wanglab/gogpt-training-data huggingface dataset:
Protein: Fumitremorgin C monooxygenase (EC 1.14.14.119) (Cytochrome P450 monooxygenase ftmP450-3) (Fumitremorgin biosynthesis protein G) (Q4WAX0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fumitremorgin C synthase
- 12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase
- Tryprostatin B 6-hydroxylase
Sequence:
METLDAIQLPYLGVVGASLIVILGIILLFPLGSDPFITINQHPRDLFQTKAKQQFEYNAAALLNEGLQTGHSAFRLVTNMVTYLILKDQYAEEIKNDSRFGAHEAVDPVLLVDLPGLESMFQGSLHNQVPPMAVRALNKELVHLTPSLSEEAMNCLQTRWTDSTEWHGVSIPETVLALIAQMTTRALLGPELCRNPEWLDIAKSFTTNRAIAVAAVQSWPSFLQPVIHWFLPPCRALRRQIQCARNIILPALERERRAYCSDQPTKREFSNLVFIDQYAKGARYDATMAQLRIIAVAFQTTSDLVEKVIARLCKHPELIEPLREEVVSVVGNHGLHRHSLRKLTLMESVMKETQRLEPAVIIGMFRLAKEKVTLKDGTVVPKGTNIAFANDLRFDPEMYLEPETFDGYRFQRMREDPAKIDLAPFTKTRMSHLAFGHGKHACPGRFLACDEAKLILCHILLNYDIRAVEGSPPELPGSWGNDVGEKTAGD
Protein: Synaptic vesicle glycoprotein 2A (Synaptic vesicle protein 2) (Synaptic vesicle protein 2A) (Q02563)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles.
Subcellular location: Presynapse {ECO:0000250|UniProtKB:Q9JIS5}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240, ECO:0000269|PubMed:16306227}; Multi-pass membrane protein {ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:1426240, ECO:0000269|PubMed:16306227}. Note=Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas. Colocalizes with ATP2B1 at photoreceptor synaptic terminals. {ECO:0000250|UniProtKB:Q9JIS5, ECO:0000269|PubMed:10625067, ECO:0000269|PubMed:16306227}.
Interaction partners:
- Synaptophysin
- Synaptotagmin-1
- Synaptic vesicle glycoprotein 2C
- Neuronal acetylcholine receptor subunit alpha-7
- Vesicle-associated membrane protein 2
- Synaptotagmin-2
- Laminin subunit alpha-5
- Pancreatic secretory granule membrane major glycoprotein GP2
- Synapsin-1
- Vesicular glutamate transporter 1
Sequence:
MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEEDDDDFPAPADGYYRGEGAQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKDREELAQQYETILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFSPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYAARTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLVNSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVLSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ
Protein: Phytochrome-associated protein phosphatase type 2C (F4I1B4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGKFCCFTSASEVVGGQSSSRSGKGRSDEGMIKYGFSLVKGKANHPMEDYHVANFINIQDHELGLFAIYDGHMGDSVPAYLQKRLFSNILKEVKTKKKGEFWVDPRRSIAKAYEKTDQAILSNSSDLGRGGSTAVTAILINGRKLWIANVGDSRAVLSHGGAITQMSTDHEPRTERSSIEDRGGFVSNLPGDVPRVNGQLAVSRAFGDKGLKTHLSSEPDIKEATVDSQTDVLLLASDGIWKVMTNEEAMEIARRVKDPQKAAKELTAEALRRESKDDISCVVVRFR
Protein: Ankyrin repeat domain 6 (E5RJ05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKGSVSAGDTPSSEQAVARKEEAREEFLSASPEPRAKDDRRRKSRPKVSAFSDPTPPADQQPGHQKNLHAHNHPKKRNRHRCSSPPPPHEFRAYQLYTLYRGKDGKVMQAPINGCRCEPLINKLENQLEATVEEIKAELGSVQDKMNTKLGQMENKTQHQMRVLDKLMVERLSAERTECLNRLQQHSDTEKH
Protein: Calcium/calmodulin-dependent protein kinase kinase 2 (CaM-KK 2) (CaM-kinase kinase 2) (CaMKK 2) (EC 2.7.11.17) (Calcium/calmodulin-dependent protein kinase kinase beta) (CaM-KK beta) (CaM-kinase kinase beta) (CaMKK beta) (Q96RR4)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.
Subcellular location: Nucleus {ECO:0000269|PubMed:21957496}. Cytoplasm {ECO:0000269|PubMed:21957496}. Cell projection, neuron projection {ECO:0000269|PubMed:21957496}. Note=Predominantly nuclear in unstimulated cells, relocalizes into cytoplasm and neurites after forskolin induction. {ECO:0000269|PubMed:21957496}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- 5'-AMP-activated protein kinase subunit beta-2
- 5'-AMP-activated protein kinase subunit gamma-1
- 5'-AMP-activated protein kinase subunit gamma-2
- 5'-AMP-activated protein kinase subunit beta-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
Sequence:
MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE
Protein: Uncharacterized protein Rv1993c (P9WLP5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable cation-transporting ATPase G
- HTH-type transcriptional regulator CmtR
- Uncharacterized protein Rv1995
Sequence:
MVTHELLVKAAGAVLTGLVGVSAYETLRKALGTAPIRRASVTVMEWGLRGTRRAEAAAESARLTVADVVAEARGRIGEEAPLPAGARVDE
Protein: EEF1AKMT4-ECE2 readthrough transcript protein (EC 3.4.24.71) [Includes: Methyltransferase-like region (EC 2.1.1.-); Endothelin-converting enzyme 2 region (EC 3.4.24.71)] (P0DPE2)
Organism: Bos taurus (Bovine)
Function: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (Probable).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12054617}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12054617}.
Interaction partners:
Sequence:
MACLGPSAQVPELPEKNCGYREVQYWDQRYQGAADSAPYEWFGDFSCFRDLLEPELRPLDRILVLGCGNSALSYEIFLGGFPDVTSVDYSSVVVAAMRARYAHVPTLRWETMDVRALGFPSGSFDVVLEKGTLDALLTGEQDPWTVSSEGVHTVDQVLNEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW
Protein: Collagen alpha-1(III) chain (P08121)
Organism: Mus musculus (Mouse)
Function: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-2
- Lumican
- Integrin alpha-2
- Fibrillin-1
- Collagen alpha-1
- Procollagen C-endopeptidase enhancer 1
- Periostin
- Integrin beta-1
Sequence:
MMSFVQSGTWFLLTLLHPTLILAQQSNVDELGCSHLGQSYESRDVWKPEPCQICVCDSGSVLCDDIICDEEPLDCPNPEIPFGECCAICPQPSTPAPVLPDGHGPQGPKGDPGPPGIPGRNGDPGLPGQPGLPGPPGSPGICESCPTGGQNYSPQFDSYDVKSGVGGMGGYPGPAGPPGPPGPPGSSGHPGSPGSPGYQGPPGEPGQAGPAGPPGPPGALGPAGPAGKDGESGRPGRPGERGLPGPPGIKGPAGMPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGDNGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGSPGQRGEPGPQGHAGAQGPPGPPGNNGSPGGKGEMGPAGIPGAPGLIGARGPPGPAGTNGIPGTRGPSGEPGKNGAKGEPGARGERGEAGSPGIPGPKGEDGKDGSPGEPGANGLPGAAGERGPSGFRGPAGPNGIPGEKGPPGERGGPGPAGPRGVAGEPGRDGTPGGPGIRGMPGSPGGPGNDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGLPGPAGKNGETGPQGPPGPTGPAGDKGDSGPPGPQGLQGIPGTGGPPGENGKPGEPGPKGEVGAPGAPGGKGDSGAPGERGPPGTAGIPGARGGAGPPGPEGGKGPAGPPGPPGASGSPGLQGMPGERGGPGSPGPKGEKGEPGGAGADGVPGKDGPRGPAGPIGPPGPAGQPGDKGEGGSPGLPGIAGPRGGPGERGEHGPPGPAGFPGAPGQNGEPGAKGERGAPGEKGEGGPPGPAGPTGSSGPAGPPGPQGVKGERGSPGGPGTAGFPGGRGLPGPPGNNGNPGPPGPSGAPGKDGPPGPAGNSGSPGNPGIAGPKGDAGQPGEKGPPGAQGPPGSPGPLGIAGLTGARGLAGPPGMPGPRGSPGPQGIKGESGKPGASGHNGERGPPGPQGLPGQPGTAGEPGRDGNPGSDGQPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPSGKSGDRGETGPAGPSGAPGPAGARGAPGPQGPRGDKGETGERGSNGIKGHRGFPGNPGPPGSPGAAGHQGAIGSPGPAGPRGPVGPHGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGGAAAIAGVGGEKSGGFSPYYGDDPMDFKINTEEIMSSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKMDAIKVFCNMETGETCINASPMTVPRKHWWTDSGAEKKHVWFGESMNGGFQFSYGPPDLPEDVVDVQLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKSLKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYQTRKAMRLPIIDIAPYDIGGPDQEFGVDIGPVCFL
Protein: Soluble guanylate cyclase gcy-33 (G5EGJ1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MQDENNRPPTWSASHSQDIRKPRKTESKITLNSRLSSSDLAVSRVETSKDSDGETPRPTSSELKEVNRIREEALAQEKEEERTTKEENQKIEEVGEDHVSEATSLLDSEVSHGDNNISFSQMPSDSIPHEDRTSLPSATPSEIGDAISKKKLEKEDSNSSMSSLDERTTVSAKPTTTRRLLNQKDLEKEKKRSSMAGSSVTSSSAHSHSIRSKKDTRDKSRCKCEDIRADNKLKTKVCSIM
Protein: 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI13 (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 13) (Thiamine pyrimidine synthase) (Q07748)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Thiamine thiazole synthase
- Putative pyridoxal kinase BUD16
- Pyridoxamine 5'-phosphate oxidase
- Probable pyridoxal 5'-phosphate synthase subunit SNZ3
- Thiamine biosynthetic bifunctional enzyme
- Putative pyridoxal kinase BUD17
- Uncharacterized protein YGR017W
- Probable pyridoxal 5'-phosphate synthase subunit SNO2
Sequence:
MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA
Protein: BARP protein (Q38CU9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRADDILNNCSAGRKPPPAVYVTALCRVAEQLRGLGGTISSSLLTVTSASSKAFKAKVQAEKAVKLAESRGLNVTKAKEAAVRATLAAEAAATAVSYCITHSTKVGSIAEMLWEVDEELHVFSLCGNKDRDVQDTALKCTDTAEGVTAQSLSEALEGLAKLVFDDNVARKLRQEDTVFQREFMWLQQHMEEAVRAQKQAEDAAADANETAGPNTGPVVNSVASPEGSVLLLMAGLFLGSVL
Protein: Aspartic-type endopeptidase ctsD (EC 3.4.23.-) (Q4WNV0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Secreted aspartic-type endopeptidase which is secreted and contributes to virulence.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MHLLQCLLSTISLASTVTAFVPYSFNLEVSTEGPPSNDVARRFVPWKLLLDDSYNNHGSSSNGVSLTLDLKKFPVRRDNKYKVVLADEPTTPNTAALNQEGLDYSYFATVRVGSQGQQMWLVLDTGGPNTWVFGSDCTTVACQRHETFGEAASKSLKLLPLNWAVGYGTGLVSGVLGTDSLSLAGLDVNMTFGLAKNASTDFESYPVDGILGLGRSANSNFNTPSFMETVATQRLLKSNIIGFSFSRNSDGARDGAANFGDLDTTRFTGDIVYTNTTGDSNNWRIPLDDASVNGTPCRFVNKTAVIDTGTSYAMLPPKDATVLHNLIPGAVTTSHGQNFTLPCNSTAVVQVSFSGLSYNISPKDYVGPAYGSACLSTIVGQALYGDDVWLLGDVFLKNVYSVFDYDNHRIGFANRSVPIASPTTTVAAAANPSATDGAGSTLTGSMAVHTGSASIVSRFVHWPFIFALLCMVLV
Protein: Fibroblast growth factor receptor 2 (Q63240)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
AYIFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDRPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPTNCTNELNTWTSPSLSNSILLVTPTQGALVLQGTILCFLQTPCLMTPACLSIHT
Protein: ADP-ribose glycohydrolase AF_1521 ([Protein ADP-ribosylaspartate] hydrolase AF_1521) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase AF_1521) (EC 3.2.2.-) (O28751)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.
Interaction partners:
- Thioredoxin
- Glyceraldehyde-3-phosphate dehydrogenase
- Elongation factor 2
Sequence:
MEVLFEAKVGDITLKLAQGDITQYPAKAIVNAANKRLEHGGGVAYAIAKACAGDAGLYTEISKKAMREQFGRDYIDHGEVVVTPAMNLEERGIKYVFHTVGPICSGMWSEELKEKLYKAFLGPLEKAEEMGVESIAFPAVSAGIYGCDLEKVVETFLEAVKNFKGSAVKEVALVIYDRKSAEVALKVFERSL
Protein: Troponin I, slow skeletal muscle (Troponin I, slow-twitch isoform) (Q9WUZ5)
Organism: Mus musculus (Mouse)
Function: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.
Interaction partners:
- Troponin T, slow skeletal muscle
- Troponin T, cardiac muscle
- Troponin T, fast skeletal muscle
- Troponin C, skeletal muscle
- Troponin C, slow skeletal and cardiac muscles
- Myosin light chain 3
- Myosin light chain 1/3, skeletal muscle isoform
- Tropomyosin alpha-3 chain
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin-7
Sequence:
MPEVERKSKITASRKLMLKSLMLAKAKECWEQEHEEREAEKVRYLSERIPTLQTRGLSLSALQDLCRELHAKVEVVDEERYDIEAKCLHNTREIKDLKLKVLDLRGKFKRPPLRRVRVSADAMLRALLGSKHKVSMDLRANLKSVKKEDTEKERPVEVGDWRKNVEAMSGMEGRKKMFDAAKSPTSQ
Protein: At3g56360 (Q9LY04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein
- Probable plastid-lipid-associated protein 14, chloroplastic
- Calcium load-activated calcium channel
- Protein yippee-like At5g53940
- Arginine/serine-rich-like splicing factor
- thiohydroximate-O-sulfate sulfate/sulfur-lyase
- Ferric reduction oxidase 3, mitochondrial
- At3g45160
- AT1G11360 protein
- Transcription factor bHLH47
Sequence:
MATSARICCGGGSACAVRCDRRTLNLNSRSSCVVPVTNRRNMCAIGKISMSMEDLSPPSAAVKIERIGGRKRGGSVVSREKLDVWLRDSVVEIVKNLRESPLLMHLYAEANGGLTTTATNPKAEDWTEMEGKWGRGEERTPEGVILVEKLADGDIADDDDHDGGACGEDTSAWGIVAQGRGSDTGPVCYLLKTTRVRSGMGTVCTHFCLVKVKSFRETAMSQLNNSWLVQTGQ
Protein: Dihydrofolate synthetase (DHFS) (EC 6.3.2.12) (Q12676)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Glutamate-adding enzyme which catalyzes the binding of the first glutamyl side chain to dihydropteroate. Leads to the de nove synthesis of tetrahydrofolate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Folic acid synthesis protein FOL1
- Dihydrofolate reductase
- Probable folylpolyglutamate synthase
- GTP cyclohydrolase 1
- Folylpolyglutamate synthase
- Thymidylate synthase
- Aminodeoxychorismate lyase
- Aminodeoxychorismate synthase
- Methylenetetrahydrofolate reductase 2
- Methylenetetrahydrofolate reductase 1
Sequence:
MAIELGLSRITKLLEHLGNPQNSLRVLHIAGTNGKGSVCTYLSSVLQQKSYQIGKFTTPHLVHVTDSITINNKPIPLERYQNIRLQLEALNKSHSLKCTEFELLTCTAFKYFYDVQCQWCVIEVGLGGRLDATNVIPGANKACCGITKISLDHESFLGNTLSEISKEKAGIITEGVPFTVIDGTNEASVINVVKERCKALGSELSVTDSQLNGNMIDTNSWGCFDLAKLPLNGEYQIFNLRVAMGMLDYLQMNELIDITKNEVSTRLAKVDWPGRLYRMDYRFDKVSNRTVPILMDGAHNGSAAVELVKYLRKEYGNQPLTFVMAVTHGKNLEPLLQPLLRPIDQVILTRFNNVEGMPWIHATDPEEIKDFILTQGYTKEIVIENDLHQVLPSLAHVSDEQRRPIVVCGSLYLCGELLRIHNSHLRN
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q49II7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EHEVKLQRLREELSRPVIEGHHHQSHHQKQAQHRQLHQSHHRKKHRRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVPEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEIKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFD
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (P97931)
Organism: Mus musculus (Mouse)
Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000305|PubMed:10871356}. Nucleus {ECO:0000269|PubMed:10871356}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:10871356}.
Interaction partners:
- DNA repair nuclease/redox regulator APEX1
- DNA ligase 1
- DDB1- and CUL4-associated factor 1
- Cytidine deaminase
- Single-stranded DNA cytosine deaminase
- Single-strand selective monofunctional uracil DNA glycosylase
- DNA damage-binding protein 1
- Flap endonuclease 1
- G/T mismatch-specific thymine DNA glycosylase
- N-glycosylase/DNA lyase
Sequence:
MIGQKTLYSFFSPTPTGKRTTRSPEPVPGSGVAAEIGGDAVASPAKKARVEQNEQGSPLSAEQLVRIQRNKAAALLRLAARNVPAGFGESWKQQLCGEFGKPYFVKLMGFVAEERNHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLSGLVFLLWGSYAQKKGSVIDRKRHHVLQTAHPSPLSVHRGFLGCRHFSKANELLQKSGKKPINWKEL
Protein: Sodium/hydrogen exchanger (A4GWV1)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MRTMGGFSQMKLAVNFLTIGLVILSLPCGSYTEIPPKPPGSLTVLPPVKPAGGPQAFPDAENSNLPAFTMDYARIQVPFEVTLWVLLASFAKIGFHVYHKITFWVPESCLLISIGLIVGAIMHSVHEEPPAVLSYNVFFLFMLPPHRTGVWILYAPRDRSSRTWEPVLWFAVVGTLWNSIGIGMSLYAVCQIEAFEVQDINLQENMLFAAIISAVDPVAVLSVFEDVSVNEQLYIVVFGECLFNDAVTVVLYNMFIFVADMPVVEPVDVFLGVARFFVVGLGGMGFGVIFGFVASFTTRFTSNVREIEPLFIFMYSYLAYLVAELFSISSIMAIVTCALTMKYYVEENVSQRSCTTIRHVVKMLGTISETLIFFFLGVVTITTEHEWNWGYIMFTLLLALVWRGLGVLVLTQIINPFRTIPFNFKDQFILGYGGLRGAISFALVFTLPDSIGRKKLFVTTTICMIMFTVFIQGISIRPLIEFINVRRTNRNLETINVEIHSRLIEHTIAGVEDLCGQWSHYYWKDKFLKFNNRILRKIPIRDNRAESSIVALYKKLELQNAMGILDTVSGDINAGSSIVPLHEEKKSSGKPKRKFVAADLMNMHDILSKNMYKIRQRTTAYTTKHSLPNDSRTKEILIRRHTSIRRSLGPGSFNGPNEAKSQKYFSLPPGKSLDSKFPPQRLRHTGNDDDETMSEMDYPSARSRFNQPSRSSSRAMLPLRRLNTLTEVPSSSVVDLVDERSGGRGAWGRGMSRLNSSSSDSRIPAPRRHHDPSNGPDNGSSGDHGSGDNGPEGEQQPLSPTPAWAAEPGDRDDSGTQKPLLRPQWKTRKP
Protein: Uncharacterized transcriptional regulatory protein C417.09c (O94490)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus membrane {ECO:0000255|PROSITE-ProRule:PRU00227}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ubiquitin-like-conjugating enzyme ATG10
- FAS1 domain-containing protein fsc1
Sequence:
MHARMQPHEDRSRSGMSRSEAMELEDQLEEEERGGNVVVGSSSANANASTAETGKKSAGGSKPKRRRGERIPPSKRIRKAIAYVNKYASGCFGRVERRLVCTRSISRHSNQKLLDFCVECKKHKIKCVGNFPCGRCLKKGLECVIETPPRLLMNKDEISLNLQRLSHMETILSKLMPSMSLDLPSLEAKIAELSESLQTYPDKVLTDIELGSYQQVTLNETQTYYEDAGSNESFVARVHEIICQGREFQVQHKLTNKGNKTFEDILDPADNTVASLIHALPPKDITFYLLMTFWQFSSDNNHFYYNTKLFAAKVHHLFDDPTSFQSKDGGFVCMLLLSMAMGSLFSYIRHPEFLSDENHDRWTYPGSQFYQNAKLLFPKVISESSLETVQSFFLAGMYLSPTLAHEVVYMYFGIAMRAAVANGMHKKSANAQFSGDVAELRKRLFWSVYCMERKIGISLGRPESLVRSEIDIHFPEYRESLDSQNFIASFRTFTLAIKISLLTNKVYDMWYSSLHGKANLKAATIKEIVNEIEAWRQQLSPDLEIQNIGPDSRSYRGIVHLHLAYHIVRIAMGRPFLLHRLRERTMNSKTDEGARLLTDKLISYCYSSALHIVDLLVLLRMHKFLSVYSFMDYHSCHAASFIILVHLLINPSEQTIEQLNTAIDILNFVTDRFPLLKGSTDVITNLRAFAEQSEVYQSRLNATEPAYSTQVPFFPRDADYHNQINLQNLWNDENINASLEALFNDAKGFGFLLPADNFIFPSDDGDM
Protein: NEDD8-conjugating enzyme ubc12 (EC 2.3.2.34) (RUB1-conjugating enzyme) (Ubiquitin carrier protein 12) (O74549)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein 1
- RING-box protein pip1
- NEDD8-activating enzyme E1 regulatory subunit
- Defective in cullin neddylation protein 1
- Cullin-1
- Cullin-3
- NEDD8-specific protease 2
- NEDD8-specific protease 1
- Ubiquitin-activating enzyme E1-like
Sequence:
MRKIWELKKKEAQKEKNASGISPAQIRIQKDVTDLEIPSTMSTSWPDPIKLNVLHLEIRPDEGYYKGGKFKFRIQIDDNYPHDPPKVKCLNKIYHPNIDIEGNVCLNILRQDWNPVLNLNSILVGLQFLFLSPNAEDPLNKEAAADLHKDPQGFASRVRTAMKGGLVNGISFDNVMA