wanglab/gogpt-training-data huggingface dataset:
Protein: DNA mismatch repair protein Mlh1 (MutL protein homolog 1) (P97679)
Organism: Rattus norvegicus (Rat)
Function: Heterodimerizes with Pms2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (Msh2-Msh6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of Pms2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (Mlh1-Pms2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with Mlh3 to form MutL gamma which plays a role in meiosis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P40692}. Chromosome {ECO:0000250|UniProtKB:P40692}. Note=Recruited to chromatin in a MCM9-dependent manner. {ECO:0000250|UniProtKB:P40692}.
Interaction partners:
- Mismatch repair endonuclease PMS2
- DNA mismatch repair protein Msh2
- DNA mismatch repair protein
- DNA 5'-3' helicase
- MutL homolog 3
- Fanconi-associated nuclease
- PMS1 homolog 1, mismatch repair system component
- DNA mismatch repair protein
- Breast cancer type 1 susceptibility protein homolog
- RecQ-like DNA helicase BLM
Sequence:
MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMTENCLDAKSTNIQVIVREGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQTFEDLAMISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLQAPPKPCAGNQGTLITVEDLFYNIITRKKALKNPSEEYGKILEVVGRYSIHNSGISFSVKKQGETVSDVRTLPNATTVDNIRSIFGNAVSRELIEVGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESAALKKAIEAVYAAYLPKNTHPFLYLILEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEAVKSTTGIASSSTSGSGDKVHAYQMVRTDSRDQKLDAFMQPVSRRLPSQPQDPVPGNRTEGSPEKAMQKDQEISELPAPMEAAADSASLERESVIGASEVVAPQRHPSSPGSSRKRHPEDSDVEMMENDSRKEMTAACYPRRRIINLTSVLSLQEEINDRGHETLREMLRNHTFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLPEPAPLFDFAMLALDSPESGWTEEDGPKEGLAEYIVEFLKKKAKMLADYFSVEIDEEGNLIGLPLLIDSYVPPLEGLPIFILRLATEVNWDEEECFESLSKECAVFYSIRKQYILEESALSGQQSDMPGSPSKPWKWTVEHIIYKAFRSHLLPPKHFTEDGNVLQLANLPDLCKVFERC
Protein: F-box protein At2g17690 (Protein SUPPRESSOR OF DRM1 DRM2 CMT3) (Q3EBY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in heat stress response. Contributes to recovery from heat stress.
Interaction partners:
- At2g34655
- Pumilio homolog 9
- Uncharacterized protein
- DNA-directed RNA polymerases II, IV and V subunit 12
- Helicase protein MOM1
- YTH domain-containing family protein
- DNA-directed RNA polymerase IV subunit 1
Sequence:
MGDWSKLPEELLGLIALRLYSVIELIRFRSICKSWRSSASGVNKNHSLSSPLIYFKPLQIILARAQANGQILSKYHGTVLSRATFFRVTLASSPDQGWLIKSDTDLKYRNFHLLNCLSRKALGRSRKLISLSEFIVSEIQESYAVVGRRTRETASEFKRVFLVRVQGGDHRVLVIGIDGKIRFWKGGIWNGIKKQVAQFSDFVLDEGLTYAVDTKGIMWWISSAYDIIRYGTKLHENITNGSCGEKRFVRCRGELYIVDRLIDENLLKRKADSYDDNAIVHFRNADYTNADLWEDGNGNDDFFAAQAHRFIHVLHDNLGNVSCKPFERDPPKTIGFKVYKNDEELLKWVEVKSLGDKAIVIATDACFSVSAHEFYGCLPNSIYFTDKKEEEVKVFKLDDGSITTMSESEQSCFQMFVPSFL
Protein: Carboxypeptidase E (CPE) (EC 3.4.17.10) (Carboxypeptidase H) (CPH) (Enkephalin convertase) (Prohormone-processing carboxypeptidase) (P15087)
Organism: Rattus norvegicus (Rat)
Function: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage.
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:14597614}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:14597614}; Peripheral membrane protein {ECO:0000269|PubMed:14597614}. Secreted {ECO:0000269|PubMed:14597614}. Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. {ECO:0000269|PubMed:14597614}.
Interaction partners:
- Neuroendocrine convertase 2
- Pro-opiomelanocortin
- Secretogranin-3
- Secretogranin-2
- Chromogranin-A
- Peptidylglycine alpha-amidating monooxygenase
- Receptor-type tyrosine-protein phosphatase N2
- Carboxypeptidase B
- Neuroendocrine convertase 1
- ProSAAS
Sequence:
MAGRGGRVLLALCAALVAGGWLLAAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQRGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNLKKIVDQNSKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGTAHEYSSCPDDAIFQSLARAYSSFNPVMSDPNRPPCRKNDDDSSFVDGTTNGGAWYSVPGGMQDFNYLSSNCFEITVELSCEKFPPEETLKSYWEDNKNSLINYLEQIHRGVKGFVRDLQGNPIANATISVDGIDHDVTSAKDGDYWRLLVPGNYKLTASAPGYLAITKKVAVPFSPAVGVDFELESFSERKEEEKEELMEWWKMMSETLNF
Protein: U1 snRNP-associated protein usp107 (Q8WZK0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Pre-mRNA-processing factor 39
- U1 snRNP-associated protein usp106
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing protein prp40
- Small nuclear ribonucleoprotein-associated protein B
- Splicing factor U2AF 59 kDa subunit
- Pre-mRNA-splicing factor prp12
- U4/U6.U5 tri-snRNP-associated protein snu66
Sequence:
MQRQNTQAAGMPMMPQVPMVGNGVPYVVPIQPVFAPLPPDYRSLYKKLYGQGAFLVDNPVEASSPYDFSQPILKFGKLPIKQVLRDNESQQKDRKNLPRNQKSNEIQEKQTFQTPSSEKSTTERESRPFVPPNSQQMRRMLFIGNIPKELDDFWMDKILRLSGKLASWRRVADADNSMTSFGFAEFESNEQFSRALEALNDFVVPPLYEGGPSTRLSLITDVENEGLYREWQTSRYARNKQKEINILQQIRFNLERICQDIGNFDVRSRIERAARQAREKNEKLLQNVKTSEIPINAADLEGINPELLPVIEEEIRSFRDQSAMKKREKQRSKDEYASLYKEYTRKEQEKLRKQNDDLQNLLSKHRISRIPMSTVNAFLRAEDSIPESFSDEQAYYEEKRRKDQLEAEEYYARERRWMNREKARTAALEREAAREEEERVNNTSFGTYLSEKLASFDDDEEARVSRDEYFVDRAAWIRHRAVARAREEDADALDRKEEERELRTRGEGATVETENYVENGKLVTSEMPQHENGPFKIKIQTKKPAVPSERREFGLPERLLLEEEDEEPQGYSPNPQKPKPAMEENDAEKTKRLRSLIEKIPVEAESLWALPIDWSKVTEDLLKEEMQAFVTKKIIEYIGIQEDSLITFTIDHIRQHKGAEQLVSELDLALAEDAPEFVSKVYRYLHVLLILRSEA
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q2Y080)
Organism: Aotus azarae (Azara's night monkey) (Simia azarae)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVNPTVFFDIAVDGEPLGRVSFELFADKLPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTPHNGTGGKSIYGVKFDDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNVVEAMERFGCRYGKTSKKITIADCGQL
Protein: Large ribosomal subunit protein uL16B (60S ribosomal protein L10-B) (Q9P769)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein eL28
- Elongation factor 3
- Large ribosomal subunit protein uL24
- mRNA export factor elf1
- Large ribosomal subunit protein eL30A
- Large ribosomal subunit protein uL2A
- Large ribosomal subunit protein uL5B
- Large ribosomal subunit protein uL3A
- Small ribosomal subunit protein eS12A
- Large ribosomal subunit protein uL30B
Sequence:
MARRPARCYRYCKNKPYPKSRYNRAVPDSKIRIFDLGRKRAGVDEFPLCIHLVSNEYEQITSEALEAARICANKYLVKIGGKDSFHLRVRAHPFHVVRINKMLSCAGADRLQTGMRHAFGKPNGLVARVNIGQVLMSVRTKDSSRATAIEALRRCQYKFPGQQRIIVSKKWGFSQYARDEYIEKRSRGEIIPDGCYAKFLNKRGSLQEKLDLFPEASFNLA
Protein: U-box domain-containing protein 20 (EC 2.3.2.27) (Plant U-box protein 20) (RING-type E3 ubiquitin transferase PUB20) (Q9C8D1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- Exocyst complex component EXO70B2
- Squamosa promoter-binding-like protein 11
- CF9 protein
- Serine/threonine-protein phosphatase BSL1
- Mediator of RNA polymerase II transcription subunit 19a
- At2g30880/F7F1.9
- Indole-3-acetic acid-amido synthetase GH3.2
Sequence:
MGLSLRVRRRGGSVSKKEIIPVTSCSEEVEITIPSQFQCPISYELMKDPVIIASGITYDRENIEKWFESGYQTCPVTNTVLTSLEQIPNHTIRRMIQGWCGSSLGGGIERIPTPRVPVTSHQVSEICERLSAATRRGDYAACMEMVTKMTRLGKESERNRKCVKENGAGLVLCVCFDAFSENANASLLLEETVSVLTWMLPIGLEGQSKLTTTSSFNRLVELLRNGDQNAAFLIKELLELNVTHVHALTKINGVQEAFMKSINRDSTCVNSLISIHHMILTNQETVSRFLELDLVNITVEMLVDSENSVCEKALTVLNVICETKEGREKVRRNKLVIPILVKKILKISEKKDLVSVMWKVCKSGDGSEVEEALRLGAFKKLVVMLQVGCGEGTKEKVTELLKMMNKVMKMNGFVDRSYSSSIEFKHVKKPF
Protein: Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (Q6FJH3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- 40S ribosomal protein S12
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS9
- Candida glabrata strain CBS138 chromosome K complete sequence
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL5
- L37
- Large ribosomal subunit protein eL38
- 60S ribosomal protein L6
- 40S ribosomal protein S30
Sequence:
MKLNIAYPVNGTQKTVEVDDEHRVRVFYDKRIGQEIEGEAVGDEFKGYTFKITGGNDKQGFPMKQGVLLPTRVKLLLAKGHSCYRPRRSGERKRKSVRGAIVGPDLAVLSLVIVKKGEQELEGVTDATVPKRLGPKRANHIRKFFGLTKEDDVRDFVIRREVTKGEKTYTKAPKIQRLVTPQRLQRKRYQRNLKVRNAQAQREAAAEYAQLLAKRLAERKAEKAETRKRRASSLKA
Protein: Protein KTI13 (Alpha-tubulin suppressor 1) (Kluyveromyces lactis toxin-insensitive protein 13) (P31386)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Together with KTI11; associates with the elongator complex and is required for tRNA Wobble base modifications mediated by the elongator complex. Association with the elongator complex is mediated via interaction with KTI11. The elongator complex is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s 2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). Together with KTI11; also required for diphthamide biosynthesis; diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. May participate in regulatory interactions between microtubules and the cell cycle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18466297}.
Interaction partners:
- Diphthamide biosynthesis protein 3
- Protein KTI12
- 2-
- 2-
- Elongator complex protein 3
- GTP-binding protein YPT1
- tRNA
- Adenylyltransferase and sulfurtransferase UBA4
- Diphthine methyltransferase
- Elongator complex protein 6
Sequence:
MSCVYAFGSNGQRQLGLGHDEDMDTPQRSVPGDDGAIVRKIACGGNHSVMLTNDGNLVGCGDNRRGELDSAQALRQVHDWRPVEVPAPVVDVACGWDTTVIVDADGRVWQRGGGCYEFTQQHVPLNSNDERIAVYGCFQNFVVVQGTRVYGWGSNTKCQLQEPKSRSLKEPVLVYDTGSVAVDYVAMGKDFMVIVDEGGRIVHASGRLPTGFELKQQQKRHNLVVLCMWTSIHLWNARLNTVESFGRGTHSQLFPQERLDFPIVGVATGSEHGILTTANQEGKSHCYNVYCWGWGEHGNCGPQKGSQPGLQLVGQYSGKPRVFGGCATTWIVL
Protein: TPR repeat-containing protein associated with Hsp90 (P25638)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein interacting with Hsp90 1
- RuvB-like protein 2
- RuvB-like protein 1
- ATP-dependent molecular chaperone HSP82
- Nucleolar protein 58
- Co-chaperone protein SBA1
- ATP-dependent molecular chaperone HSC82
- Kinesin-like protein KAR3
- Hsp90 co-chaperone AHA1
- Box C/D snoRNA protein 1
Sequence:
MSQFEKQKEQGNSLFKQGLYREAVHCYDQLITAQPQNPVGYSNKAMALIKLGEYTQAIQMCQQGLRYTSTAEHVAIRSKLQYRLELAQGAVGSVQIPVVEVDELPEGYDRS
Protein: Cysteine S-methyltransferase NleE (EC 2.1.1.-) (Effector protein NleE) (Non-LEE-encoded type III effector E) (B7UI22)
Organism: Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Function: Cysteine methyltransferase effector that inhibits host cell NF-kappa-B activation by preventing nuclear translocation of host protein RELA/p65. Acts by mediating cysteine methylation of host proteins TAB2 and TAB3: methylation of a conserved cysteine residue of the RanBP2-type zinc finger (NZF) of TAB2 and TAB3 disrupts zinc-binding, thereby inactivating the ubiquitin chain-binding activity of TAB2 and TAB3, leading to NF-kappa-B inactivation. Also mediates cysteine methylation of host protein ZRANB3, inactivating its ability to bind ubiquitin chains.
Subcellular location: Secreted {ECO:0000269|PubMed:17984206}. Host nucleus {ECO:0000269|PubMed:17984206}. Note=Secreted via the type III secretion system (T3SS) (PubMed:17984206). Localizes in the nucleus of the infected cells (PubMed:17984206). {ECO:0000269|PubMed:17984206}.
Interaction partners:
Sequence:
MINPVTNTQGVSPINTKYAEHVVKNIYPKIKHDYFNESPNIYDKKYISGITRGVAELKQEEFVNEKARRFSYMKTMYSVCPEAFEPISRNEASTPEGSWLTVISGKRPMGQFSVDSLYNPDLHALCELPDICCKIFPKENNDFLYIVVVYRNDSPLGEQRANRFIELYNIKRDIMQELNYELPELKAVKSEMIIAREMGEIFSYMPGEIDSYMKYINNKLSKIE
Protein: Odorant receptor 22a (P81909)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Involved in the behavioral responses ethyl butyrate and to esters in more general. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23196131}; Multi-pass membrane protein {ECO:0000269|PubMed:23196131}.
Interaction partners:
- Odorant receptor coreceptor
- Odorant receptor 85b
- Odorant receptor 47a
- Odorant receptor 56a
- Odorant receptor 67d
- Odorant receptor 47b
- Odorant receptor 35a
- Gustatory and odorant receptor 21a
- Odorant receptor 10a
- Ionotropic receptor 75a
Sequence:
MLSKFFPHIKEKPLSERVKSRDAFIYLDRVMWSFGWTEPENKRWILPYKLWLAFVNIVMLILLPISISIEYLHRFKTFSAGEFLSSLEIGVNMYGSSFKCAFTLIGFKKRQEAKVLLDQLDKRCLSDKERSTVHRYVAMGNFFDILYHIFYSTFVVMNFPYFLLERRHAWRMYFPYIDSDEQFYISSIAECFLMTEAIYMDLCTDVCPLISMLMARCHISLLKQRLRNLRSKPGRTEDEYLEELTECIRDHRLLLDYVDALRPVFSGTIFVQFLLIGTVLGLSMINLMFFSTFWTGVATCLFMFDVSMETFPFCYLCNMIIDDCQEMSNCLFQSDWTSADRRYKSTLVYFLHNLQQPITLTAGGVFPISMQTNLAMVKLAFSVVTVIKQFNLAERFQ
Protein: Cotranscriptional regulator ARB2A (ARB2 cotranscriptional regulator A) (Cotranscriptional regulator FAM172A) (Protein FAM172A) (Q8WUF8)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of alternative splicing, by interacting with AGO2 and CHD7. Seems to be required for stabilizing protein-protein interactions at the chromatin-spliceosome interface. May have hydrolase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q3TNH5}. Cytoplasm {ECO:0000250|UniProtKB:Q3TNH5}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q3TNH5}.
Interaction partners:
- PLAC8-like protein 1
Sequence:
MSISLSSLILLPIWINMAQIQQGGPDEKEKTTALKDLLSRIDLDELMKKDEPPLDFPDTLEGFEYAFNEKGQLRHIKTGEPFVFNYREDLHRWNQKRYEALGEIITKYVYELLEKDCNLKKVSIPVDATESEPKSFIFMSEDALTNPQKLMVLIHGSGVVRAGQWARRLIINEDLDSGTQIPFIKRAVAEGYGVIVLNPNENYIEVEKPKIHVQSSSDSSDEPAEKRERKDKVSKETKKRRDFYEKYRNPQREKEMMQLYIRENGSPEEHAIYVWDHFIAQAAAENVFFVAHSYGGLAFVELMIQREADVKNKVTAVALTDSVHNVWHQEAGKTIREWMRENCCNWVSSSEPLDTSVESMLPDCPRVSAGTDRHELTSWKSFPSIFKFFTEASEAKTSSLKPAVTRRSHRIKHEEL
Protein: Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (P15254)
Organism: Escherichia coli (strain K12)
Function: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:2659070}.
Interaction partners:
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylamine--glycine ligase
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Bifunctional purine biosynthesis protein PurH
- N5-carboxyaminoimidazole ribonucleotide mutase
- Amidophosphoribosyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Adenylosuccinate lyase
Sequence:
MMEILRGSPALSAFRINKLLARFQAARLPVHNIYAEYVHFADLNAPLNDDEHAQLERLLKYGPALASHAPQGKLLLVTPRPGTISPWSSKATDIAHNCGLQQVNRLERGVAYYIEAGTLTNEQWQQVTAELHDRMMETVFFALDDAEQLFAHHQPTPVTSVDLLGQGRQALIDANLRLGLALAEDEIDYLQDAFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWVIDGEQQPKSLFKMIKNTFETTPDHVLSAYKDNAAVMEGSEVGRYFADHETGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGSGGEIRDEGATGRGAKPKAGLVGFSVSNLRIPGFEQPWEEDFGKPERIVTALDIMTEGPLGGAAFNNEFGRPALNGYFRTYEEKVNSHNGEELRGYHKPIMLAGGIGNIRADHVQKGEINVGAKLVVLGGPAMNIGLGGGAASSMASGQSDADLDFASVQRDNPEMERRCQEVIDRCWQLGDANPILFIHDVGAGGLSNAMPELVSDGGRGGKFELREILSDEPGMSPLEIWCNESQERYVLAVAADQLPLFDELCKRERAPYAVIGEATEELHLSLHDRHFDNQPIDLPLDVLLGKTPKMTRDVQTLKAKGDALAREGITIADAVKRVLHLPTVAEKTFLVTIGDRSVTGMVARDQMVGPWQVPVANCAVTTASLDSYYGEAMAIGERAPVALLDFAASARLAVGEALTNIAATQIGDIKRIKLSANWMAAAGHPGEDAGLYEAVKAVGEELCPALGLTIPVGKDSMSMKTRWQEGNEEREMTSPLSLVISAFARVEDVRHTITPQLSTEDNALLLIDLGKGNNALGATALAQVYRQLGDKPADVRDVAQLKGFYDAIQALVAQRKLLAYHDRSDGGLLVTLAEMAFAGHCGIDADIATLGDDRLAALFNEELGAVIQVRAADREAVESVLAQHGLADCVHYVGQAVSGDRFVITANGQTVFSESRTTLRVWWAETTWQMQRLRDNPECADQEHQAKSNDADPGLNVKLSFDINEDVAAPYIATGARPKVAVLREQGVNSHVEMAAAFHRAGFDAIDVHMSDLLTGRTGLEDFHALVACGGFSYGDVLGAGEGWAKSILFNDRVRDEFATFFHRPQTLALGVCNGCQMMSNLRELIPGSELWPRFVRNTSDRFEARFSLVEVTQSPSLLLQGMVGSQMPIAVSHGEGRVEVRDAAHLAALESKGLVALRYVDNFGKVTETYPANPNGSPNGITAVTTESGRVTIMMPHPERVFRTVSNSWHPENWGEDGPWMRIFRNARKQLG
Protein: FI02861p (Tyrosine decarboxylase 1 (EC 4.1.1.-, EC 4.1.1.25)) (A1Z6N2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tryptophan 5-hydroxylase 2
- Tyramine beta-hydroxylase
Sequence:
MDVEEFRKYGKEVIDYICQYGTNIEERDVAPTLDPGYLKKLLPADAPQSPEPFKDVLEDFEQKIMPGVVHWNHPKFFAYFPSGNSFPSVLGDMLSSAIGSIGFSWASCPAAAELETIVMNWYAKALGLPKAFVSDAPGSTGGGALQGSASECVLVSLITARARAISELKGQTSVHDSVFLPSLIAYASREAHSSVEKATKMALVKLRIIDADEHGRMRVDLLRQAIQNDVNAGLTPFFVVATVGTTGGCAFDDITEIGKVCRQVSSIWLHVDGAYAGNSFILPEMRVFSAGLEYADSFNTNPNKLLLTNFDASALWVRDVMNLKSALNVNPLYLRHEHLTGVDYRHYGIPLSRRFRALKLWFVFRTYGIRGLQEYIRNHMALAKKFEMLVRKDERFEVRNDVHLGLVCFRMRTGDEPNHMLLAQINHSGKMHMTPAKFNGRYVIRFCVTYEHATEKDILEAWTQIKCFAEEILRDHQLESSSVPTTPEGSERTSSEPLAPVAGKPPIKKRLTRTKSLRFSFTRSISREQYQSQSEHLMDGCTPILVVDPKTLQENFQKAADDNDRNNSNGNVKLKDISDVDTDEASN
Protein: SRPBCC family protein (O53408)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- PNPLA domain-containing protein
- Conserved protein
- Long-chain-fatty-acid--CoA ligase FadD13
- PE-PGRS family protein PE_PGRS42
Sequence:
MAKSVVVEQSRAIPVQSEDAFGGTLAAALPVICSHWYGLIPPIKEVRDQTGAWDSVGQARVITMVGGGRVREELTSVDPPRSFGYTLTDIKGPLAPLVALVEGKWSFAPADTGTTVTWQWTIHPRSALAAPVLPVFARMWRGYARGVLEKLSALLVG
Protein: G1/S-specific cyclin-D2 (P30280)
Organism: Mus musculus (Mouse)
Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P30279}. Cytoplasm {ECO:0000250|UniProtKB:P30279}. Nucleus membrane {ECO:0000250|UniProtKB:P30279}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000250|UniProtKB:P30279}.
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase inhibitor 1C
- Retinoblastoma-like protein 2
- Cyclin-dependent kinase 4 inhibitor C
- Cyclin-dependent kinase 4 inhibitor B
- Retinoblastoma-associated protein
Sequence:
MELLCCEVDPVRRAVPDRNLLEDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKTHLQLLGAVCMFLASKLKETIPLTAEKLCIYTDNSVKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQKEKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDDEVNTLTCDALTELLAKITHTDVDCLKACQEQIEALLLNSLQQFRQEQHNAGSKSVEDPDQATTPTDVRDVDL
Protein: 8-demethyl-8-alpha-L-rhamnosyl tetracenomycin-C 2'-O-methyltransferase (EC 2.1.1.305) (O-methyltransferase I) (Q9AJU2)
Organism: Streptomyces olivaceus
Function: O-methyltransferase involved in the biosynthesis of the permethylated L-rhamnose moiety of elloramycin, an antitumor polyketide. Mediates the methylation of the hydroxy groups at the 2'-position after the sugar moiety has been attached to the aglycon.
Interaction partners:
Sequence:
MDSPQVARTLVDSAGGTAAHTREAIRQIGVPETAAFLADELAGRTETVTIRHAAEVQFVFDDRYAPDAADPVPWTFRVGPEGVTHRAGALPDPGAVVTQDLTELARSLYGPAADRSDATRTVWWRDHDDPRVYFDPPPVFPAVERLLAAADGRDVPGLAGLALRHGSDKWGIHTYTAAYEQHFAPFRDRAVTVVEIGVGGYDDPAAGGGSLRMWKRYFRRGLVYGVDIADKSRHREPRVHTVVADQSDPASLRDLADAIGPIDIVIDDGSHISAHVVTAFSTLFPRLNPGGLYVVEDLQTSYWPAFQGAYDDDTRTSVGFLKRLVDGLHHAEYPSRAGRPAQPTDRTVGSLHFHPNLAFVEKRANSGHGGISRLREAT
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (Protein raspberry) (Q07152)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein ATIC
- Inosine triphosphate pyrophosphatase
- AMP deaminase
- Adenylosuccinate lyase
- Raf homolog serine/threonine-protein kinase Raf
- CTP synthase
- 5'-nucleotidase
- Uncharacterized protein, isoform C
Sequence:
MESTTKVKVNGFVESTSSSAAPAIQTKSTTGFDAELQDGLSCKELFQNGEGLTYNDFLILPGYIDFTAEEVDLSSPLTKSLTLRAPLVSSPMDTVTESEMAIAMALCGGIGIIHHNCTPEYQALEVHKVKKYKHGFMRDPSVMSPTNTVGDVLEARRKNGFTGYPVTENGKLGGKLLGMVTSRDIDFRENQPEVLLADIMTTELVTAPNGINLPTANAILEKSKKGKLPIVNQAGELVAMIARTDLKKARSYPNASKDSNKQLLVGAAIGTRSEDKARLALLVANGVDVIILDSSQGNSVYQVEMIKYIKETYPELQVIGGNVVTRAQAKNLIDAGVDGLRVGMGSGSICITQEVMACGCPQATAVYQVSTYARQFGVPVIADGGIQSIGHIVKAIALGASAVMMGSLLAGTSEAPGEYFFSDGVRLKKYRGMGSLEAMERGDAKGAAMSRYYHNEMDKMKVAQGVSGSIVDKGSVLRYLPYLECGLQHSCQDIGANSINKLRDMIYNGQLRFMKRTHSAQLEGNVHGLFSYEKRLF
Protein: Rano class II histocompatibility antigen, D-1 beta chain (RT1 class II histocompatibility antigen, D-1 beta chain) (P18211)
Organism: Rattus norvegicus (Rat)
Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- H-2 class II histocompatibility antigen gamma chain
- Rano class II histocompatibility antigen, B alpha chain
- Rano class II histocompatibility antigen, B-1 beta chain
- Histocompatibility 2, class II antigen E alpha
- Major histocompatibility complex, class II, DM alpha
- T-cell surface glycoprotein CD4
- Hla-dmb protein
- T-cell receptor alpha chain V region PHDS58-like.
- RT1 class II, locus Ha
- RT1 class II, locus DOa
Sequence:
MVWLARDSCVAAVILLLTVLSPPVALVRDPTPRFLEQVKGECHFYNGTQRVRFLARYIYNREEYTRFDSDVGEFRAVTELGRPSAEYYNKQKEYMEQLRATVDTACKHDYEISESFLVPRTVEPKVTVYPSKTQPLEHHNLLVCSVSDFYPGSVEVRWFRNGEEEKDGLVSTGLIRNGDWTFQLLVMLETVPQGGEVYTCQVEHPSLPSPVRVEWKAQSTSAQNKKMSGVGGIVLGLLFLGAGLFVYFRNQKGQSGLQPTGLLN