicing factor U2af 38 kDa subunit (U2 auxiliary factor 38 kDa subunit) (U2 snRNP auxiliary factor small subunit) (Q94535)
Organism: Drosophila melanogaster (Fruit fly)
Function: Necessary for the splicing of pre-mRNA. Binds to the polypyrimidine tract of introns early during spliceosome assembly (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor U2AF 50 kDa subunit
- Splicing factor U2AF subunit
- LD32469p
- LD40489p
- Pre-mRNA-processing factor 17
- RNA-binding protein 1
- U1 small nuclear ribonucleoprotein 70 kDa
- LD21442p
- Polyadenylate-binding protein 2
- LD29830p
Sequence:
MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRIHNKPTFSQTVLLQNLYVNPQNSAKSADGSHLVANVSDEEMQEHYDNFFEDVFVECEDKYGEIEEMNVCDNLGDHLVGNVYIKFRNEADAEKAANDLNNRWFGGRPVYSELSPVTDFREACCRQYEMGECTRSGFCNFMHLKPISRELRRYLYSRRRRARSRSRSPGRRRGSRSRSRSPGRRGGGRGDGVGGGNYLNNERDNMRGNDRGNDRDRRKGGGGGGGGGGGRY
Protein: PE family protein (Q7D7I5)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSFVNVDPFGMLAAAATLESLGSHMAVSNAAVASVTTKVPPPAADYVSKKLSLFFSSHGQQYQVQAARGTAFHRKLVRTLANGALAYEEVEIANNEGF
Protein: Early activation antigen CD69 (CD antigen CD69) (P37217)
Organism: Mus musculus (Mouse)
Function: Involved in lymphocyte proliferation and functions as a signal transmitting receptor in lymphocytes, natural killer (NK) cells, and platelets.
Subcellular location: Cell membrane {ECO:0000269|PubMed:38540778}; Single-pass type II membrane protein.
Interaction partners:
- Sphingosine 1-phosphate receptor 1
- T-cell surface glycoprotein CD4
- L-selectin
- Interferon gamma
- Receptor-type tyrosine-protein phosphatase C
- T-lymphocyte activation antigen CD80
- C-C chemokine receptor type 7
- Interleukin-7 receptor subunit alpha
- Interleukin-2
- B-lymphocyte antigen CD19
Sequence:
MDSENCSITENSSSHLERGQKDHGTSIHFEKHHEGSIQVSIPWAVLIVVLITSLIIALIALNVGKYNCPGLYEKLESSDHHVATCKNEWISYKRTCYFFSTTTKSWALAQRSCSEDAATLAVIDSEKDMTFLKRYSGELEHWIGLKNEANQTWKWANGKEFNSWFNLTGSGRCVSVNHKNVTAVDCEANFHWVCSKPSR
Protein: Major urinary protein 2 (MUP 2) (P11589)
Organism: Mus musculus (Mouse)
Function: Binds pheromones that are released from drying urine of males. These pheromones affect the sexual behavior of females.
Subcellular location: Secreted.
Interaction partners:
- Major urinary protein 3
- Major urinary protein 12
- Major urinary protein 1
- Serine protease inhibitor A3K
Sequence:
MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLEKSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAKLCEEHGILRENIIDLSNANRCLQARE
Protein: Claudin-18 (P56856)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity (By similarity). Required for lung alveolarization and maintenance of the paracellular alveolar epithelial barrier (By similarity). Acts as a negative regulator of RANKL-induced osteoclast differentiation, potentially via relocation of TJP2/ZO-2 away from the nucleus, subsequently involved in bone resorption in response to calcium deficiency (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:P56857}. Cell membrane {ECO:0000250|UniProtKB:P56857}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to tight junctions in epithelial cells. {ECO:0000250|UniProtKB:P56857}.; SUBCELLULAR LOCATION: [Isoform A1]: Cell junction, tight junction {ECO:0000250|UniProtKB:P56857}.; SUBCELLULAR LOCATION: [Isoform A2]: Cell junction, tight junction {ECO:0000250|UniProtKB:P56857}. Lateral cell membrane {ECO:0000250|UniProtKB:P56857}.
Interaction partners:
- Occludin
- Homeobox protein Nkx-2.1
- Tight junction protein 1
- Claudin-15
- Claudin-8
- Claudin-34
- Claudin-16
- Tight junction protein ZO-3
- Claudin-10
- Claudin-23
Sequence:
MSTTTCQVVAFLLSILGLAGCIAATGMDMWSTQDLYDNPVTSVFQYEGLWRSCVRQSSGFTECRPYFTILGLPAMLQAVRALMIVGIVLGAIGLLVSIFALKCIRIGSMEDSAKANMTLTSGIMFIVSGLCAIAGVSVFANMLVTNFWMSTANMYTGMGGMVQTVQTRYTFGAALFVGWVAGGLTLIGGVMMCIACRGLAPEETNYKAVSYHASGHSVAYKPGGFKASTGFGSNTKNKKIYDGGARTEDEVQSYPSKHDYV
Protein: Serine/threonine-protein kinase 1 (EC 2.7.11.1) (O24527)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase. Regulates organ size in coordination with MOB1A by modulating cell proliferation and cell expansion, possibly by facilitating cell cycle exit. Positive regulator of the pathogen-associated molecular pattern (PAMP, e.g. flg22)-triggered immunity (PTI) signaling by stabilizing BIK1 and activating RBOHD by phosphorylation to promote the extracellular reactive oxygen species (ROS) burst involved in defense responses to bacterial infection.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26685188}. Nucleus {ECO:0000269|PubMed:26685188}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:26685188}. Early endosome {ECO:0000269|PubMed:26685188}. Note=Observed at the plasma membrane and in the nucleus when associated with MOB1A. {ECO:0000269|PubMed:26685188}.
Interaction partners:
- At1g69210/F4N2_11
- Putative clathrin assembly protein At1g33340
- Putative clathrin assembly protein At1g14686
- Putative clathrin assembly protein At5g65370
- Putative clathrin assembly protein At5g35200
- Putative clathrin assembly protein At1g14910
- Putative clathrin assembly protein At5g10410
- Putative clathrin assembly protein At4g25940
- U-box domain-containing protein 26
- Putative clathrin assembly protein At5g57200
Sequence:
MDHNSPKSRRSRKPEPKPDIYSTFVVHSDSDSDQGRDRDKRKAKPEEDENVDLYATMVYKGDSDGEGEEDDDDDSMLPPLLKRLPKDFGGGASLDYDDDDGDESGDFGTMIVKTDRSSHSKKNSPYSSKPRMGVSPRRRARGGDEESSDEEDEEEDDDDDDGDYGTFVVKSKDKKGKKKDKEIDMTTMGRAVASMQKSNFGGKTRKLDPSSSSSKLHGEDNRKMQQQNSKMSTTSLPDSITREDPTTKYEFLNELGKGSYGSVYKARDLKTSEIVAVKVISLTEGEEGYEEIRGEIEMLQQCNHPNVVRYLGSYQGEDYLWIVMEYCGGGSVADLMNVTEEALEEYQIAYICREALKGLAYLHSIYKVHRDIKGGNILLTEQGEVKLGDFGVAAQLTRTMSKRNTFIGTPHWMAPEVIQENRYDGKVDVWALGVSAIEMAEGLPPRSSVHPMRVLFMISIEPAPMLEDKEKWSLVFHDFVAKCLTKEPRLRPTAAEMLKHKFVERCKTGASAMSPKIEKSRQIRATMALQAQSVVAPSLEDTSTLGPKSSEELGITVPSKPPQNSTEAPLTSTLNRQHITGNTVLAGEGGDFGTMIVHGEDETEESDSRSQLVREKESSSSQFEGVPREFPGEELPDSWIHDKKKPPAIDLPVEASISQSMQASSSHEHRTKLHNIAGTQMEGGSDASGSTLKNETVGRKAFALQDKLWSIYAAGNTVPIPFLRATDISPIALLSENMIGGMQQDGNGTVAVEALQELFTSSDPQSKKGRRGQNEMPLPPSVYQRLTTSSSLMNLAQVLAYHRACYEEMPLQELQATQEQQTIQNLCDTLRTILRL
Protein: M (M protein) (Matrix protein) (Matrix protein M) (Membrane protein) (ORF6) (Unglycosylated membrane protein) (A0FJB3)
Organism: Porcine reproductive and respiratory syndrome virus (PRRSV)
Interaction partners:
Sequence:
MGSSLDDFCNDSTAPQKVLLAFSITYTPVMIYALKVSRGRLLGLLHLLIFLNCAFTFGYMTFVHFESTNRVALTMGAVVALLWGVYSAIETWKFITSRCRLCLLGRKYILAPAHHVESAAGFHPIAANDNHAFVVRRPGSTTVNGTLVPGLKSLVLGGRKAVKQGVVNLVKYAK
Protein: Methylthioalkylmalate synthase 1, chloroplastic (EC 2.3.3.17) (2-isopropylmalate synthase 3) (Q9FG67)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Determines the side chain length of aliphatic glucosinolate structures. Catalyzes exclusively the condensation reactions of both the first and second methionine carbon chain elongation.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Methionine aminotransferase BCAT4
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydrogenase 1, chloroplastic
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- Cytochrome P450 83A1
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- Dihydroxy-acid dehydratase, chloroplastic
- 3-isopropylmalate dehydratase small subunit 1
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
Sequence:
MASSLLTSSVMIPTTGSTVVGRSVLPFQSSLHSLRLTHSYKNPALFISCCSSVSKNAATSSTDLKPVVERWPEYIPNKLPDGNYVRVFDTTLRDGEQSPGGSLTPPQKLEIARQLAKLRVDIMEVGFPGSSEEELETIKTIAKTVGNEVDEETGYVPVICAIARCKHRDIEATWEALKYAKRPRILVFTSTSDIHMKYKLKKTQEEVIEMAVSSIRFAKSLGFNDIQFGCEDGGRSDKDFLCKILGEAIKAGVTVVTIGDTVGINMPHEYGELVTYLKANTPGIDDVVVAVHCHNDLGLATANSIAGIRAGARQVEVTINGIGERSGNASLEEVVMALKCRGAYVINGVYTKIDTRQIMATSKMVQEYTGLYVQAHKPIVGANCFVHESGIHQDGILKNRSTYEILSPEDIGIVKSQNSGLVLGKLSGRHAVKDRLKELGYELDDEKLNAVFSLFRDLTKNKKRITDADLKALVTSSDEISLEKLNGANGLKSNGYIPVPQVSSNV
Protein: Uncharacterized protein, isoform B (M9PFZ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGDDNQRFQFQLQAVATVFLLENDGNIQNSASGRPVDYHTVVGHFKDFFMYLPVMMTTLKETMSGFPKFAEGMRILTSGKGRVDGEDCKCSQNALASGELLDTNSRFG
Protein: Uncharacterized protein (Q584T5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGLFIRVVSGSPRQRHSDVENTTPEYTILCAQTPNAADRITQLMNRFRTSTEASSTQTMIYLLQTCVGTDVPPDEVENIVETLVGFANEHPMWTDTIQWICAFVHYYCTDEFTVSLFSEFEVPSVAVRALKEAPQNSHLVLAGCTLLSHFNLYPIGDGISQLTRALSMHSKDPLVCKAACRALAEFTSYVVEAPNLYVTANKEFVGAGGIDVLESVLHEQIGDEETTRYVARIAANAIGSGEPNTLEPDFKVVMYLAEALERYSDSEQLCSCTLRVFSVFPSSPYVDMNAIASLFKNTESEAVAIEAIHFLCSVAMSVKTLKQLIHTTGCVQRVLEVMRKYAGNASIQEYACSLLSYLSFDSETITSFITDANGIILVLAAMRNFPESEDLLVSACAALSGLTFNNLKGQEVIVSEKGVALILEAMGRGKSARLQDNGCLALGTMCWNSDLKADVIRYGGVQMIMRALAAHYTNAGLVKNACRALAQVAFNCEAYRDDMHASGVIPLIMKGMAEHPNYDRVQMHGCVALSYLSWNNEQNSAQIISNNGYAVIINAMRNHAHNAEVQEHASRALANIGGVRSDELTPALELIIGAMRRHEHVSEVQEETCRAIVTLSLISTSYKDKLFELGAAECVVTAMHNFPSTQVVQQEACNALAHLAYEHANLNRAVTELSGVEVLLRAMKTYVNVPKIQLNACGGLSALAFDNTIAQKQIYDLGGVACIIRAMENFERLRMLELGCSVLGTLAWNSEIKESVAVVAIPEILKAMRVHHDSPLLQKSTCRAISQFAFNSESNRKLLAESGAIPLIVLAMRTHVTTDKLLVHGIKALTYLCWENSQVAEAIISEGIEEVLQHVIDTYPASTRVYGEAAHLSKILFRKVTGSPNPSVRVYSPPVFSPVSVSQTPGSAVTRTDTAMLLSPPLRDASDVGHFYGRHSDTGRKDDWHPAEYQKSPKLEHQQQRQQHQRNNRGDKETQGPGETRGEIDGAGRRRRNRRRGGGGGGGGGGGRFDRPPNQCEPPGALVRDSPERRTEVHNTWSPRRDGGSSRPLSPDDLWDDPHPSTYHGNRELGNLSWQQVQLTRQQEERHVTSGDRSYRGGGGGGRGGRRYPNPRGNAPTRGRGDSRRCQ
Protein: Alpha/beta hydrolase (O06255)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MPRIRKLVAALHRRGPHRVLRGDLAFAGLPGVVYTPEAGLHLPGVAFGHDWLTGTSRYSGLLEHLASWGIVAAAPDSERGLAPSVLNLAFDLGVALDIVAGVRLGPGKISVHPAKLGLVGHGFGGSAAVFAAAGLTGTHVKSVAAIFPTVTNPAAEQPAATLDVPGLILTAPGDPKTLTSNALGLSRAWDKATLRIVSKARAGGLVEGRRLTKVLGLPGPHRRTQRSVRALLTGYLLYTLGGDKTYRRFADPDLQLPKTDPIDPEAPPITPGEKIVTLLK
Protein: Glutathione hydrolase proenzyme (EC 3.4.19.13) (Gamma-glutamyltranspeptidase proenzyme) (GGT) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase large chain; Glutathione hydrolase small chain] (P18956)
Organism: Escherichia coli (strain K12)
Function: Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D-gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acceptors. The KM values for gamma-glutamyl acceptors are so high that it has been proposed transpeptidation is not the physiological role in E.coli.
Subcellular location: Periplasm {ECO:0000269|PubMed:1360205, ECO:0000269|PubMed:2877974}.
Interaction partners:
- Cytosol aminopeptidase
- Glutathione synthetase
- Thioredoxin/glutathione peroxidase BtuE
- Cytosol non-specific dipeptidase
- Putative glutamate--cysteine ligase 2
- Glutathione reductase
- Aminopeptidase N
- Glutamate decarboxylase beta
- Glutamate decarboxylase alpha
- Glutamate--cysteine ligase
Sequence:
MIKPTFLRRVAIAALLSGSCFSAAAAPPAPPVSYGVEEDVFHPVRAKQGMVASVDATATQVGVDILKEGGNAVDAAVAVGYALAVTHPQAGNLGGGGFMLIRSKNGNTTAIDFREMAPAKATRDMFLDDQGNPDSKKSLTSHLASGTPGTVAGFSLALDKYGTMPLNKVVQPAFKLARDGFIVNDALADDLKTYGSEVLPNHENSKAIFWKEGEPLKKGDTLVQANLAKSLEMIAENGPDEFYKGTIAEQIAQEMQKNGGLITKEDLAAYKAVERTPISGDYRGYQVYSMPPPSSGGIHIVQILNILENFDMKKYGFGSADAMQIMAEAEKYAYADRSEYLGDPDFVKVPWQALTNKAYAKSIADQIDINKAKPSSEIRPGKLAPYESNQTTHYSVVDKDGNAVAVTYTLNTTFGTGIVAGESGILLNNQMDDFSAKPGVPNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITTVLQMVVNSIDYGLNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAKGQKVALKEAMGSTQSIMVGPDGELYGASDPRSVDDLTAGY
Protein: [Thr6]-phyllokinin (C0HKA7)
Organism: Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)
Function: May produce in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle. May target bradykinin receptors (BDKRB).
Subcellular location: Secreted {ECO:0000269|PubMed:26443407}.
Interaction partners:
Sequence:
RPPGFTPFRIY
Protein: Matrilin-4 (MAT-4) (O89029)
Organism: Mus musculus (Mouse)
Function: Major component of the extracellular matrix of cartilage.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRGPCCWPLSLLLLFLQSWETQLQSAGPRCYNGPLDLVFMIDSSRSVRPFEFETMRQFLVGLLRSLDVGLNATRVGVIQYSSQVQSVFPLGAFSRREDMERAIRAVVPLAQGTMTGLAIQYAMNVAFSEAEGARPSEERVPRVLVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRTMASPPLDQHVFLVESFDLIQEFGLQFQGRLCGKDLCAELVHGCQHLCVNAPGTFYCACNSGYKLAPDNKNCLALDLCAEGTHGCEHLCVNSVDSYFCRCRAGFALQQDQRSCRAIDYCSFGNHSCQHECVSTLAGPQCRCREGHDLLPDGRSCRVRDFCNGVDHGCEFQCVSEGLSFHCLCPEGRRLQADGKSCDRCREGHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTMTGLALRHMVEHSFSEAQGARPRDLNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEEELREIASEPSELHVSYSPDFSTMTHLLENLKGSICPEEGIGAGTELRSPCECESLVEFQGRTLGALESLTQNLARLTERLEELENQLASRK
Protein: Trehalose-phosphate phosphatase (TPP) (EC 3.1.3.12) (Trehalose-6-phosphate phosphatase) (P9WFZ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
Interaction partners:
- Trehalose-6-phosphate synthase
- Malto-oligosyltrehalose trehalohydrolase
- Trehalose synthase/amylase TreS
- Trehalase
- Uncharacterized glycosyl hydrolase Rv2006
- Uncharacterized glycosyl hydrolase Rv3401
- Putative maltooligosyl trehalose synthase
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- Maltokinase
- 1,4-alpha-glucan branching enzyme GlgB
Sequence:
MRKLGPVTIDPRRHDAVLFDTTLDATQELVRQLQEVGVGTGVFGSGLDVPIVAAGRLAVRPGRCVVVSAHSAGVTAARESGFALIIGVDRTGCRDALRRDGADTVVTDLSEVSVRTGDRRMSQLPDALQALGLADGLVARQPAVFFDFDGTLSDIVEDPDAAWLAPGALEALQKLAARCPIAVLSGRDLADVTQRVGLPGIWYAGSHGFELTAPDGTHHQNDAAAAAIPVLKQAAAELRQQLGPFPGVVVEHKRFGVAVHYRNAARDRVGEVAAAVRTAEQRHALRVTTGREVIELRPDVDWDKGKTLLWVLDHLPHSGSAPLVPIYLGDDITDEDAFDVVGPHGVPIVVRHTDDGDRATAALFALDSPARVAEFTDRLARQLREAPLRAT
Protein: Female sterile (2) ltoPP43, isoform B (Q86BK4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPAVVRIKRRIDEEPQTAFVLNGKRRRLHNDENALEDAGAVAGAVAGAVASDKDELTTVLKFAGTLEKQDDCATRKFAAARLNKAAARDLVQQQRSNDAAIASALRRDRQRQEAQENSREQRFRVVNCLRSTLENSAAEAECPESQSHESSSHITIVDIESQQQQHMGTASAAAEEQQQQEIAPSQDQQQPADSDVGYVYDLYVPENEMQAAYVDMMDDNYLRFVIQVEPQKTLSITNYYM
Protein: Ribosomal oxygenase 2 (60S ribosomal protein L27a histidine hydroxylase) (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) (EC 1.14.11.79) (Histone lysine demethylase MINA) (MYC-induced nuclear antigen) (Mineral dust-induced gene protein) (Nucleolar protein 52) (Ribosomal oxygenase MINA) (ROX) (Q8IUF8)
Organism: Homo sapiens (Human)
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39'. May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles.
Subcellular location: Nucleus {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}. Nucleus, nucleolus {ECO:0000269|PubMed:12091391, ECO:0000269|PubMed:15819408}.
Interaction partners:
- Large ribosomal subunit protein uL15
- Low-density lipoprotein receptor-related protein 4
- tRNA wybutosine-synthesizing protein 5
- Large ribosomal subunit protein uL2
- 2-oxoglutarate and iron-dependent oxygenase JMJD4
Sequence:
MPKKAKPTGSGKEEGPAPCKQMKLEAAGGPSALNFDSPSSLFESLISPIKTETFFKEFWEQKPLLIQRDDPALATYYGSLFKLTDLKSLCSRGMYYGRDVNVCRCVNGKKKVLNKDGKAHFLQLRKDFDQKRATIQFHQPQRFKDELWRIQEKLECYFGSLVGSNVYITPAGSQGLPPHYDDVEVFILQLEGEKHWRLYHPTVPLAREYSVEAEERIGRPVHEFMLKPGDLLYFPRGTIHQADTPAGLAHSTHVTISTYQNNSWGDFLLDTISGLVFDTAKEDVELRTGIPRQLLLQVESTTVATRRLSGFLRTLADRLEGTKELLSSDMKKDFIMHRLPPYSAGDGAELSTPGGKLPRLDSVVRLQFKDHIVLTVLPDQDQSDEAQEKMVYIYHSLKNSRETHMMGNEEETEFHGLRFPLSHLDALKQIWNSPAISVKDLKLTTDEEKESLVLSLWTECLIQVV
Protein: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Q6INN8)
Organism: Xenopus laevis (African clawed frog)
Function: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks (By similarity). Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells (By similarity). Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of mre11, activating the ATR-CHK1 pathway and allowing the forks to restart replication. Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}. Chromosome {ECO:0000269|PubMed:29670289}. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage. {ECO:0000269|PubMed:29670289}.
Interaction partners:
Sequence:
MKGINGAKRVRHDASPSAQDGYVTPEKRVKRWSGGQTAANYREWDVEEVCLFLASHGLGELEVIFRENKIKGRILEYLTDSHLKDLQISSVALRLDLLSCLRMLCQNSPSIMKVFNDPIHGHIELHPLLVRIIDTPEFQRLRYIKQLGGSYYVFPGASHNRFEHSIGVGYLAGCLVQALHERQPDLQIDMRDMLCVQIAGLCHDLGHGPFSHMFDGRFMPLACPQKKFKHESASVAMFDHLIQSNGLEEAMKENGLCLPDDLTFIKEQIAGPLSSEAEQQFNSSPNSSSWPYRGRTEEKSFLYEIVANKRNGIDVDKWDYFARDCHHLGIQNNFDYKRFLKFARVCEVGSKKHICTRDKEVGNLYDMFHTRNCLHRRAYQHKVGNIIETMITDAFVKADPHIKIEGANGKYYSISGSVDDMVAYTKLTDNIYHQILYSNDPNLKEAREILQKVERRHLYKYIGQTHPHSNSRIEPDKYDKLPADLASSVPQTSAKDVELHAEDFIVDVIHMDYGMKEQNPINNVRFYCKADPRKAIKIRRDQVSQLLPEKFAEQIIRVYCKKTDEKSLETAKRYFIQWCMNKDFSKPQDGDVVAPDMTPLKASWVDDDDDEDNEGKQQTELLHKSRVKLFTN
Protein: Alpha-mannosidase (EC 3.2.1.-) (B5DEJ3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGPLRWLPLLGQLLLLWPLAARPASPIRAFVVPHSHMDVGWVYTVQESMRAYAANVYTTVVEELVRGRQRRFIAVEQEFFRLWWDGVASEQQKQQVRQLLDEGCLEFVLGGQVMHDEAVTHLDDQILQLTEGHGFLYETFGIRPQFSWHVDPFGASATTPTLFSLAGFNAHLISRIDYDLKDAMQEAQGLQFVWHGSPSLSEQQEIYTHVMDLYSYCTPSHIPFSNRSGFYWNGVAVFPEPPPDGVYPNMSEPVTVDNIHLYAEALVANIKQRAAWFRTPHVLWPWGCDKQFFNASVQFDNMDPLLEYINNRSAQFGISVQYATLNDYFQALHDFNVTWDIRDHHDFLPYSSEPQQAWTGFYTSRSTLKGLARQASALLYAGESMFTRYMWPHPRGTLDPTWALQQLQQLRWAVSEVQHHDAITGTESPKVKNMYMEHLSMGMRGVHKLMASIALDRSPGSGTDTRPVGYSASVYNPLAWKITTIITLTVAFPSVSVTDELGRPVSAQIQNSTKDPSAYDLLILTTIPGLSYRYYKVRRILGDQAGTRELVTPRANTLKFSRKLRNQTSQEGKLLVPVMNDCYTLLFDQDTNMLHSIQDRQSNRTVHMTQEFLEYRANGDVKQGPISDNYLFASNDTAEPSWEAVGMEMVVGTLATDVRQYFYRNITDQGYIYSIHTRLAHVHPSLAGELLCRRIEQQYQVGPLDLNREAILRTSSDLNSQQVLYSDNNGYQMQRRPYKAFKSNPIPRNYYPMVQSAFIEDDKSRLVLLAERPHGVSSQENGQVEVMLHRRLWNNLVWDLNYNLTLNDTSVVHPVLWLLLGPKSTTTALRPRSGVALQHRPVVLLKELTDEEETAIHRPHHPWPVTLPPSLHLQVLSLRGWQYSRNHAQHLKNLQRGHPEKPQVNLQRVLLRLHHLYEAGEDPVLSRPATVDLKIALRGLGSVVAVEERSLTGTWDVQTLQRWHWRTKIGQLKGHPTSPPRSPGGSIITVYPKEIRTFFIYLQQ
Protein: Complement C3 (F1SBS4)
Organism: Sus scrofa (Pig)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGSTSGPRLLLLLLTSLPLALGDPIYTIITPNVLRLESEEMVVLEAHEGQGDIRVSVTVHDFPAKRQVLSSETTTLNNANNYLSTVNIKIPASKEFKSEKGHKFVTVQALFGNVQVEKVVLVSLQSGYLFIQTDKTIYTPGSTVLYRIFTVDHKLLPVGQTIVVTIETPEGIDIKRDSLSSHNQFGILALSWNIPELVNMGQWKIRAHYEDAPQQVFSAEFEVKEYVLPSFEVQVEPSEKFYYIDDPNGLTVNIIARFLYGESVDGTAFVIFGVQDGDQRISLSQSLTRVPIIDGTGEATLSQGVLLNGVHYSSVNDLVGKSIYVSVTVILNSGSDMVEAERTGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVYVTNPDGSPARHIPVVTEDFKVRSLTQEDGVAKLSINTPDNRNSLPITVRTEKDGIPAARQATKTMHVLPYNTQGNSKNYLHLSVPRVELKPGENLNVNFHLRTDPGYQDKIRYFTYLIMNKGKLLKVGRQPRESGQVVVVLPLTITTDFIPSFRLVAYYTLIAANGQREVVADSVWVDVKDSCVGTLVVKGGGKQDKQHRPGQQMTLEIQGDRGARVGLVAVDKGVFVLNKKNKLTQRKIWDVVEKADIGCTPGSGKDFAGVFTDAGLAFKSSKGLQTPQRADLECPKPAARKRRSVQLMEKRMDKLGQYSKELRRCCEHGMRDNPMKFSCQRRAQFIQHGDACVKAFLDCCEYIAKLRQQHSRNKPLGLARSDLDEEIIPEEDIISRSQFPESWLWTIEEFKEPDKNGISTKTMNVFLKDSITTWEILAVSLSDKKGICVADPYEVVVKQDFFIDLRLPYSVVRNEQVEIRAILYNYREAEDLKVRVELLYNPAFCSLATAKKRHQQTLTVPAKSSVPVPYIIVPLKTGLQEVEVKAAVYNHFISDGVKKTLKVVPEGMRVNKTVVTRTLDPEHKGQQGVQREEIPPADLSDQVPDTESETKILLQGTPVAQMVEDAIDGDRLKHLIQTPSGCGEQNMIGMTPTVIAVHYLDSTEQWEKFGLEKRQEALELIKKGYTQQLAFRQKNSAFAAFQDRLSSTWLTAYVVKVFAMAANLIAIDSQVLCGAVKWLILEKQKPDGVFEENGPVIHQEMIGGFKNTEEKDVSLTAFVLIALQEAKDICEPQVNSLLRSINKARDFLADYYLELKRPYTVAIAGYALALSDKLDEPFLNKLLSTAKERNRWEEPGQKLYNVEATSYALLALLVVKDFDSVPPIVRWLNEQRYYGGGYGSTQATFMVFQALAQYQKDVPDHKDLNLDVSIHLPSRSAPVRHRILWESASLLRSEETKENERFTLIAEGKGQGTLSVVTMYHAKTKGKTTCKKFDLKVSIHPAPEPVKKPQEAKSSMVLDICTRYLGNQDATMSILDISMMTGFSPDTEDLKLLSTGVDRYISKYELNKALSNKNTLIIYLDKISHTLEDCISFKVHQYFNVGLIQPGSVKVYSYYNLDESCTRFYHPEKEDGMLNKLCHKEMCRCAEENCFMHHDEEEVTLDDRLERACEPGVDYAQLPFPSPPGSDEVQVGQERRFISHIKCREALKLKEGGHYLVWGVSSDLWGEKPNISYIIGKDTWVELWPDGDVCQDEENQKQCQDLANFSENMVVFGCPN
Protein: Serine/threonine-protein kinase ISR1 (EC 2.7.11.1) (Inhibition of staurosporine resistance protein 1) (Q06098)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable serine/threonine protein kinase which may function redundantly with MPK1-independent branch of the PCK1 pathway that is presumed to be required for the tolerance to high temperatures and staurosporine.
Interaction partners:
- Protein GIR2
- Chitin synthase 2
Sequence:
MNSTPPTSPVTRVSDGSFPSISNNSKGFAYRQPQKHKSNFAYSHLVSPVEEPTAKFSEAFQTDYSSKAPVATSEAHLKNDLDVLFTTPRFYSPENLALMFRLSNTVSSLEFLDEFLMGILLAPEMDFLSNPSYSLPSNKLVGQGSYSYVYPISSSASSRCNNDSGVVLKFAKSQHKSKVILQEALTLAYLQYMSPSTNESHIIPFYGLTYITKSHFRRLRSNECVPGLILPKCEMSLYHFNTAVSHKLSLITKRKIWWRLMKQMIDALKSLKTNGIIHGDIKTANILITEMHVLNGGHCKDFDFYLADFTSAFHINQTPTDLNTTVEYCAPELIDSSSDHVPTFESDLYAVGLCLLSFISQHEPYNELQALVSHGSSPGIGSSSIQQSQWLINALLKKDPINLNMLRNDLFQDWKSELALLSRILVDRLPLENLITILDSNYI