wanglab/gogpt-training-data huggingface dataset:
Protein: ARM repeat superfamily protein (Q9SV06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g43860
- Heat shock 70 kDa protein 17
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Heat shock 70 kDa protein 4
- Large ribosomal subunit protein bL28c
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
Sequence:
MPTIFFFRYVFLLVVISLVGFSIAEKVNSSGGMVWSSVRDEAELVEDSGVVIGEQDQIDGGFSSLDGMLHWAIGHSDPATLKEAAKDAEKMSLDELQKRQLELKELVEKLKMPSNAKLMQIAIDDLNNSSLSLEDRHRALQELLILVEPIDNANDLSKSGGLRVVAGELNHDDTEVRKLAAWVLGKASQNNPFVQEQVLELGALTTLIKMVNSSSTEEAVKALFAVSALIRNNIAGQDLFFAAHGYIMLRDVMNNGSLDMKLRRKAVFLVGDLAESQLQNTEKDELPIFKDRLFLKSVVDLIVVLDLDLQEKALTAIQTLLQLKSIEPQVLKESCGLEEALERMKLQLEESMADEYKRDYAADVESIRGEVELIFRQKLGLL
Protein: ECF RNA polymerase sigma factor SigM (ECF sigma factor SigM) (Alternative RNA polymerase sigma factor SigM) (RNA polymerase sigma-M factor) (Sigma-M factor) (O53590)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Extracytoplasmic function (ECF) sigma factors are held in an inactive form by an anti-sigma factor (RsaM, AC L7N5D7) until released by regulated intramembrane proteolysis (Probable). This sigma factor is required for the synthesis of surface or secreted molecules.
Interaction partners:
- ECF RNA polymerase sigma factor SigL
- ECF RNA polymerase sigma factor SigC
- ECF RNA polymerase sigma factor SigD
- Anti-sigma-M factor RsmA
- ECF RNA polymerase sigma factor SigK
- Conserved protein
- Probable ECF RNA polymerase sigma factor SigI
- ECF RNA polymerase sigma factor SigJ
- ECF RNA polymerase sigma factor SigG
- Probable peptidoglycan biosynthesis protein MviN
Sequence:
MPPPIGYCPAVGFGGRHERSDAELLAAHVAGDRYAFDQLFRRHHRQLHRLARLTSRTSEDADDALQDAMLSAHRGAGSFRYDAAVSSWLHRIVVNACLDRLRRAKAHPTAPLEDVYPVADRTAQVETAIAVQRALMRLPVEQRAAVVAVDMQGYSIADTARMLGVAEGTVKSRCARARARLARLLGYLNTGVNIRR
Protein: Uncharacterized transporter C1529.01 (Q9USN4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDLEKKPQDKVETAEIDVKEDPFLVTWQSPTDPKNPKNWIYARKWTQLILVSAFALLGPMASSMVAPCLDQIADRFHIQNSTEKALILSIYLLVFAISPMISAPLSEVFGRRMLLQVGNVIFIVFNMACGLARTKAQMYIFRFLAGFGSATPMGLGSGTISDLFTPDERGKAVAVMSLAPLLGPTIGPVVSGFIAEYTTYKWIFWSTTIFSGFIFALSLPLLAETYPKTLLGEKARKLNKSEKTNKYHTEWNLEHIPRLKLVTPALMRPIRMLFTQPIVILCSTYMAIQYGILYLVLTTYPTLWTEEYHERPSIAGLNYIASGIGLIFGSQASGIFIDKTFRYLKRRNNGKMAPEFRVPVILLGTFFFPAGLFIYGWTAQYHTHWIGPDIGAAMFNIGLMLGWRGIQTYLIDSFMIYAASSTAVACCVRSIAAFAFPLFGQDMYDTLGYGWGNSLLAFIVLGSSIITCSLLWFGGKRLRALSSMVIFKDDV
Protein: At4g13160 (Q9SVR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDYQESYRLTFYGILVAFMELAFAYCLLCVSAFVFITSKLLLFMPCIGYQNSDLCIQKLLFDWPFRIILRVQKLATTNRPSVLHHQEQEQEQEQEQEEKTMVDKDKNSELMDRVRLLEVAVEQEKVAKAALMVELEQERAASASAADEAMAMILRLQADKASLEMEGKQYERMIDEKFAYDEEEMNILKEILFKREREKHFLEKELETYKHIDDDQETEDNEKRECDEDGEPIVYDVHVIEDNSQTKVRDDDVAEHKEMKEEEIVKDHDSVSSPTSSSTHLP
Protein: 2-ketoarginine methyltransferase (EC 2.1.1.243) (5-guanidino-2-oxopentanoate (3R)-methyltransferase) (SAM-dependent methyltransferase MrsA) (D5FKJ3)
Organism: Pseudomonas syringae pv. syringae
Function: S-adenosyl-L-methionine-dependent methyltransferase involved in the formation of 3-methylarginine (MeArg), a potent antibiotic against the closely related soybean pathogen P.syringae pv. glycinea. Transfers the methyl group from S-adenosyl-L-methionine into 5-guanidino-2-oxopentanoate acid to yield 5-guanidino-3-methyl-2-oxopentanoate5-guanidino-3-methyl-2-oxopentanoate, a precursor of MeArg.
Interaction partners:
Sequence:
MNLLDSIKSENTGFETTLIKGIEPIRQFVLAISIYHLFDTKLFSLLIKHEVASPEVACNELGMEKEKLLGLFRYLKNEGILLETIDGFSLSKEGHALAPFEGWYVMLVGGYATTFLQMGERLQEGAGWATRDATKVGVGSCGISHFDAIPLTRSLMAQAPGTCTKLLDLGCGNGRYLAEFCKALPQIQAWGAEPDRGGFEEAVDLIEKEGLSHRVHISHSGAVEFLDSDFDFEPDFIVLGFVLHEILGQAGRPAVVNFLKKIVHRFPAINLIIIEVDNQFDNAGAMRHGLALAYYNPYYLLHCFTNQLLVQDADWLDIFAEAGLSLVTRETTSDQVDSTGLEIGYLLRRA
Protein: Monoglyceride lipase, putative (Q57U43)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acyltransferase
- glycerol kinase
- glycerol kinase
- glycerol kinase
- glycerol kinase
- Monoglyceride lipase, putative
- Fungal lipase-type domain-containing protein
- Lipase-like protein, putative
- Fatty acyl CoA synthetase, putative
- Long-chain-fatty acid-CoA ligase protein, putative
Sequence:
MGCFCCCCCCAVRDSHDLKYATPDRVPPDGELFPWYIQNRQGLWLHFRDWPPPRDVPNVRGVLFIVSGLGEHTARYGGVGRYFSREGFHVFCMDNQGAGASEGARLYVSDFDDFIVDFFLFKRHVFSLYPEYEALPRFLLGHSMGGLIATHVSLRDPTGFTGFIFSGPALKPHPKLASCFKQCCVGLMSSCVPKFGVGSIDPKSVSTNRQVVELLEQDPLNFDAKLTARWGKTMLDAMESVWTQVERATYPVLILHGAKDALCPISGSRKFLESVPTTDKQLIEYPGLGHEVLTEVRWREVLGDILKFINAHCK
Protein: Vesicle transport protein SEC20 (BCL2/adenovirus E1B 19 kDa protein-interacting protein 1) (Transformation-related gene 8 protein) (TRG-8) (Q12981)
Organism: Homo sapiens (Human)
Function: As part of a SNARE complex may be involved in endoplasmic reticulum membranes fusion and be required for the maintenance of endoplasmic reticulum organization. Also plays a role in apoptosis. It is for instance required for endoplasmic reticulum stress-induced apoptosis. As a substrate of RNF185 interacting with SQSTM1, might also be involved in mitochondrial autophagy (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:23896122}; Single-pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:21931693, ECO:0000269|PubMed:23896122}; Single-pass type IV membrane protein {ECO:0000255}. Note=Localization to the mitochondrion is regulated by RNF186. {ECO:0000269|PubMed:23896122}.
Interaction partners:
- Syntaxin-18
- RAD50-interacting protein 1
- Vesicle transport protein USE1
- Vesicle-trafficking protein SEC22b
- Centromere/kinetochore protein zw10 homolog
- Zinc finger protein 787
- Alpha-soluble NSF attachment protein
- Golgi SNAP receptor complex member 2
- Syntaxin-6
- NBAS subunit of NRZ tethering complex
Sequence:
MAAPQDVHVRICNQEIVKFDLEVKALIQDIRDCSGPLSALTELNTKVKEKFQQLRHRIQDLEQLAKEQDKESEKQLLLQEVENHKKQMLSNQASWRKANLTCKIAIDNLEKAELLQGGDLLRQRKTTKESLAQTSSTITESLMGISRMMAQQVQQSEEAMQSLVTSSRTILDANEEFKSMSGTIQLGRKLITKYNRRELTDKLLIFLALALFLATVLYIVKKRLFPFL
Protein: FERM and PDZ domain containing 4 (D4A3K7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- G-protein signaling modulator 2
Sequence:
MEEDLEGENWSTFPIPWGFGKAVEDNREHVCRHRTKSSGWPPPSGTWGLNQVPPYGWEMMTNRDGRDYFINHMTQAIPFDDPRFDSCQIIPPAPRKVEMRRDPVLGFGFVAGSEKPVVVRSVTPGGPSEGKLIPGDQIVMINDEPVSAAPRERVIDLVRSCKESILFTVIQPYPSPKSAFISAAKKARLKSNPVKVRFSEEVIINGQVSETVKDNSLLFMPNVLKVYLENGQTKSFRFDCSTSIKDVILTLQEKLSIKGIEHFSLMLEQRTEGAGTKLLLLHEQETLTQVTQRPSSHKMRCLFRISFVPKDPIDLLRRDPVAFEYLYVQSCNDVVQERFGPELKYDIALRLAALQMYIATVTTKQTQKISLKYIEKEWGLETFLPSAVLQSMKEKNIKKALSHLVKANQNLVPPGKKLSALQAKVHYLKFLSDLRLYGGRVFKATLVQAEKRSEVTLLVGPRYGISHVINTKTNLVALLADFSHVNRIEMFTEEESLVRVELHVLDVKPITLLMESSDAMNLACLTAGYYRLLVDSRRSIFNMANKKNAGTQDTGTENKGKHNLLGPDWNCMPQMTTFIGEGEQEAQITYIDSKQKAVEMTDSTLCPKEHRHLYIDNTYSSDELSQPLTQPGDAPCEADYRSLAQRSLLTLSGPDTLKKAQESPRGAKVSFIFGDLALDDGMSPPTLGYERMLDENPEMLEKQRNLYISSANDMKNLDLTPDTDSIQFVANSVYANIGDVKNFEAPEGIEEPLLHDICYAENTDDAEDEDEVSCEEDLVVSEINQPAILDLSGSSDDIIDLTTLPPPEGDDNEDDFLLRSLNMAIAAPPPGFRDSSDEEDTQSQATSFHENKEQGSSLQNEEIPVSLIDAVPTSAEGKCEKGLDPTVVSTLEALEALSEEQQKSENSGVAILRAYSPESSSDSGNETNSSEMTEGSELAAAQKQSESLSRMFLATHEGYHPLAEEQTEFPTSKTPSVGLPPKSSHGLAARPATDLPPKVVPSKQILHSDHMEMEPETMETKSVTDYFSKLHMGSVAYSCTSKRKSKLAEGEGKCPLSGNVPGKKQQGTKIAETEEDTKGKVGTVSSRDNPHLSTFNLERTAFRKDSQRWYVASDGGVVEKSGVEAPAMKAFPRGPGLGNREAEGKEDGTMEGEADDASGLGQGERFLSDMACVASAKDLDNPEDTDSPTCDHATKLPEAEDNVARLCDYHLAKRMSSLQSEGHFSLQSSQGSSVDTGCGPGSSSSACATPVESPLCPSMGKHLIPDASGKGGSYISPEERVAGHPNHGATFKELHPQTEGMCPRMTVPALHTAINADPLFGTLRDGCHRLPKIKETTALTEPGKERQGGMPSAWSPHPEADPILLPSNIHLESKVPSPNQDPNDFSQGNQAFGEAVSWRPADLRGGSLRTPPSQRALRHSSSILSGPVGLETFQEGTKGVVSLKYPGITEAQEASSERRAELPLGKKLTKSFSQSSMHFISEGKFHKRSPMSHKDSKVYRTLPLRKLESSNWRCRGPFSYCFLNQGQDEDGDEDEEGEATLQVSCLYRPHITQGMPETSNSSLAVGLQKQGEELSRGTVLKDWTEDPDGPDDLDFSSLAFDARIARINALKANTYGMPDGFLEAQNDANELLCLVRATKAKREESRPEAYDLTLSQYKQLLSIESRQLGSACRKMAMAEKSPEEMLLAMSSSFQVLCCLTEACMRLVKVVNSETQRQEIVEKIDEVVINYICLLKAAEAATGKTTGDPSIGLSMRHSTTMAALVSTLTRSLKMLLNK
Protein: 26S proteasome non-ATPase regulatory subunit 3 (26S proteasome regulatory subunit rpn-3) (Q04908)
Organism: Caenorhabditis elegans
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- Proteasomal ubiquitin receptor ADRM1 homolog
- PCI domain-containing protein
- 26S protease regulatory subunit 6A
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 2
- Probable 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 7
- Probable 26S proteasome regulatory subunit 10B
Sequence:
MAPKTGETVVEKMEVDEAKQDVPATEPAKDLNAIAVENIKEQLAALDKGEEHLITRVLQVLPKTRKQINDNVLYKLVSSHLSSDAQFAEGMLKYLHYTPAADTEVQPMDTSNVKTKSPKKGVKPVFASPESDCYLRLLVLLHLYAQKKNTEALALGENQLTSIYNFDRRTLDGLAAKTLYFLCVIYEREGRLFDHQGFLNSRLRTATLRNFSESQAVLICWLLRCYLINRQYQSAAHLVSKVAFPDNASNNDLARYMYYQGRIKALQLDYNSAAGYFLQAQRKAPQEGAIGFKQAVQKWVVVIGLLQGEIPDRSVFRQPIYRKCLAHYLDLSRGVRDGDVARFNHNLEQFKTQFEADDTLTLIVRLRQNVIKTAIKQISLAYSRIYIKDIAKKLYITNETETEYIVAKAIADGAIDAVITSDVRDGPRYMQSSETADIYRTSEPQAHFDTRIRYCLELHNQAVKALRYPPKKKIAVETIEQAREREQQELEFAKELADEDDDDF
Protein: Large ribosomal subunit protein mL55 (39S ribosomal protein L55, mitochondrial) (L55mt) (MRP-L55) (P0C2B8)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11551941}.
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL16m
- Small ribosomal subunit protein mS25
- Large ribosomal subunit protein mL62
- Large ribosomal subunit protein mL51
- Aurora kinase A interacting protein 1.
- Large ribosomal subunit protein mL52
- Small ribosomal subunit protein uS7m
Sequence:
MSAKGSLLRLLWQCGMTRAAPESCRYLYTSSWRADCNRASLTRVHRQTYARLYPILLVKQDGSTIHIRYPEPRRILTMPVDLDSLSPEERRARFRKREGQLKEKKEEPELADDFDVEQYKQFWTKK
Protein: Glutamate dehydrogenase (A2QHT6)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSNLPHEPEFEQAYKELASTLENSTLFQKNPEYRKALAVVSVPERVIQFRVVWEDDAGNVQVNRGFRVQFNSALGPYKGGLRFHPSVNLSILKFLGFEQIFKNALTGLNMGGGKGGSDFDPKGKSDNEIRRFCVSFMTELCKHIGADTDVPAGDIGVTGREVGFLFGQYRKIRNQWEGVLTGKGGSWGGSLIRPEATGYGVVYYVEHMIAHATNGQESFKGKRVAISGSGNVAQYAALKVIELGGSVVSLSDSQGSLIINGEGSFTPEEIELIAQTKVERKQLASIVGAAPFSDANKFKYIAGARPWVHVGKVDVALPSATQNEVSGEEAQVLINAGCKFIAEGSNMGCTQEAIDTFEAHRTANAGAAAIWYAPGKAANAGGVAVSGLEMAQNSARLSWTSEEVDARLKDIMRDCFKNGLETAQEYATPAEGVLPSLVTGSNIAGFTKVAAAMKDQGDWW
Protein: WD repeat domain 26 (C9JCS7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQESGCRLEHPSATKFRNHVMEGDWDKAENDLNELKPLVHSPHAIVVRGALEISQTLLGIIVRMKFLLLQQKYLEYLEDGKVLEALQVLRCELTPLKYNTERIHVLSGYLMCSHAEDLRAKAEWE
Protein: GH18608p (Q9VAQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSAIFAKIVQLGAVLLVSFVAWASAQDSDIARTCTAYKRSVWEETSEFSFLIENAPIIYKTLDKCTSYAPLIIGGGPAVPKEFPHAARLGHKDENGEVEWFCGGTLISDRHVLTAAHCHYSPQGSVNIARLGDLEFDTNNDDADPEDFDVKDFTAHPEFSYPAIYNDISVVRLSRPVTFNDYKHPACLPFDDGRLGTSFIAIGWGQLEIVPRTENKKLQKVKLYNYGTRCRITADRNDELPEGYNATTQLCIGSNEHKDTCNGDSGGPVLIYHMDYPCMYHVMGITSIGVACDTPDLPAMYTRVHFYLDWIKQQLAKN
Protein: Uncharacterized protein (Q57Y84)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEYQGSPQQEEGDAALAKRLHEELNRSEASGHQEPSDQTGGRRQVECPMCSSVSVVVGAADGVQQVCERCKATTHGGFASGEDNENYSMQKLLLCNICQSYNRVPKGTFDAILCGACGNQLKAGGSVTENLSPEDTRVRTQEIRVRCPKCSSINTVEANTDALSVRFECGSCRYANEVFF
Protein: Serine/threonine-protein phosphatase PP1-beta catalytic subunit (PP-1B) (PPP1CD) (EC 3.1.3.16) (EC 3.1.3.53) (P62140)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E. Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11739654}. Nucleus {ECO:0000269|PubMed:11739654}. Nucleus, nucleoplasm {ECO:0000269|PubMed:11739654}. Nucleus, nucleolus {ECO:0000269|PubMed:11739654, ECO:0000269|PubMed:20926688}. Note=Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles. {ECO:0000269|PubMed:11739654}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 12A
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Protein phosphatase 1 regulatory subunit 15A
- Protein phosphatase 1 regulatory subunit 12B
- WD repeat-containing protein 82
- Protein phosphatase 1 regulatory subunit 12C
- Integrator complex subunit 1
- Integrator complex subunit 6
- Protein phosphatase 1 regulatory subunit 7
Sequence:
MADGELNVDSLITRLLEVRGCRPGKIVQMTEAEVRGLCIKSREIFLSQPILLELEAPLKICGDIHGQYTDLLRLFEYGGFPPEANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVSKFLNRHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGGMMSVDETLMCSFQILKPSEKKAKYQYGGLNSGRPVTPPRTANPPKKR
Protein: RecBCD enzyme subunit RecC (Exodeoxyribonuclease V 125 kDa polypeptide) (Exodeoxyribonuclease V gamma chain) (Exonuclease V subunit RecC) (ExoV subunit RecC) (Helicase/nuclease RecBCD subunit RecC) (P07648)
Organism: Escherichia coli (strain K12)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a rapid (>1 kb/second) and highly processive (>30 kb) ATP-dependent bidirectional helicase. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator, 5'-GCTGGTGG-3') sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to Chi site, by nicking one strand or switching the strand degraded (depending on the reaction conditions). The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang which facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit almost certainly recognizes the wild-type Chi sequence, when added to isolated RecB increases its ATP-dependent helicase processivity. The RecBC complex requires the RecD subunit for nuclease activity, but can translocate along ssDNA in both directions.
Interaction partners:
- RecBCD enzyme subunit RecB
- RecBCD enzyme subunit RecD
- Protease 3
- Exodeoxyribonuclease I
- Protein RecA
- DNA replication and repair protein RecF
- Single-stranded-DNA-specific exonuclease RecJ
- Exodeoxyribonuclease 8
- DNA repair protein RecO
- Crossover junction endodeoxyribonuclease RuvC
Sequence:
MLRVYHSNRLDVLEALMEFIVERERLDDPFEPEMILVQSTGMAQWLQMTLSQKFGIAANIDFPLPASFIWDMFVRVLPEIPKESAFNKQSMSWKLMTLLPQLLEREDFTLLRHYLTDDSDKRKLFQLSSKAADLFDQYLVYRPDWLAQWETGHLVEGLGEAQAWQAPLWKALVEYTHQLGQPRWHRANLYQRFIETLESATTCPPGLPSRVFICGISALPPVYLQALQALGKHIEIHLLFTNPCRYYWGDIKDPAYLAKLLTRQRRHSFEDRELPLFRDSENAGQLFNSDGEQDVGNPLLASWGKLGRDYIYLLSDLESSQELDAFVDVTPDNLLHNIQSDILELENRAVAGVNIEEFSRSDNKRPLDPLDSSITFHVCHSPQREVEVLHDRLLAMLEEDPTLTPRDIIVMVADIDSYSPFIQAVFGSAPADRYLPYAISDRRARQSHPVLEAFISLLSLPDSRFVSEDVLALLDVPVLAARFDITEEGLRYLRQWVNESGIRWGIDDDNVRELELPATGQHTWRFGLTRMLLGYAMESAQGEWQSVLPYDESSGLIAELVGHLASLLMQLNIWRRGLAQERPLEEWLPVCRDMLNAFFLPDAETEAAMTLIEQQWQAIIAEGLGAQYGDAVPLSLLRDELAQRLDQERISQRFLAGPVNICTLMPMRSIPFKVVCLLGMNDGVYPRQLAPLGFDLMSQKPKRGDRSRRDDDRYLFLEALISAQQKLYISYIGRSIQDNSERFPSVLVQELIDYIGQSHYLPGDEALNCDESEARVKAHLTCLHTRMPFDPQNYQPGERQSYAREWLPAASQAGKAHSEFVQPLPFTLPETVPLETLQRFWAHPVRAFFQMRLQVNFRTEDSEIPDTEPFILEGLSRYQINQQLLNALVEQDDAERLFRRFRAAGDLPYGAFGEIFWETQCQEMQQLADRVIACRQPGQSMEIDLACNGVQITGWLPQVQPDGLLRWRPSLLSVAQGMQLWLEHLVYCASGGNGESRLFLRKDGEWRFPPLAAEQALHYLSQLIEGYREGMSAPLLVLPESGGAWLKTCYDAQNDAMLDDDSTLQKARTKFLQAYEGNMMVRGEGDDIWYQRLWRQLTPETMEAIVEQSQRFLLPLFRFNQS
Protein: Nitrophorin Cim l NP (NP) (Salivary nitrophorin) (cNP) (allergen Cim l NP) (O76745)
Organism: Cimex lectularius (Bed bug) (Acanthia lectularia)
Function: Heme-based protein that delivers nitric oxide gas (NO) to the victim while feeding, resulting in vasodilation (Probable). In place of heme, the heme-binding cysteine can also reversibly bind NO when it is present in high concentrations.
Subcellular location: Secreted {ECO:0000305|PubMed:16417223, ECO:0000305|PubMed:22305681, ECO:0000305|PubMed:9716517}.
Interaction partners:
Sequence:
MKLLLSAGAALAFVLGLCAAGSPPAQLSVHTVSWNSGHERAPTNLEELLGLNSGETPDVIAVAVQGFGFQTDKPQQGPACVKNFQSLLTSKGYTKLKNTITETMGLTVYCLEKHLDQNTLKNETIIVTVDDQKKSGGIVTSFTIYNKRFSFTTSRMSDEDVTSTNTKYAYDTRLDYSKKDDPSDFLFWIGDLNVRVETNATHAKSLVDQNNIDGLMAFDQLKKAKEQKLFDGWTEPQVTFKPTYKFKPNTDEYDLSATPSWTDRALYKSGTGKTIQPLSYNSLTNYKQTEHRPVLAKFRVTL
Protein: Probable aminomethyltransferase, mitochondrial (EC 2.1.2.10) (Glycine cleavage system T protein) (GCVT) (O14110)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The glycine cleavage system catalyzes the degradation of glycine.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Putative glycine dehydrogenase
- Putative glycine cleavage system H protein, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Methylenetetrahydrofolate dehydrogenase [NAD
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable thymidylate synthase
- Dihydrofolate reductase
- Bifunctional purine biosynthesis protein ade10
- Methylenetetrahydrofolate reductase 1
Sequence:
MNRSAALSILKRQSSTAASSSLKRTPLYDLHLKEGATIVPFAGFSMPVQYKGQTISASHKWTREHSGLFDVSHMVQWFVRGENATAYLESITPSSLKELKPFHSTLSAFTNETGGIIDDTIISKQDENTYYIVTNAACSEKDEANLKKHIENWKGVELERVQGRALIAIQGPETASVVQKLIPNVDFSVLKFGQSAYVDFKGVKCLFSRSGYTGEDGFEVSIPEEVSVDFASTLLADTRVRPIGLGARDTLRLEAGMCLYGSDIDDTTSPVEGSLSWIIGKRRRKEGGFVGSSRILKELKDGPSRRRVGFIVEKVPARHGSAVEVDGVEVGQVTSGCPSPTLGKNIAMGYISTGLHQVGTPAHIKVRNKLHPAQVVRMPFVETHYYK
Protein: Voltage-dependent L-type calcium channel subunit beta-1 (Calcium channel voltage-dependent subunit beta 1) (Q2Q551)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004278}.
Interaction partners:
- Si:dkey-266j7.2.
- SH3 and cysteine-rich domain-containing protein 3
- Voltage-dependent L-type calcium channel subunit alpha
- Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit, a.
- Voltage-dependent L-type calcium channel subunit alpha
- Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit, b.
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel gamma-1 subunit
- Calcium channel, voltage-dependent, R type, alpha 1E subunit a.
- Voltage-dependent L-type calcium channel subunit alpha
Sequence:
MVQEGNMSRTPSTSTQEIQMDMFDHHGSHAQGKYAKRKSRFKRSDGSTSSDTTSNSFVRQGSADSYTSRPSDSDVSLEEDPEALRKEADRQALATLEKAKTKPVAFAVRTNVGYNPGPNDDVPVQGMAISFEPKDFLHIKEKYNNDWWIGRLVKEGCEVGFIPSPVKLESTRQLQEQRMRQNRLSSSKSGGSSSLDVATGARRPTPPGTGGPAKQKQKSMEHVPPYDVVPSMRPIILVGPSLKGYEVTDMMQKALFDFLKHKFEGRISITRVTADISLAKRSVLNNPSKHTIIERSSTRSSLAEVQSEIERIFELARTLQLVALDADTINHPSQLAKTSLAPIIVYIKIASPKVLQRLIKSRGKSQAKHLNVQMVAADKLAQCPPELFDIILDENQLEDACEHLAEYLEAYWKATHPPSSNPPNPLLNRTMATAALAASPEPVSNLQGPFLVHGEQKREMPERGGLQDYQSDLSGKQPLRSSRSQLQTGSRGLSRQDTFDSETQGSRDSAYTDDMETDPYEEPDPCRSYRLNPAHHAPRQASWEDEGAEPDQENLNMVPPPANQHQRGRGKLRERYCQDAEAGGATTGRNHNQEEWSRDVYIR
Protein: Gabarap protein (Q6NZZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
ALVPCISLRPPTQLSKNPDLVCKHYRRQVFLEILKISQTLTMKFMYKEEHPFEKRRSEGEKIRKKYPDRVPVIVEKAPKARIGDLDKKKYLVPSDLTVGQFYFLIRKRIHLRAEDALFFFVNNVIPPTSATMGLLYQEHHEEDFFLYIAYSDESVYGDVLKDV
Protein: Uncoupling protein 1 (Ucp4 protein) (Uncoupling protein 4) (Q7ZVP4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Cell death-inducing DFFA-like effector a
- Si:ch211-263k4.2.
- Peroxisome proliferator-activated receptor gamma
- Insulin
- Insulin
- Hormone-sensitive lipase
- Lipase, hormone-sensitive b.
Sequence:
MVGLKPSDVPPPLTVKVLSAGTAACIADLVTFPLDTAKVRLQIQGEKAVTGAAKGIRYKGVFGTISTMMRTEGPRSLYNGLVAGLQRQMAFASIRIGLYDNVKSFYTRGKDNPNVAVRILAGCTTGAMAVSMAQPTDVVKVRFQAQMNLQGVGRRYNGTMQAYRQIFQLEGLRGLWKGTLPNITRNALVNCTELVSYDLIKEAILKHRLLSDNLPCHFVSAFGAGFITTVIASPVDVVKTRYMNSPPGQYSSSTNCAWTMLTKEGPTAFYKGFVPSFLRLGSWNVVMFVSFEQLKRAMMVSRNRIEAAA
Protein: T. brucei spp.-specific protein (Q38F86)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTDYEELRQRLWRDIGKSARRRSRRRSRSCGPSSTVTSRQPQSTEMSLRSLCKGASPRRCASGRISSAYDPLSGSRGREVEYDSCLVHALLSLVEEMDEKSSCRSSSSPKRRASPLRSGARDRQATRTGILPSGINAPPRTRLGSTYGRGRRSRTREMTSRHRTHVDCEHGMDPRKLAEAFYVNNTSWKLAEAVYLHFVAETNKQQLPGICHEQRGRRG
Protein: Telomeric repeat-binding factor 2-interacting protein 1 (TERF2-interacting telomeric protein 1) (TRF2-interacting telomeric protein 1) (Repressor/activator protein 1 homolog) (RAP1 homolog) (cRAP1) (Q7T0L4)
Organism: Gallus gallus (Chicken)
Function: Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with terf2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with terf2 or other factors, and regulates gene expression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14659874}. Chromosome, telomere {ECO:0000269|PubMed:14659874}.
Interaction partners:
- Telomeric repeat-binding factor 2
- Protection of telomeres protein 1
- Telomeric repeat-binding factor
- SLX4 structure-specific endonuclease subunit.
- Zinc finger BED-type containing 4.
Sequence:
MAAPPRKVFVWEDGTPMRFYIRPGMAKLRLAPLLLAGGAGLCRVQEPGAVHLVQPGEPAPDGAVSTDYVVACVESQRRLPLDLYRHSGPAPLAASPRGRLPFTEAEDAALLRAVRERSGAPRVSGTALWKELECTGLTRHSWQAMRDRYLRHLRPLHRESQQTEEAAAPMGIFEAANREFESSESGSDTSDTPDELPLQNGEGTFPLEAASGLQTGLDDCALPAAQGENKQTNTFSDSSKAEEAAQIIQHFMEEFHTDLLTVTQALLKNSGEVEATSYYLHAGQRLDGYPVWSREDDLELQKDDEDVRSKLIAKFGAENVARRVAFRKS