wanglab/gogpt-training-data huggingface dataset:
Protein: Phospholipase A2 group V (EC 3.1.1.4) (PLA2-10) (Phosphatidylcholine 2-acylhydrolase 5) (P51433)
Organism: Rattus norvegicus (Rat)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity), preferentially releasing fatty acyl groups with a low degree of unsaturation such as oleoyl (C18:1) and linoleoyl (C18:2) groups (By similarity). Hydrolyzes low-density lipoprotein (LDL) phospholipids releasing unsaturated fatty acids that drive macrophage polarization toward an M2 phenotype (By similarity). May act in an autocrine and paracrine manner. Contributes to lipid remodeling of cellular membranes at different subcellular locations and generation of lipid mediators involved in pathogen clearance. Cleaves sn-2 fatty acyl chains of cardiolipin, a major component of the inner membrane of mitochondria and bacterial membranes. Promotes phagocytosis of bacteria in macrophages through production of lysophosphatidylethanolamines. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (By similarity). Promotes phagocytosis and killing of ingested fungi likely through controlling phagosome-lysosome fusion and phagosome maturation (By similarity). Plays a role in biosynthesis of cysteinyl leukotrienes (CysLTs) in myeloid cells. In eosinophils, triggers perinuclear arachidonate release and LTC4 synthesis in a PLA2G4A-independent way. In neutrophils, amplifies CysLTs biosynthesis initiated by PLA2G4A (By similarity). Promotes immune complex clearance in macrophages via stimulating synthesis of CysLTs, which act through CYSLTR1 to trigger phagocytosis. May regulate antigen processing in antigen-presenting cells. In pulmonary macrophages regulates IL33 production required for activation of group 2 innate lymphoid cells (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P97391}. Cell membrane {ECO:0000250|UniProtKB:P97391}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P97391}. Recycling endosome {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P97391}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P97391}.
Interaction partners:
- Phospholipase A2, group III
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Phospholipase A and acyltransferase 3
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Group 10 secretory phospholipase A2
- Phospholipase A2
- Phospholipase A2
- Group IIC secretory phospholipase A2
- Phospholipase A2, membrane associated
Sequence:
MKRLLTLAWFLACSVPAVPGGLLELKSMIEKVTGKNAVKNYGFYGCYCGWGGHGTPKDGTDWCCRMHDRCYGLLEEKHCAIRTQSYDYRFTQDLVICEHDSFCPVRLCACDRKLVYCLRRNLWSYNRLYQYYPNFLC
Protein: Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31) (K6UCV4)
Organism: Plasmodium cynomolgi (strain B)
Function: Catalyzes the hydrolytic deamination of adenosine to produce inosine. Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable).
Interaction partners:
Sequence:
MNILQEPIDFLKKDEIKNIDLSQMSKKERYKIWKRIPKCELHCHLDLCFSADFFLSCIRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFHDYEVIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKYKLDIELIHQAIVKGIKEVVELLDHKIHVALMCIGDTGHEAANIKASADFCLKHRADFVGFDHGGHEVDLKQYKEIFDYVRESGIPLSVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKEKNILLEVCPISNVLLKNAKSMDTHPIRQLYDAGVKVSVNSDDPGMFLTNINDDYEELYTHLNFTLEDFMKMNEWALEKSFMDSNIKDKVKNLYF
Protein: Iron-sulfur assembly protein 2 (Q12425)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the assembly of mitochondrial and cytoplasmic iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Iron-sulfur assembly protein 1
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron sulfur cluster assembly protein 1, mitochondrial
- NifU-like protein
- Cysteine desulfurase, mitochondrial
- Iron sulfur cluster assembly protein 2, mitochondrial
- Monothiol glutaredoxin-5
- Adrenodoxin homolog, mitochondrial
- J-type co-chaperone JAC1, mitochondrial
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
Sequence:
MQAKLLFTRLNFRRPSTTLRQFPLTCFLFHSKAFYSDLVTKEPLITPKRIINKTPGLNLSISERASNRLAEIYRNSKENLRISVESGGCHGFQYNLTLEPATKPDIKNDVKDKEFSDDLDDDDSKDIIYVLPEDKGRVIIDSKSLNILNNTTLTYTNELIGSSFKIINGSLKSSCGCGSSFDIEN
Protein: ArfGAP with FG repeats 1 isoform 1 (A0A0S2Z444)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAASVNANFAHFDNFPKSSSADFGTFNTSQSHQTASAVSKVSTNKAGLQTADKYAALANLDNIFSAGQGGDQGSGFGTTGKAPVGSVVSVPSQSSASSDKYAALAELDSVFSSAATSSNAYTSTSNASSNVFGTVPVVASAQTQPASSSVPAPFGATPSTNPFVAAAGPSVASSTNPFQTNARGATAATFGTASMSMPTGFGTPAPYSLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGAGFAAFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQFPTGSSSTNPFL
Protein: Beta-1,4-N-acetyl-galactosaminyltransferase 3 (E9PHD9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARADLVPKARPWGEHQHQFRGRANLHVFEDWCGSSIQQLRRNLHFPLYPHIRTTLRKLAVSPKWTNYGLRIFGYLHPFTDGKIQFAIAADDNAEFWLSLDDQVSGLQLLASVGKTGKEWTAPGEFGKFRSQISKPVSLSASHRYYFEVLHKQNEEGTDHVEVAWRRNDPGAKFTIIDSLSLSLFTNETFLQMDEVGHIPQTAASHVDSSNALPRDEQPPADMLRPDPRDTLYRVPLIPKSHLRHVLPDCPYKPSYLVDGLPLQRYQGLRFVHLSFVYPNDYTRLSHMETHNKCFYQENAYYQDRFSFQEYIKIDQPEKQGLEQPAGFEENLLEESQYGEVAEETPASNNQNARMLEGRQTPASTLEQDATDYRLRSLRKLLAQPREGLLAPFSKRNSTASFPGRTSHIPVQQPEKRKQKPSPEPSQDSPHSDKWPPGHPVKNLPQMRGPRPRPAGDSPRKTQWLNQVESYIAEQRRGDRMRPQAPGRGWHGEEEVVAAAGQEGQVEGEEEGEEEEEEEDMSEVFEYVPVFDPVVNWDQTFSARNLDFQALRTDWIDLSCNTSGNLLLPEQEALEVTRVFLKKLNQRSRGSVDFPIPDILCKWNHVMCGLYIGLFAEYSLSTSFIRVVESIKHFIP
Protein: SIP1a (B0LVE9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKQEIMAEGPRCKRRKQANPRRKNVLSYENVVDAGSGSDDEDRLLGSEGEGSPAGVPSLEASPRVAHALLSCRGDEENESQDGAGAHVWRHGELNGSEERKAEYNSMSPDISLHGIGNGTVKGIDASSELESFFAKRKLDDGEGHAASIAEYLQDTVIIYPEDPEEGTRLGTPEANGQDENENDLALRTPDAFAQLLTCPYCDRGYKRLTSLKEHIKYRHEKNDESFPCPLCSDTFAYRTQLERHMATHKPARDQPQLLNEGAGNRKFKCTECGKAFKYKHHLKEHLRIHSGEKPYECSNCKKRFSHSGSYSSHISSKKCIGLISINGRVRHGVNNKPGSSPNSAASSPGSPALAQLRHKLENGRSMSLQDPSAHTDIKSEPMDFNEYRLMIASQQEYGASGAFLNGGGRGGSPPGMHSSSQNPLQHLGIGSDSHPLGYTGFINNMSEVQKVLQIVDNTVCRQKMDGNPEEISKLRAYMKELGSQMEEQNRVLASQQSFLGVGHNSPTKTIIDYTLEKVNEAKACLQSLTEDSKRRLMDIKKERPSHAMDLLSEDKALERDAQYAPFSCQYCKETFSGPIPLHQHERYLCKMNEEIKAVLKPNDTVPTGRRGLFGSEQQAGVISSSLERDATSPVNPYKDHMSLLNVYFSMNTEPNSEELRKISMAVGLPQEFVKDAFVQWKAQSHHSFSRKRSPPPERSGETNHVRDSAFARSPVSLGQYGDSTAEIQAITNGDSGHKLSRPHQITGTRQTNEKPLDSVDHLRGETPSPLNLSSSSSKHSHSSSYTPNSLTSEDAHGEPLDLSLPKQVSKAERRAKPNGFSIEHTSNSTAREPGTEPLNLAHIKKEFNGPNSLGNENQMDKSSSPIFSINPFGGGHMYTSLPPHGAFPPPTFMSTTQASIPGLRPYPGLDPMSFLPPMAYTYAAGAATFAEMQQRRKYQRKQGFQGDLLDSAGDYLSGLEDLTDSESLLARKKIKKTESGMYACDLCDKTFQKTSSLLRHKYEHTGKRPHQCQICKKAFKHKHHLIEHSRLHSGEKPYQCDKCGKRFSHSGSYSQHMNHRYSYCKREAEEREAAKQENHNNGGPLEPTELLMRRAYLQGLGPLGFSDPEDQAEDITRENTILRDGTESGARETEETYAEVTDRQETGLMGEEEMEGQRFDTRSPDGTAKDEKESEVTGGTEDESSEEGKRNHDGENEDAD
Protein: Thymidylate synthase (TS) (TSase) (EC 2.1.1.45) (Cell division cycle protein 21) (Constitutive RNR3 transcription protein 9) (P06785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Thymidylate synthase required for de novo biosynthesis of pyrimidine deoxyribonucleotides. Required for both nuclear and mitochondrial DNA synthesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:8132557}. Note=Localizes to the nuclear periphery.
Interaction partners:
- Thymidylate kinase
- Dihydrofolate reductase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Deoxycytidylate deaminase
- Methylenetetrahydrofolate dehydrogenase [NAD
- Cytosine deaminase
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, mitochondrial
Sequence:
MTMDGKNKEEEQYLDLCKRIIDEGEFRPDRTGTGTLSLFAPPQLRFSLRDDTFPLLTTKKVFTRGIILELLWFLAGDTDANLLSEQGVKIWDGNGSREYLDKMGFKDRKVGDLGPVYGFQWRHFGAKYKTCDDDYTGQGIDQLKQVIHKLKTNPYDRRIIMSAWNPADFDKMALPPCHIFSQFYVSFPKEGEGSGKPRLSCLLYQRSCDMGLGVPFNIASYALLTRMIAKVVDMEPGEFIHTLGDAHVYKDHIDALKEQITRNPRPFPKLKIKRDVKDIDDFKLTDFEIEDYNPHPRIQMKMSV
Protein: Dehydrodolichyl diphosphate synthase complex subunit nus1 (EC 2.5.1.87) (Di-trans,poly-cis-decaprenylcistransferase) (Nogo-B receptor) (NgBR) (Nuclear undecaprenyl pyrophosphate synthase 1 homolog) (Q6DHR8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: With DHDDS, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B, a neural and cardiovascular regulator.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q96E22}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96E22}.
Interaction partners:
- Alkyl transferase
- Geranylgeranyl diphosphate synthase 1
- All trans-polyprenyl-diphosphate synthase PDSS1
- Farnesyl pyrophosphate synthase
- Prenyl
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Reticulon
- Polyprenal reductase
- Protein farnesyltransferase subunit beta
- Dolichyldiphosphatase 1.
Sequence:
MASLYEMVWRFLHALLYLQRAIVAWFRVHIWRWKLAVVDLLLPLALGFHNQKKTGPKGTRTSRRVRWGADGRTLEKLPLHVGLLVTEEEIHYTDIANLVVWCMAVGISYVSVYDNQGVFKRNNSRLMEEILKQQQELLGMGSSKYSVEILKNGTNKQEHQVLSCQSMVKVLSPDDGRLSIVQAAQQLCRAVEQKEKTSKDINVSVLDSLLKESKNIPDPDLVLKFGTVQSTLGFLPWHIRLTEIISMPSHIDASYDDLYDALQRFAGCEQRLGK
Protein: DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (DNA-directed RNA polymerase III subunit C) (RNA polymerase III 62 kDa subunit) (RPC62) (Q9BUI4)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway. Preferentially binds single-stranded DNA (ssDNA) in a sequence-independent manner.
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC8
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC7
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC7-like
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC2
Sequence:
MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLESVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQEIPKTPDHAPSRTFYLYTVNILSAARMLLHRCYKSIANLIERRQFETKENKRLLEKSQRVEAIIASMQATGAEEAQLQEIEEMITAPERQQLETLKRNVNKLDASEIQVDETIFLLESYIECTMKRQ
Protein: Pheophorbidase (RsPPD) (EC 3.1.1.82) (Q2V0W1)
Organism: Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus)
Function: Involved in chlorophyll degradation. Specific for the pheophorbides of the dihydroporphyrin and tetrahydroporphyrin types. Chlorophyllide a, pheophytin a and the nonfluorescent chlorophyll catabolite (NCC) are not used as substrates.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MGGEGGADDSVVHFVFVHGASHGAWCWYKLTTLLVAAGFKATSVDLTGAGINLTDSNTVFDFDHYNRPLFSLLSDLPSHHKIVLVGHSIGGGSVTEALCKFTDKISMVVYLAADMVQPGSTSSTHDSIMTVGEEDIWEYIYGEGADKPPTGVLMKEEFRRHYYYSQSPLEDVSLASKLLRPAPVRALGGADKLSPNPEAEKVPRVYIKTAKDNLFDPLRQDRLVEKWPPSQLYILEESDHSAFFSVPTTLFAYLLRAVSFLQL
Protein: CBL-interacting serine/threonine-protein kinase 9 (EC 2.7.11.1) (SNF1-related kinase 3.12) (SOS2-like protein kinase PKS6) (Q9MAM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Involved in K(+) homeostasis under low-K(+) stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23109687}. Nucleus {ECO:0000269|PubMed:23109687}. Note=Targeted to the tonoplast when interacting with CBL2 or CBL3.
Interaction partners:
- Calcineurin B-like protein 3
- Calcineurin B-like protein 2
- Calcineurin B-like protein 1
- Calcineurin B-like protein 9
- Calcineurin B-like protein 4
- Potassium channel AKT2/3
- Potassium transporter 5
- Calcineurin B-like protein 10
- Potassium channel AKT1
- Transmembrane protein, putative
Sequence:
MSGSRRKATPASRTRVGNYEMGRTLGEGSFAKVKYAKNTVTGDQAAIKILDREKVFRHKMVEQLKREISTMKLIKHPNVVEIIEVMASKTKIYIVLELVNGGELFDKIAQQGRLKEDEARRYFQQLINAVDYCHSRGVYHRDLKPENLILDANGVLKVSDFGLSAFSRQVREDGLLHTACGTPNYVAPEVLSDKGYDGAAADVWSCGVILFVLMAGYLPFDEPNLMTLYKRICKAEFSCPPWFSQGAKRVIKRILEPNPITRISIAELLEDEWFKKGYKPPSFDQDDEDITIDDVDAAFSNSKECLVTEKKEKPVSMNAFELISSSSEFSLENLFEKQAQLVKKETRFTSQRSASEIMSKMEETAKPLGFNVRKDNYKIKMKGDKSGRKGQLSVATEVFEVAPSLHVVELRKTGGDTLEFHKFYKNFSSGLKDVVWNTDAAAEEQKQ
Protein: Inter-alpha-trypsin inhibitor heavy chain H4 (ITI heavy chain H4) (ITI-HC4) (Inter-alpha-inhibitor heavy chain 4) (Inter-alpha-trypsin inhibitor family heavy chain-related protein) (IHRP) (Major acute phase protein) (MAP) (P79263)
Organism: Sus scrofa (Pig)
Function: Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration.
Subcellular location: Secreted {ECO:0000269|PubMed:10712621}.
Interaction partners:
- Haptoglobin
- C-reactive protein
- Protoporphyrinogen oxidase
- 5'-nucleotidase
- GMP synthase
- Lipocalin/cytosolic fatty-acid binding domain-containing protein
- Inter-alpha-trypsin inhibitor heavy chain H3
Sequence:
MKTLSPTGYGLLLVLPLLLAVLQSTTAHKNDINIYSLTVDSKVSSRFAHTVVTSRVVNKGSAVQEATFQMELPKKAFITNFSMIIDGVTYPGNIKEKAAAQEQYSAVARGESAGLVRATGRKTEQFQVAVSVAPAAKVTFELVYEELLARHLGVYELLLKIQPQQLVKHLQMDIHIFEPQGISFLETESTFMTNELAEALTISQNKTKAHIRFKPTLSQQQKSPEQQETVLDGNFIVRYDVNRTVTGGSIQIENGYFVHYFAPEVWSAIPKNVIFVIDTSGSMRGRKIQQTREALIKILGDLGSRDQFNLVSFSGEAPRRRAVAASAENVEEAKSYAAEIHAQGGTNINDAMLMAVQLLERANREELLPARSVTFIILLTDGDPTVGETNPSKIQKNVREAIDGQHSLFCLGFGFDVPYAFLEKMALENGGLARRIYEDSDSALQLEDFYQEVANPLLRLVAFEYPSNAVEEVTQDNFRLFFKGSELVVAGKLRDQSPDVLSAKVRGQLHMENVTFVMESRVAEQEAEFLSPKYIFHSFMERLWAYLTIQQLLAQTVSASDAEKKALEARALSLSLNYSFVTPLTSMVITKPEGQEQSQVAEKPVENGNRQGNTHSGHSSFQFHSVGDRTSRLTGGSSVDPVFSHRRGWKGQAQGFEKMSYLPPRLGPPGPLQPTRFSHPFSRITLDRVLPEVLSVPDETSHDMDSRIIGATIPPPPARIQAPSVILPLPGQSVDQLCVDLKHSQGPVKLLSDPGQGVEVTGHYEREKARFSWIEVTFKHPPLQVRASLEHIVVIRNRQSSAYKWKETLYSVMPGLKITMDKAGLLLLSSPNRVTIGLLSWDGPGKGLRLLLRDTDHFSSQISGTFGQFYQDVVWGPPAAADDSKRTVTVQGHDHSATRELKLDYQEGSPGKEISCWTVVL
Protein: Replication factor A protein 2 (RF-A protein 2) (DNA-binding protein BUF1) (Replication protein A 36 kDa subunit) (P26754)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Subcellular location: Nucleus.
Interaction partners:
- Replication factor A protein 1
- Replication factor A protein 3
- DNA repair and recombination protein RAD52
- Serine/threonine-protein kinase MEC1
- DNA primase large subunit
- DNA primase small subunit
- ATP-dependent helicase SGS1
- DNA polymerase alpha catalytic subunit A
- DNA polymerase alpha subunit B
- DNA polymerase delta catalytic subunit
Sequence:
MATYQPYNEYSSVTGGGFENSESRPGSGESETNTRVNTLTPVTIKQILESKQDIQDGPFVSHNQELHHVCFVGVVRNITDHTANIFLTIEDGTGQIEVRKWSEDANDLAAGNDDSSGKGYGSQVAQQFEIGGYVKVFGALKEFGGKKNIQYAVIKPIDSFNEVLTHHLEVIKCHSIASGMMKQPLESASNNNGQSLFVKDDNDTSSGSSPLQRILEFCKKQCEGKDANSFAVPIPLISQSLNLDETTVRNCCTTLTDQGFIYPTFDDNNFFAL
Protein: RAN binding protein 9 (A0A8I6ACK2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGQPPPPPPQQQPPPPPAAGAPGSGVALPAPAAASAGSSPAGSPGGGLGAAAAALLLHPPPPPPPPPATAAPPPPASAAAPATAPPGLAVGPGSVAGVPVPGLAAGSSAAAPFPHGDSALNEQEKELQRRLKRLYPAVDEQETPLPRSWSPKDKFSYIGLSQNNLRVHYKGHGKTPKDAASVRATHPIPAALQSLVGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLINNTCFYTKNGHSLGTEIYLKKYVVLQPNLYPTVGLQTPGEVVDANFGQHPFVFDIEDYMREWRTKIQAQIDRFPIGDREGEWQTMIQKMVSSYLVHHGYCATAEAFARSTDQTVLEELASIKNRQRIQKLVLAGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGGRSPKSQDSYPVSPRPFSSPSMSPSHGMSIHSLAPGKGSTAHFPGFESCSNGVISNKAHQSYCHSKHQLSSLNVPELNSINVSRSQQVNNFTSNDVDMETDHYSNGVGETSSNGFLNGSSKHDHEMEDCDTEMEVDCSQLRRQLCGGSQAAIERMIHFGRELQAMSEQLRRECGKNTANKKMLKDAFSLLAYSDPWNSPVGNQLDPIQREPVCSALNSAILETHNLPKQPPLALAMGQATQCLGLMARAGVGSCAFATVEDYLH
Protein: Splicing factor, suppressor of white-apricot homolog (Splicing factor, arginine/serine-rich 8) (Suppressor of white apricot protein homolog) (Q3USH5)
Organism: Mus musculus (Mouse)
Function: Plays a role as an alternative splicing regulator. Regulates its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MYGAGGGRAKPERKGGVKEEAGPGGTGTGGNRVELLVFGYACKLFRDDERALAQEQGQHLIPWMGDPKILIDRYDGRGHLHDLSAYDAEYATWNRDYQLSEEEARVEALCDEERYLALHTDLLEEEARQEEEYKRLSEALAEDGNYSAVGFTYGSDYYDPSEPTEEEEPSKQREKNEAENLEENEEPFIAPLGLSVPSDVELPPTAKMHAIIERTANFVCKQGAQFEIMLKAKQARNSQFDFLRFDHYLNPYYKFIQKAMKEGRYTVLAESKNEEKKKSGPTSDNEEEDDEEDGSYLHPSLFASKKSSRLEELMKPLKVVDPDHPLAALVRKAQADSSAPAPPTADGTPAQPSQVEYTADSTVAAMYYSYYMLPDGTYCLAPPPPGIDVATYYSTLPAGVTVSSSPGVTTTVPPPPGTTPPPPPTTAEPSSGVTSTTTTTSALAPVAIIPPPPDIQPVIDKLAEYVARNGLKFETSVRAKNDQRFEFLQPWHQYNAYYEFKKQFFLQKEGGGSTQAASTAEEAPTETAVEESGEAGEDGAPEGMAETGGRGSGKKEAGSSKSTVDGKLVKASFAPISFAIKAKENDLLPLEKNRVKLDDDSEEDEESRECQESTSSVANPSPAAAPPSVAVEEKKPQLTQEELEAKQAKQKLEDRLAAAAREKLAQASKESKEKQLQAERKRKAALFLQTLKNPLPEAEVGKLEESTFGVEDTGVMPCPLLVGGRTLPILEGKPPERPSNRCRDPPREEEREKKKKKHKKRSRTRSRSPKYHSSSKPRSRSHSKAKHSLPSAYRTVRRSRSRSRSPRRRAHSPERRREERSVPTAYRMSGSPGVSRKRTRSRSPHEKKKKRRSRSRTKAKARSQSTSPSKQAAQRPSAHSAHSASISPVESRGSSQERSRGVSQEKDGQISSAIVSSVQSKITQDLMAKVRAMLAASKNLQTSAS
Protein: Gamma-aminobutyric acid type B receptor subunit 1 isoform a (H9FSF4)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPDPSGGLPRGPPEPPDRLSCDGSRVHLLYK
Protein: Probable serine/threonine-protein kinase PBL2 (EC 2.7.11.1) (PBS1-like protein 2) (Protein kinase 2A) (O49839)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in disease resistance signaling. Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense responses downstream of FLS2. Acts as a BIK1 decoy and enables Xanthomonas campestris AvrAC/XopAC detection; X.campestris effector AvrAC/XopAC-mediated uridylylation promotes the formation of a complex with RKS1 and RPP13L4/ZAR1 which, in turn, activates effector-triggered immunity (ETI) against X.campestris. Promotes, when uridylylated by AvrAC/XopAC, the release of ADP from the inactive RKS1-ZAR1 complex, thus activating the resistosome.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21219905}; Lipid-anchor {ECO:0000305|PubMed:21219905}. Nucleus {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the plasma membrane. {ECO:0000269|PubMed:21219905}.
Interaction partners:
- Disease resistance RPP13-like protein 4
- Serine/threonine-protein kinase ZRK1
- Disease resistance protein RRS1
- RPM1-interacting protein 4
- Toll/interleukin-1 receptor-like protein
- Senescence-associated carboxylesterase 101
Sequence:
MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRKLFRIMDTKLGGQYPQKGAFTAANLALQCLNPDAKLRPKMSEVLVTLEQLESVAKPGTKHTQMESPRFHHSSVMQKSPVRYSHDRPLLHMTPGASPLPSYTQSPRVR
Protein: Necdin, MAGE family member (G3V7A4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cellular tumor antigen p53
- Transcription factor E2F1
- Small nuclear ribonucleoprotein-associated protein N
- Cellular tumor antigen p53
- NAD-dependent protein deacetylase sirtuin-1
Sequence:
MSEQSKDLSDPNFAAEDPDTEMQVSDAVPVGVPPPAPLAANLSGPSCAPEGPMAAPQASPPPAERFEEVDPKILQQAAEEGRAHQPQSPARPIPAPPAPAQLVQKAHELMWYVLVKDQKRMVLWFPDMVKEVMGSYKKWCRSILRRTSVILARVFGLHLRLTNLHTMEFALVKALSPEELDRVALNNRMPMTGLLLMILSLIYVKGRGAREGAVWNVLRILGLRPWKKHSTFGDVRKIITEEFVQQNYLKYQRVPHIEPPEYEFFWGPRANREITKMQIMEFLARVFKKDPQAWPSRYREALEQARALREANLVAQAPRSSVSED