wanglab/gogpt-training-data huggingface dataset:
Protein: NADH-dependent flavin oxidoreductase iccE (EC 1.-.-.-) (Epimerase iliE) (Ilicicolin H biosynthesis cluster protein E) (A0A482N8M8)
Organism: Talaromyces variabilis (Penicillium variabile)
Function: NADH-dependent flavin oxidoreductase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2-pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain. IccE acts as an epimerase and catalyzes the conversion of 8-epi-ilicicolin H into the final product ilicicolin H. The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iccA with the partnering trans-enoyl reductase iccB since iccA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iccC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iccD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. Finally, the epimerase iccE converts 8-epi-ilicicolin H into ilicicolin H via epimerization. IccA to iccE are sufficient for ilicicolin H biosynthesis and the roles of the remaining enzymes, iccF, iccG and iccH within the pathway have still to be determined (Probable).
Interaction partners:
Sequence:
MADLHLAKSITLRCGLTLPNRLAKTAIAESIAPRNMLIDEGFHRVYAPWAEGGWGMVLTGHVQVDSMHLGTHTDPAVNADFSDDQIVGSWKVWAAVCNRHGTPTIMQLNHPGRQAPIGAGTSGVFAKNISASAVPMDIGSGLLARAVSKIVFGTPREMTVDDIGKLVRQFARAARLASQSGFAGVELHASHGYLLAQFLSAATNRRKDAYGGTPANRARIVVEIIKAVRAEVPASFCVGIILTAVHGSASTEEFQSFIEQAQLICDAGVDFIEISGGTFETPSMFIGPEKRGKAYDWDNQEAFFLDFAQAIRPHLGTVPLLLTGGFRSCHAMEAAVKRGDCDMIGLARPAVVNPLLPKTVVFNPEVNKSGDTKLHATRTPAPWYIKLFGITALNVHMDNAWYVGRLQTLAKTGR
Protein: Cathepsin B-like protease 2 (EC 3.4.22.-) (Cathepsin B2) (AtCathB2) (Q93VC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol protease that plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required for abiotic stress-induced PCD. Functions redundantly with CATHB1 and CATHB3 in basal defense and distinct forms of plant programmed cell death (PCD). Participates in the establishment of basal resistance against the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required for full levels of PCD during resistance (R) gene-mediated hypersensitive response (HR). Involved in the regulation of senescence, a developmental form of PCD in plants.
Subcellular location: Vacuole {ECO:0000269|PubMed:15539469}.
Interaction partners:
- Vacuolar-processing enzyme beta-isozyme
- Vacuolar-processing enzyme delta-isozyme
- Vacuolar-processing enzyme alpha-isozyme
- Vacuolar-processing enzyme gamma-isozyme
- UPF0235 protein At5g63440
- Eukaryotic aspartyl protease family protein
- Eukaryotic aspartyl protease family protein
- Proteasome subunit beta type-6
- Thiamine thiazole synthase, chloroplastic
- Cysteine proteinase inhibitor 6
Sequence:
MADNCIRLLHSASVFFCLGLLISSFNLLQGIAAENLSKQKLTSWILQNEIVKEVNENPNAGWKASFNDRFANATVAEFKRLLGVKPTPKTEFLGVPIVSHDISLKLPKEFDARTAWSQCTSIGRILDQGHCGSCWAFGAVESLSDRFCIKYNMNVSLSVNDLLACCGFLCGQGCNGGYPIAAWRYFKHHGVVTEECDPYFDNTGCSHPGCEPAYPTPKCARKCVSGNQLWRESKHYGVSAYKVRSHPDDIMAEVYKNGPVEVAFTVYEDFAHYKSGVYKHITGTNIGGHAVKLIGWGTSDDGEDYWLLANQWNRSWGDDGYFKIRRGTNECGIEHGVVAGLPSDRNVVKGITTSDDLLVSSF
Protein: Collagen and calcium-binding EGF domain-containing protein 1 (Full of fluid protein homolog) (Q6UXH8)
Organism: Homo sapiens (Human)
Function: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis.
Subcellular location: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.
Interaction partners:
- Vascular endothelial growth factor C
- A disintegrin and metalloproteinase with thrombospondin motifs 2
- A disintegrin and metalloproteinase with thrombospondin motifs 3
Sequence:
MVPPPPSRGGAARGQLGRSLGPLLLLLALGHTWTYREEPEDGDREICSESKIATTKYPCLKSSGELTTCYRKKCCKGYKFVLGQCIPEDYDVCAEAPCEQQCTDNFGRVLCTCYPGYRYDRERHRKREKPYCLDIDECASSNGTLCAHICINTLGSYRCECREGYIREDDGKTCTRGDKYPNDTGHEKSENMVKAGTCCATCKEFYQMKQTVLQLKQKIALLPNNAADLGKYITGDKVLASNTYLPGPPGLPGGQGPPGSPGPKGSPGFPGMPGPPGQPGPRGSMGPMGPSPDLSHIKQGRRGPVGPPGAPGRDGSKGERGAPGPRGSPGPPGSFDFLLLMLADIRNDITELQEKVFGHRTHSSAEEFPLPQEFPSYPEAMDLGSGDDHPRRTETRDLRAPRDFYP
Protein: Bromodomain adjacent to zinc finger domain 2A (F8VU39)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEANDHFNFTGLPPAPAASGLKPSPSSGEGLYTNGSPMNFPQQGKSLNGDVNVNGLSTVSHTTTSGILNSAPHSSSTSHLHHPSVAYDCLWNYSQYPSANPGSNLKDPPLLSQFSGGQYPLNGILGGSRQPSSPSHNTNLRAGSQEFWANGTQSPMGLNFDSQELYDSFPDQNFEVMPNGPPSFFTSPQTSPMLGSSIQTFAPSQEVGSGIHPDEAAEKEMTSVVAENGTGLVGSLELEEEQPELKMCGYNGSVPSVESLHQEVSVLVPDPTVSCLDDPSHLPDQLEDTPILSEDSLEPFNSLAPEPVSGGLYGIDDTELMGAEDKLPLEDSPVISALDCPSLNNATAFSLLADDSQTSTSIFASPTSPPVLGESVLQDNSFDLNNGSDAEQEEMETQSSDFPPSLTQPAPDQSSTIQLHPATSPAVSPTTSPAVSLVVSPAASPEISPEVCPAASTVVSPAVFSVVSPASSAVLPAVSLEVPLTASVTSPKASPVTSPAAAFPTASPANKDVSSFLETTADVEEITGEGLTASGSGDVMRRRIATPEEVRLPLQHGWRREVRIKKGSHRWQGETWYYGPCGKRMKQFPEVIKYLSRNVVHSVRREHFSFSPRMPVGDFFEERDTPEGLQWVQLSAEEIPSRIQAITGKRGRPRNTEKAKTKEVPKVKRGRGRPPKVKITELLNKTDNRPLKKLEAQETLNEEDKAKIAKSKKKMRQKVQRGECQTTIQGQARNKRKQETKSLKQKEAKKKSKAEKEKGKTKQEKLKEKVKREKKEKVKMKEKEEVTKAKPACKADKTLATQRRLEERQRQQMILEEMKKPTEDMCLTDHQPLPDFSRVPGLTLPSGAFSDCLTIVEFLHSFGKVLGFDPAKDVPSLGVLQEGLLCQGDSLGEVQDLLVRLLKAALHDPGFPSYCQSLKILGEKVSEIPLTRDNVSEILRCFLMAYGVEPALCDRLRTQPFQAQPPQQKAAVLAFLVHELNGSTLIINEIDKTLESMSSYRKNKWIVEGRLRRLKTVLAKRTGRSEVEMEGPEECLGRRRSSRIMEETSGMEEEEEEESIAAVPGRRGRRDGEVDATASSIPELERQIEKLSKRQLFFRKKLLHSSQMLRAVSLGQDRYRRRYWVLPYLAGIFVEGTEGNLVPEEVIKKETDSLKVAAHASLNPALFSMKMELAGSNTTASSPARARGRPRKTKPGSMQPRHLKSPVRGQDSEQPQAQLQPEAQLHAPAQPQPQLQLQLQSHKGFLEQEGSPLSLGQSQHDLSQSAFLSWLSQTQSHSSLLSSSVLTPDSSPGKLDPAPSQPPEEPEPDEAESSPDPQALWFNISAQMPCNAAPTPPPAVSEDQPTPSPQQLASSKPMNRPSAANPCSPVQFSSTPLAGLAPKRRAGDPGEMPQSPTGLGQPKRRGRPPSKFFKQMEQRYLTQLTAQPVPPEMCSGWWWIRDPEMLDAMLKALHPRGIREKALHKHLNKHRDFLQEVCLRPSADPIFEPRQLPAFQEGIMSWSPKEKTYETDLAVLQWVEELEQRVIMSDLQIRGWTCPSPDSTREDLAYCEHLSDSQEDITWRGRGREGLAPQRKTTNPLDLAVMRLAALEQNVERRYLREPLWPTHEVVLEKALLSTPNGAPEGTTTEISYEITPRIRVWRQTLERCRSAAQVCLCLGQLERSIAWEKSVNKVTCLVCRKGDNDEFLLLCDGCDRGCHIYCHRPKMEAVPEGDWFCTVCLAQQVEGEFTQKPGFPKRGQKRKSGYSLNFSEGDGRRRRVLLRGRESPAAGPRYSEEGLSPSKRRRLSMRNHHSDLTFCEIILMEMESHDAAWPFLEPVNPRLVSGYRRIIKNPMDFSTMRERLLRGGYTSSEEFAADALLVFDNCQTFNEDDSEVGKAGHIMRRFFESRWEEFYQGKQANL
Protein: Suprabasin (Q6UWP8)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Keratinocyte differentiation-associated protein
- Protein-glutamine gamma-glutamyltransferase E
- Dermokine
Sequence:
MHLARLVGSCSLLLLLGALSGWAASDDPIEKVIEGINRGLSNAEREVGKALDGINSGITHAGREVEKVFNGLSNMGSHTGKELDKGVQGLNHGMDKVAHEINHGIGQAGKEAEKLGHGVNNAAGQVGKEADKLIHHGVHHGANQAGSEAGKFGQGVDNAAGQAGNEAGRFGQGVHHAAGQAGNEAGRFGQGVHHAAGQAGNEAGRFGQGAHHGLSEGWKETEKFGQGIHHAAGQVGKEAEKFGQGAHHAAGQAGNEAGRFGQGVHHGLSEGWKETEKFGQGVHHTAGQVGKEAEKFGQGAHHAAGQAGNEAGRFGQGAHHAAGQAGNEAGRFGQGVHHGLSEGWKETEKFGQGVHHAASQFGKETEKLGHGVHHGVNEAWKEAEKFGQGVHHAASQVGKEEDRVVQGLHHGVSQAGREAGQFGHDIHHTAGQAGKEGDIAVHGVQPGVHEAGKEAGQFGQGVHHTLEQAGKEADKAVQGFHTGVHQAGKEAEKLGQGVNHAADQAGKEVEKLGQGAHHAAGQAGKELQNAHNGVNQASKEANQLLNGNHQSGSSSHQGGATTTPLASGASVNTPFINLPALWRSVANIMP
Protein: COP9 signalosome complex subunit 9 (Q03981)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the COP9 signalosome (CSN) complex that acts as a regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:14562095}. Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- 26S proteasome regulatory subunit RPN5
- Cop9 signalosome complex subunit 11
- COP9 signalosome complex subunit 10
- COP9 signalosome complex subunit 5
- Cop9 signalosome-interactor 1
- Cop9 signalosome complex subunit 12
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit C
Sequence:
MVMREETIKSLEDPYKYHYKEEWLNTKDPDEQQLFEIFAFGNIKDLPENIILTSLMRSKLEKLTLVTLSEIYNELSYELIKEECQIEDDGIIESHLIQLQNIFKAEMDSVSKSMKFSRRFDCRDVYCHEKELTIIKNPRVTKEYLVQNLRSWETKLKQNILE
Protein: C-1-tetrahydrofolate synthase, cytoplasmic (EC 1.5.1.5) (EC 3.5.4.9) (EC 6.3.4.3) (V9GYY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAILQVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEVMKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPEKDVDGLTSINAGKLARGDLNDCFIPCTPKGCLELIKETGVPIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAHLDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYVPDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAKRFLEKFKPGKWMIQYNNLNLKTPVPSDIDISRSCKPKPIGKLAREIGLLSEEVELYGETKAKVLLSALERLKHRPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLYQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVPSVNGVRRFSDIQIRRLKRLGIEKTDPTTLTDEEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQAPTEKGHTRTAQFDISVASEIMAVLALTTSLEDMRERLGKMVVASSKKGEPVSAEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLCPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYIQENLELVEKGFSNLKKQIENARMFGIPVVVAVNAFKTDTESELDLISRLSREHGAFDAVKCTHWAEGGKGALALAQAVQRAAQAPSSFQLLYDLKLPVEDKIRIIAQKIYGADDIELLPEAQHKAEVYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFILPIRDIRASVGAGFLYPLVGTVSACCKGVVGASALLV
Protein: Anaphase-promoting complex subunit 4 (Q04601)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. In early mitosis, the APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5, and other anaphase inhibitory proteins for proteolysis, thereby triggering the separation of sister chromatids at the metaphase-to-anaphase transition. In late mitosis and in G1, degradation of CLB5 allows activation of the APC/C by CDH1, which is needed to destroy CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and creating the low CDK state necessary for cytokinesis and for reforming prereplicative complexes in G1 prior to another round of replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Anaphase-promoting complex subunit DOC1
- Anaphase-promoting complex subunit SWM1
- Anaphase-promoting complex subunit 9
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit MND2
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit CDC16
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit CDC26
- Anaphase-promoting complex subunit CDC23
Sequence:
MSSPINDYFIDYNPLFPIFATRIAKGLAIYRVSDHARLAVIPIRNINLVANYDWDTTTGKFLSIFFKDGTIRIHDIFKDGRLVSFLRIPSTKISKGIWDRIPLRYEPNNRDFACNIIDDLPKLIRFVKDSKRINIVPYTQPNSLWRGPDEDDLDSNEKLDVHVVFNEGNDKITVFFNGDYAVFLSVDNIENENSLKSIIKVQDGFYQCFYEDGTVQTLNLGPLLQSKSSVNLLNYIMVIKELIGYMLTHLEFINRELATPYLDFVKRLCDEAYGYGKLKSELEALFLLGEISCDLEDWLCNSVGEKNFKRWKYLGCEAYQKTVQILTLIFVPACERIIIYVEKLRAILQAFSIQNKLSYTSDLTAVEVLLKSSQKLLTMTLNSIIGLGRDETLFEKFFIWFNDRLHEALDEDYKLKFQFEDDLYFGYDLLSYFDRILSKKGTEPSSIIDVKLYRDLINSMSDMEKDIAQSNVNSHIQQHILVDLKTDVFAQKYPSSQINLLDAIKLPKHNYIVYLIQVTKHNSAQEPFSEENKKKLYIGTLKDENLGIISKESSVKIPALFKSYRLSSTRFVPNRVHSLLRDIGLSDSNYHSSHVTDYRGENYENEEDDGTIAIPAYIRENRENDDFIACTAKVSVDGRSASLVFPKEKQNV
Protein: Protein-arginine deiminase (EC 3.5.3.15) (F1NP39)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR001247}.
Interaction partners:
Sequence:
MAQQRRVQLCTQRPTSTVCVLGTELSLDIQGSAPKDAIAFHVQGTPGVKVYVVHETQSVKLPSSVTRWPLATGTEVLLTMEAISKDVGDEKVRISYFGEASGVPVGRAMLYLTCVDISLDADTGRNGSVSKTLVDKATWTWGPDGHGAILLVNCDCDDPKSRLMGDSSEPQSQLTDNRDTVVCSYEDLKDMSQMVLRTRGPRTIFTGHGLVLHVNFSDADKVGVFYGGNSIALEEYKHVLGGEKLAYAVKPSQHQEESIFYVEGLAFPDVSFSGLVAFHVTLLESPEKGLLETPIFTDTVVFRMAPWIMTPNTLAPLEVFVCSVKDNEDFVAAVSALAEEAKCPVTICPLPENRNDRWIQDEVEFGYVQAPHKMFPVVLDSPRDRGLKDFPVRSILGPDFGYVAQETPENTSSLDSFGNLEVSPPVTVRSKEYPLGRILIGSSFPRFGGRRMAKAVRNFLAAQRVQAPVELFSDWLQVGHVDEFLSFIPAPDRKGFRLLLASPSACYQLLREKQEMGYGEATMFQGLHGVPKPSISEILGNEALRKFNAYAQSCISWNRDILKRELGLAEQDIIDIPQLFQADHQARAVAYFPDMVNMLVLGRHLGIPKPFGPLVDGQCCLEERVRALLQPLGLSCTFINDYFSYHKLAGEVHCGTNVRRKPFAFKWWRMVP
Protein: S5 DRBM domain-containing protein (SEL-1) (G5EFG0)
Organism: Caenorhabditis elegans
Interaction partners:
- Derlin-2
- E3 ubiquitin-protein ligase hrd-1
- Derlin-1
- Transitional endoplasmic reticulum ATPase homolog 2
- Endoplasmic reticulum lectin 1
- MRH domain-containing protein
- E3 ubiquitin ligase rnf-5
- Small ribosomal subunit protein uS5m
- E3 ubiquitin-protein ligase hrd-like protein 1
- Transitional endoplasmic reticulum ATPase homolog 1
Sequence:
MIKTYLTLLLLATSATCQKKSATLVSAEGEAPAIKVIKTTGSLLTAIDVSKADLDWEQVTSQQDENKSNREIPKVISEEYLAEKVEQPPSPEAEAEFQRGMAYIERGKGHGREGRVAAHRVFERAAAQGHQEARKAVAFSQMFGDYSRWSIQEAKTVFEDLEKNGSPDAQLALGFMHGAGIGVEKSNQAKALVYYMFSALGGNPLAQMAMGFRYSHGVGVPQNCETALSYYQKVAKTVVDNVKFTTGQTIQRLRLTDETDPTIHMQPGSAPLESNLLEYYKMLADKGDTSAQLGLGQIYLAGGRGLNQNFELAFRYLLAAAESGSADALTYLGKMYLDGTPFTPKDYQKSFEYLMKSADKSSPSAQAVLGAMYMKGKGVKKNYEKALKLLTLSADKKNADGQMYLAELHYKGVPTNKGVHRDFKKSVKLYQLASQNGHILAYYNLAQMHAAGTGVPRSCSHAVDLFKSVAERGKWGERLMEAHSAYKDNRVDEAAMKYLFMAELGYEVAQTNLAYILDRGEATSLFSGPKDNNMERAFLNWQRSANQEYAAARVKLGDYYYYGLGTEVDHSLAFSNYKMAVDRHGVAQAMFNLGYMHEVGEGITRDLYLAKRFYDQAIEHSQDAYMPSKLALAKLAFVFYLEELNKLPLISFMEKTVGPRWDAILMTVSALVPLFLFWRHRQNDN
Protein: Aldo-keto reductase family 1 member B10 (A0A0G2JT64)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MATFVELSTKAKMPIVGLGTWKSTPNQVKEAVKAAIDAGYRHIDCAYAYCNENEVGEAIQEKIKEKAVRREDLFIVSKLWPTCFEKKLLKEAFQKTLTDLKLDYLDLYLIHWPQGFQAGKELFPKDEQGNVLPSKTTFLEAWEGMEELVDQGLVKALGVSNFNHFQIERLLNKPGLKHKPVTNQVECHPYLTQEKLIQYCHSKGIVVTAYSPLGSPDRPRAKPDDPSLLQDPKIKEIAAKHKKTTAQVLIRFHIQRNVVVIPKSVTPARIQENIQLSDQEMATILSFNRNWRACLLPETVNMEEFPYDAEY
Protein: Cell division control protein 18 (P41411)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Part of the checkpoint control that prevents mitosis from occurring until S phase is completed. Plays a key role in coupling S phase to start and mitosis. Acts at the initiation of DNA replication and plays a major role in controlling the onset of S-phase. Together with orc1, involved in the maintenance of replication forks and activation of cds1-dependent S-phase checkpoint. Together with orc2, plays a role in preventing DNA rereplication and resulting genetic instability.
Interaction partners:
- Origin recognition complex subunit 3
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm7
- Origin recognition complex subunit 5
- Origin recognition complex subunit 6
- DNA replication licensing factor mcm2
- Origin recognition complex subunit 4
- DNA replication licensing factor mcm6
- Origin recognition complex subunit 2
- Cell division cycle protein cdt1
Sequence:
MCETPIGCHTPRRCNRFIDSAALIDCTNKTNQREHSPSFSIEIPTTPSRKRTLASSHFQTPTKRIKYELGELQEEKTDLYPNFPAQLKENKKPKLPTTPQTPKTPKRTIQIVTPKSLNRTCNPVPFATRLLQSTPHRQLFPPTPSTPSTPSYNSTAKLSLRKSYRSAGVVGRENEKSIVESFFRQHLDANAGGALYVSGAPGTGKTVLLHNVLDHVVSDYPKVNVCYINCMTINEPKAIFEKIHSKIVKEEILENEDHHINFQCELESHFTQSANELYNPVIIVLDEMDHLIAREQQVLYTLFEWPSRPTSRLILVGIANALDMTDRFLPRLRTKHITPKLLSFTPYTAQEISTIIKARLKTAATTSEKNNPFTPIKSISEVSDDSINVVSQHADETPFIHPAAIELCARKVAASSGDLRKALDICRHAIELAEREWKAQHDNTLSSVDIPRASIAHVVRATSAMSQSASARLKNLGLQQKAILCTLVVCEKTSLSVADVFEKYSSLCLRDRLIYPLTSSEFCDVANSLETLAIIRLRTKQRNGKPQDRIISLLVPEMDVITAVGDIGTLKRFFDRR
Protein: tRNA (guanine(37)-N(1))-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5) (P38793)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding. Postspliced cytoplasmic tRNAs are imported into the nucleus, where this first step seems to take place, after which they are reexported to the cytoplasm, where the yW sythesis is completed by cytoplasmic enzymes.
Subcellular location: Mitochondrion matrix. Nucleus. Cytoplasm. Note=Predominantly in the mitochondria and in the nucleus.
Interaction partners:
- tRNA wybutosine-synthesizing protein 3
- tRNA wybutosine-synthesizing protein 2
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- tRNA
- tRNA wybutosine-synthesizing protein 4
- tRNA
- tRNA
- tRNA
- Multisite-specific tRNA:
- tRNA
Sequence:
MKIALPVFQKFNRLISSCKMSGVFPYNPPVNRQMRELDRSFFITKIPMCAVKFPEPKNISVFSKNFKNCILRVPRIPHVVKLNSSKPKDELTSVQNKKLKTADGNNTPVTKGVLLHESIHSVEDAYGKLPEDALAFLKENSAEIVPHEYVLDYDFWKAEEILRAVLPEQFLEEVPTGFTITGHIAHLNLRTEFKPFDSLIGQVILDKNNKIECVVDKVSSIATQFRTFPMKVIAGKSDSLVVEQKESNCTFKFDFSKVYWNSRLHTEHERLVKQYFQPGQVVCDVFAGVGPFAVPAGKKDVIVLANDLNPESYKYLKENIALNKVAKTVKSFNMDGADFIRQSPQLLQQWIQDEEGGKITIPLPLKKRHRSQQHNDQQPPQPRTKELIIPSHISHYVMNLPDSAISFLGNFRGIFAAHTKGATDTIQMPWVHVHCFEKYPPGDQVTEDELHARVHARIIAALKVTADDLPLNAVSLHLVRKVAPTKPMYCASFQLPANV
Protein: Uncharacterized protein (Q2F941)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGLRFDKSIEQEIEDFFASKNLDTVAQSPYIGLIRAVELLEKEGDGPAPANGNDAGSPGPAGSERLSSSGSSVNQPEPLTQDLLADAVTYESPNYLSDAESTNSLGPVTDLASPLDPFSIHPIMDLLMGNYYLAFTNESLSMAVTVVFLLLRVYFLYIWVRAAFPRYRYDQLMGLSDDPKLKD
Protein: Fatty acid-binding protein, heart (Fatty acid-binding protein 3) (Heart-type fatty acid-binding protein) (H-FABP) (Mammary-derived growth inhibitor) (MDGI) (Muscle fatty acid-binding protein) (M-FABP) (P05413)
Organism: Homo sapiens (Human)
Function: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.
Subcellular location: Cytoplasm.
Interaction partners:
- Aspartate aminotransferase, mitochondrial
- Fatty acid-binding protein, liver
- Fatty-acid amide hydrolase 1
- Platelet glycoprotein 4
- Lysosome membrane protein 2
- Hormone-sensitive lipase
- Scavenger receptor class B member 1
- Troponin I, cardiac muscle
- Myoglobin
Sequence:
MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA
Protein: cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B (EC 3.1.4.17) (CGI PDE) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B) (RcGIPl) (Q63085)
Organism: Rattus norvegicus (Rat)
Function: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Regulates angiogenesis by inhibiting the cAMP-dependent guanine nucleotide exchange factor RAPGEF3 and downstream phosphatidylinositol 3-kinase gamma-mediated signaling (By similarity). Controls cardiac contractility by reducing cAMP concentration in cardiocytes (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q61409}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Hypoxanthine-guanine phosphoribosyltransferase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
- Guanylate kinase
- GTP:AMP phosphotransferase AK3, mitochondrial
- RAC-gamma serine/threonine-protein kinase
Sequence:
MRKDERERDTPAMRSPPPPPPPATATAASPPESLRNGYVKSCVSPLRQDPPRSFFFHLCRFCNVEPPAASLRAGARLSLAALAAFVLAALLGAGPERWAAAATGLRTLLSACSLSLSPLFSIACAFFFLTCFLTRAQRGPDRGAGSWWLLALPACCYLGDFAAWQWWSWLRGEPAAAAAGRLCLVLSCVGLLTLAPRVRLRHGVLVLLFAGLVWWVSFSGLGALPPALRPLLSCLVGGAGCLLALGLDHFFHVRGASPPPRSASTADEKVPVIRPRRRSSCVSLGESAAGYYGSGKMFRRPSLPCISREQMILWDWDLKQWCKPHYQNSGGGNGVDLSVLNEARNMVSDLLIDPSLPPQVISSLRSISSLMGAFSGSCRPKINSFTPFPGFYPCSEVEDPVEKGDRKLHKGLSSKPSFPTAQLRRSSGASGLLTSEHHSRWDRSGGKRPYQELSVSSHGCHLNGPFSSNLMTIPKQRSSSVSLTHHAGLRRAGALPSPSLLNSSSHVPVSAGCLTNRSPVGFLDTSDFLTKPSVTLHRSLGSVSSAADFHQYLRNSDSSLCSSCGHQILKYVSTCEPDGTDHHNEKSGEEDSTVFSKERLNIVETQEEETVKEDCRELFLEGDDHLMEEAQQPNIDQEVLLDPMLVEDYDSLIEKMSNWNFQIFELVEKMGEKSGRILSQVMYTLFQDTGLLETFKIPTQEFMNYFRALENGYRDIPYHNRVHATDVLHAVWYLTTRPIPGLQQLHNNHETETKADSDARLSSGQIAYLSSKSCCIPDKSYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQAVLYNDRSVLENHHAASAWNLYLSRPEYNFLLNLDHMEFKRFRFLVIEAILATDLKKHFDFLAEFNAKANDVNSNGIEWSSENDRLLVCQVCIKLADINGPAKDRDLHLRWTEGIVNEFYEQGDEEATLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWIEAEEGDDTESDDDDDDDDDDDDDDDEELDSDDEETEDNLNPKPQRRKGRRRIFCQLMHHLTENHKIWKEIIEEEEKCKAEGNKLQVDNASLPQADEIQVIEEADEEEEQMFE
Protein: Transmembrane protein, putative (DUF594) (Q9FHI8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVNAIPKPIKDIWDEWSIRSTLIFSLSLQTFLIFFAPQRKRSSRKVLLSFIWSAYLLADWSANFAAGQISDSQGDDPEPGEPKKSAELFAFWVPFLLLHLGGPDTITALALEDNELWLRHLLGLFFQSVATVYVLLQSLPNALWKPILLVFATGVIKYVERTLALYLASLDKFKDSMIQRPDPGPNYAKLMEEYAAKKDMKMPTQIIKVGEPEKDPRDDAPVKPPDGFTPLNILQYAYKYFNIFKGLVVDLIFTFQQRAESKRFFDSLKAEEALRILEVELNFIYAALYTKAEILHNWIGFLFRFIALGCLAAALRIFQYKSKKDYSGFDVGLTYALLLGGIALDCIALIMFCASDWTFVRLRKMKDEVDDPPTWSDNILNWILENILGVRKLKVEEYDECYKNTQSHEVPNTSTKKTPFLKRILNRILRVRELKTEKSHEVLDKSTSKIPGQEVPDKSAKTIPCHKVLDTSFMYRRWSEYVHAHNLIEYCLGLKPKRIHHTKGFIHIAFDKVINILYIGPAFTKLGSVIESCFRVTKQRIHQTFKWIDGKVSRLCKKYPKLNEEYIRFSFFCIFYIPSLPGRWIKSFMEFFGIRAQLDEVIYTSSDRLTLDMWEHIFGEVKAKSRFADDSESAMRVSSARGDWTLRDIQGDPETEKKREKLLRYVMEMDYDQSLLVWHIATELLYQTKKGTKANHSAREFSKILSDYMMYLLMMQPTLMSAVVGIGKIRFRDTCEEAQRFFDRRHIMGISAKKAPDAKEASVAILSVAVPAKAEPIDVKGDRSKSVLFDGAMLAKELKGLRKNKEDDSEMWKIMSQVWVELLSYAATKCGAIEHAAQLSKGGELISFVWLLMAHFGLGDQFQINQGDARAKLIIGK
Protein: Peroxisomal nicotinamide adenine dinucleotide carrier (Peroxisomal NAD carrier) (Peroxisomal membrane protein 38, (PMP36)) (AtPMP38) (Protein ABERRANT PEROXISOME MORPHOLOGY 3) (Solute carrier family 25 member 17) (O04200)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates the NAD(+) import into peroxisomes. Favors the NAD(+)(in)/AMP(out) antiport exchange, but is also able to catalyze a low unidirectional transport that might be essential under special conditions. Transports CoA, dephospho-CoA, acetyl-CoA, adenosine 3',5'-diphosphate (PAP), NAD(+), AMP, ADP and NADH, but has no activity with ATP, GTP, GDP, NADPH, NADP(+) or FAD. Required for peroxisomes proliferation.
Subcellular location: Glyoxysome membrane {ECO:0000269|PubMed:11522909, ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}; Multi-pass membrane protein {ECO:0000269|PubMed:11522909, ECO:0000269|PubMed:19073763, ECO:0000269|PubMed:21895810}.
Interaction partners:
- ABC transporter D family member 1
- Peroxisome biogenesis protein 12
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase
- Probable ADP,ATP carrier protein At5g56450
- Peroxisome biogenesis protein 19-1
- Peroxisome biogenesis protein 19-2
- Peroxisome biogenesis protein 16
- Nicotinate phosphoribosyltransferase 2
- Nicotinate phosphoribosyltransferase 1
- Mitochondrial fission 1 protein A
Sequence:
MSDALINGLAGAGGGIIAQLLTYPLQTVNTRQQTERDLKREKRKLGTIEHMCQVVKQEGWERLYGGLAPSLAGTAASQGVYYYFYQVFRNRAEATALARKKKGLGDGSVGMFASLLVAAFAGSVNVLMTNPIWVIVTRMQTHRKMTKDQTAAPESPSSNAEALVAVEPRPYGTFNTIREVYDEAGITGFWKGVIPTLIMVSNPSMQFMLYETMLTKLKKKRALKGSNNVTALETFLLGAVAKLGATVTTYPLLVVKSRLQAKQVTTGDKRQQYKGTLDAILKMIRYEGLYGFYKGMSTKIVQSVLAAAVLFMIKEELVKGAKLLLSNATSS