wanglab/gogpt-training-data huggingface dataset:
Protein: Protein flightless-1 homolog (Q13045)
Organism: Homo sapiens (Human)
Function: May play a role as coactivator in transcriptional activation by hormone-activated nuclear receptors (NR) and acts in cooperation with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved in early embryonic development (By similarity). May play a role in regulation of cytoskeletal rearrangements involved in cytokinesis and cell migration, by inhibiting Rac1-dependent paxillin phosphorylation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9JJ28}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9JJ28}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9JJ28}. Cell projection, podosome {ECO:0000250|UniProtKB:Q9JJ28}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9JJ28}. Note=Colocalizes to actin-rich structures in blastocysts and, together with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to centrosomes (By similarity). Localized to the core of macrophage podosomes (By similarity). {ECO:0000250|UniProtKB:Q9JJ28}.
Interaction partners:
- Leucine-rich repeat flightless-interacting protein 1
- Leucine-rich repeat flightless-interacting protein 2
- RNA-binding protein EWS
- Lethal
- Myeloid differentiation primary response protein MyD88
- Actin-like protein 6A
- ATP-dependent RNA helicase A
- Intron Large complex component GCFC2
- Estrogen receptor
- Myosin-9
Sequence:
MEATGVLPFVRGVDLSGNDFKGGYFPENVKAMTSLRWLKLNRTGLCYLPEELAALQKLEHLSVSHNNLTTLHGELSSLPSLRAIVARANSLKNSGVPDDIFKLDDLSVLDLSHNQLTECPRELENAKNMLVLNLSHNSIDTIPNQLFINLTDLLYLDLSENRLESLPPQMRRLVHLQTLVLNGNPLLHAQLRQLPAMTALQTLHLRSTQRTQSNLPTSLEGLSNLADVDLSCNDLTRVPECLYTLPSLRRLNLSSNQITELSLCIDQWVHVETLNLSRNQLTSLPSAICKLSKLKKLYLNSNKLDFDGLPSGIGKLTNLEEFMAANNNLELVPESLCRCPKLRKLVLNKNHLVTLPEAIHFLTEIEVLDVRENPNLVMPPKPADRAAEWYNIDFSLQNQLRLAGASPATVAAAAAAGSGPKDPMARKMRLRRRKDSAQDDQAKQVLKGMSDVAQEKNKKQEESADARAPSGKVRRWDQGLEKPRLDYSEFFTEDVGQLPGLTIWQIENFVPVLVEEAFHGKFYEADCYIVLKTFLDDSGSLNWEIYYWIGGEATLDKKACSAIHAVNLRNYLGAECRTVREEMGDESEEFLQVFDNDISYIEGGTASGFYTVEDTHYVTRMYRVYGKKNIKLEPVPLKGTSLDPRFVFLLDRGLDIYVWRGAQATLSSTTKARLFAEKINKNERKGKAEITLLVQGQELPEFWEALGGEPSEIKKHVPEDFWPPQPKLYKVGLGLGYLELPQINYKLSVEHKQRPKVELMPRMRLLQSLLDTRCVYILDCWSDVFIWLGRKSPRLVRAAALKLGQELCGMLHRPRHATVSRSLEGTEAQVFKAKFKNWDDVLTVDYTRNAEAVLQSPGLSGKVKRDAEKKDQMKADLTALFLPRQPPMSLAEAEQLMEEWNEDLDGMEGFVLEGKKFARLPEEEFGHFYTQDCYVFLCRYWVPVEYEEEEKKEDKEEKAEGKEGEEATAEAEEKQPEEDFQCIVYFWQGREASNMGWLTFTFSLQKKFESLFPGKLEVVRMTQQQENPKFLSHFKRKFIIHRGKRKAVQGAQQPSLYQIRTNGSALCTRCIQINTDSSLLNSEFCFILKVPFESEDNQGIVYAWVGRASDPDEAKLAEDILNTMFDTSYSKQVINEGEEPENFFWVGIGAQKPYDDDAEYMKHTRLFRCSNEKGYFAVTEKCSDFCQDDLADDDIMLLDNGQEVYMWVGTQTSQVEIKLSLKACQVYIQHMRSKEHERPRRLRLVRKGNEQHAFTRCFHAWSAFCKALA
Protein: Mlc1 protein (A7MBY5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQREEASAQEVFSYAQMSTLEGNSGVGTLSRHLERERLERDGYTVDVRASDLQLDQPGPLHPCFSYRVWLYSVVVGSSLLIASAFSLYMGNVFPAAMDYLRCTAGSSIPAAVVSFAIAKNRQVAVSDFQLVYVSSFAVTTTCLVWFGCKLAISPSAININFNLLLLIVLEVLTASTVILSARSVDDCCSHSKPVSEGPMIVTQTSFPTRLFKAFAVIELIVGIAAVFGGIIALNLGALLPEPYLSVTFFWILAACFPSAIASHVVAENPSKSLVEMLIAISSVTSPLLFSASAFLSSSVISFIEIFLHEVALAKQSYDILLLVLMLLLLVPAVLALATIIQCASYKSQVRMGANEWDTLRKKHCEQLASNGTLRDFDKEKAWKAVVVQMAQ
Protein: Anthranilate phosphoribosyltransferase, chloroplastic (EC 2.4.2.18) (Q02166)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- anthranilate synthase
- Anthranilate synthase beta subunit 2, chloroplastic
- anthranilate synthase
- Anthranilate synthase beta subunit 1, chloroplastic
- N-
- Anthranilate synthase alpha subunit 1, chloroplastic
- N-
- N-
- anthranilate synthase
- Anthranilate synthase alpha subunit 2, chloroplastic
Sequence:
MVIAVATTSSIVSGIKLSGILTSFNAVDDASSSCGRSNLTGVRIFPTLSRRRFSSIGAVSPIRGDAQSSFSRSSFACSQNLGLSGGFSAAEALPPACANASPSSIKSFNQLIETLIDRVDLSETEAESSLEFLLNEANEALISAFLVLLRAKGETYEEIVGLARAMMKHARKVEGLVDAVDIVGTGGDGANTVNISTGSSILAAACGAKVAKQGNRSSSSACGSADVLEALGVVLDLGPEGIKRCVEEGGIGFMMSPMYHPAMKIVGPVRKKLKIKTVFNILGPMLNPARVSYAVVGVYHKDLVVKMAKALQRFGMKRALVVHSCGLDEMSPLGGGLVYDVTPEKIEEFSFDPLDFGIPRCTLEDLRGGGPDYNADVLRRVLSGESGAIADSLILNAAAALLVSNRVQTLAEGVTVAREVQSSGKAIKTLDSWINISNLAQKSQ
Protein: Coiled-coil domain-containing protein 85A (Q96PX6)
Organism: Homo sapiens (Human)
Function: May play a role in cell-cell adhesion and epithelium development through its interaction with proteins of the beta-catenin family.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:25009281}.
Interaction partners:
Sequence:
MSKAAGGAAAAAAAAESCSPAPAGSSAAPPAPVEDLSKVSDEELLQWSKEELIRSLRRAEAEKVSAMLDHSNLIREVNRRLQLHLGEIRGLKDINQKLQEDNQELRDLCCFLDDDRQKGKRVSREWQRLGRYTAGVMHKEVALYLQKLKDLEVKQEEVVKENMELKELCVLLDEEKGAGCAGSRCSIDSQASLCQLTASTAPYVRDVGDGSSTSSTGSTDSPDHHKHHASSGSPEHLQKPRSEGSPEHSKHRSASPEHPQKPRACGTPDRPKALKGPSPEHHKPLCKGSPEQQRHPHPGSSPETLPKHVLSGSPEHFQKHRSGSSPEHARHSGGSPEHLQKHALGGSLEHLPRARGTSPEHLKQHYGGSPDHKHGGGSGGSGGSGGGSREGTLRRQAQEDGSPHHRNVYSGMNESTLSYVRQLEARVRQLEEENRMLPQASQNRRQPPTRNSSNMEKGWGSRARRVLQWWQGCRGIGRCLPTLPGSFRLSSGADGSNSSPNSAASFSGHATPSQQPEPVVHSLKVVWRKLGDAAGSCPGIRQHLSGNQYKGPM
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (EC 3.1.4.11) (Phospholipase C-1) (PLC-1) (P40977)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Interaction partners:
- Phosphatidylinositol 4-phosphate 5-kinase its3
- Inositol polyphosphate multikinase
- Phosphatidylinositol 4-kinase pik1
- Phosphatidylinositol 4-kinase stt4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase ptn1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase lsb6
- Phosphatidylinositol 3-kinase pik3
- Inositol-1,4,5-trisphosphate 5-phosphatase 2
- Inositol-1,4,5-trisphosphate 5-phosphatase 1
Sequence:
MNCEMVTSPESVNLGDSNRAVSPFCLPDCSENAVAQTRSKTLDNAALDLPYVGNRKKSEQDFFKMLSSRDRDAHSTLRKRSNSLSSFLSTKSTSASENKFHGGLNWLSLKLNLLLRLQGRMNSARTNTSMNPYSCDSNENLSTLSSVNQNFNSRQLLATIVPESIQNGCSLLRITKKKVRQRKVSLDPISGYLMLDKNTGKAYKKLCVDDIKEIRQGRDARNYREQYKISSENEKRWFTIIYCADNKLKAMHMISPTLDAHNQWIMALEGLKTYRLNEFIIGLNLVCHQGEKMIDYSENLNPWEKLEKEQSAQLDLGDVHRMCQMLHLNASMEFLEETFQKADADHSGKLSFEEFQHFVSLLKTRSEIVDIFKEYTSGSDKMSLEQFRHFLSTSQKARLDSDSIRTLYVSFCSNDDSKMGLIEFTSFLLSPHNSPVVPVIQDMSRPLNEYLISSSHNTYLLGKQFGGESSIEGYIRSLQRGCKCIEIDCWDGPNGPVVCHGHTFTSMIKFNDVIDAIRKYAFVVSPYPLFISLEIHCCPDQQRQMVSYMKQAFGDTLVMKPVTANESVLPSPEDLLNKILLKVKCSATPLHQFSTDILKVGITDSSTDTTESSELENSELTGLRKGKRRMKNIIVQELQQLAPYARSLKFRNFSLPESKTYSHIFSFSERTIKKHGKAMVPRLSKHNLRYLCRVYPGPLRVGSTNFNPQVYWRLGVQMVALNWQTYDTGLQINDALFIADPPTGYLLKPPCQRIIGTTVGEEGLPRKIKLTIDVISGQQLRRARELSNSETLSPYVEIQVHSMEESPFRWCSKVVHENGFRPFWGETMVYESIISDDFYSMIRFLVHHRGSNGNDSIFANFTCPIDRLQQGYRHIRLLDMQGENLLFSSLFLKIKKEDI
Protein: Transcription repressor OFP5 (Ovate family protein 5) (AtOFP5) (Q8VZN1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor that regulates multiple aspects of plant growth and development through the regulation of BEL1-LIKE (BLH) and KNOX TALE (KNAT) homeodomain transcription factors. Required for embryo development.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- BEL1-like homeodomain protein 1
- Homeobox protein knotted-1-like 3
- Transcription repressor OFP16
- Transcription repressor OFP15
- Transcription repressor OFP13
- Transcription repressor OFP18
- Transcription repressor OFP10
- Transcription repressor OFP12
- Transcription repressor OFP14
- Transcription repressor OFP11
Sequence:
MMRWGRKKPVSSSSSSGLSRALPVSWFSKLSGSSDLKPAKEKKQDEKASQNISVKTSLSSTTRRSDIHENSKRFQRVSVEKENSATRSADKESNEKFEEIMSSVRKKVRDFQKETCGFLEVEAMDRDNGTVILTPRIQVNRDKQRCERRDQRLLEQKPKRSEQDAGVKVKKPARRTGTGGYSREDSVILGHTITKPAHQWEKLKEVKLREVKLKADQQRKSLYLKRELNRIGTKENNKVRVFSPRASEKCRVKAIEDLKKAKQRAREHELLIETADGGMENESFAVVKCSSDPQKDFRDSMIEMIMENGINHPEELKELLVCYLRLNTDEYHDMIISVFQQVHNDFNFH
Protein: orotate phosphoribosyltransferase (EC 2.4.2.10) (Q8I3Y0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase
- NADH-cytochrome b5 reductase, putative
- ribose-phosphate diphosphokinase
- ribose-phosphate diphosphokinase
- Protein transport protein GOT1, putative
- carbamoyl-phosphate synthase
- CTP synthase
- aspartate carbamoyltransferase
- Adenylosuccinate lyase
Sequence:
MTTIKENEFLCDEEIYKSFVHLKDKICEERKKKELVNNNIDNVNFNDDDDNNYDDDGNSYSSYIKEMKKLLKVVLLKYKALKFGEFILKSKRKSNYFFSSGVLNNIVSSNIICFLLSELILKNKLSFDYLLGASYKGIPMVSLTSHFLFESKKYSNIFYLYDRKEKKEYGDKNVIVGNLDDDDKDILNLKKKTKNNQDEEKKNIIIIDDVFTCGTALTEILAKLKTYEHLKVVAFIVLLNRNEYEINENNQKIYFKDIFEKRVGIPLYSILSYKDDIQSMI
Protein: A-type flagellin (P21184)
Organism: Pseudomonas aeruginosa
Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
Sequence:
MALTVNTNIASLNTQRNLNNSSASLNTSLQRLSTGSRINSAKDDAAGLQIANRLTSQVNGLNVATKNANDGISLAQTAEGALQQSTNILQRMRDLSLQSANGSNSDSERTALNGEVKQLQKELDRISNTTTFGGRKLLDGSFGVASFQVGSAANEIISVGIDEMSAESLNGTYFKADGGGAVTAATASGTVDIAIGITGGSAVNVKVDMKGNETAEQAAAKIAAAVNDANVGIGAFSDGDTISYVSKAGKDGSGAITSAVSGVVIADTGSTGVGTAAGVTPSATAFAKTNDTVAKIDISTAKGAQSAVLVIDEAIKQIDAQRADLGAVQNRFDNTINNLKNIGENVSAARGRIEDTDFAAETANLTKNQVLQQAGTAILAQANQLPQSVLSLLR
Protein: Regulator of exponential growth motility (F7X8H2)
Organism: Sinorhizobium meliloti (strain SM11)
Interaction partners:
Sequence:
MIVVVDDRALVKDGYASLFGREGIPSTGFDPREFGEWVSSAADSDIDAVEAFLIGQGESTLTLPRAIRDRSRAPVIAMSDTPSLENTLALFDCGVDDVVRKPVHPREILARVAAIRRRLTAIANFTDIGPIRVFADGRDPEINGEVFALPRRERRILEYLVANRGRRVSKSQIFNAIYGIFDEDVEENVVESHISKLRKKLRKKLGFDPIDSKRFLGYCIDWN
Protein: Transcription factor (SPT8), putative (AFU_orthologue AFUA_5G09080) (Q5B460)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Transcriptional activator spt7
- Transcriptional co-activator
- Transcription initiation factor TFIID subunit 6
- Transcriptional adapter 2
- SAGA-like transcriptional regulatory complex subunit Spt3, putative
- Transcription initiation factor TFIID subunit 12
- Transcriptional regulator Ngg1, putative
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- histone acetyltransferase
Sequence:
MASIVEDEDDRDIAGSQDGSSDNDMDDTLRDADEGGGDNEPDMDADGDADDQDADSASNASHASESAEVATQQNQETTMTPVPDNATTDLTSVFHPSVRPECLTASSYDIVPTTAAPHSTSINAITATADMRWVFSGGSDGYVRKFNWVDSINSKLMLTVAQRHPFVDSVIKAGVLMTYWENMDGNALSPVYSLACQSEGLWLLSGLESGSIRLQSIRHDEGKEIALLQQHTSAVSVLSLTSDEKSLLSGSWDKRIYDWDLNTGQTRRVFGSSAGQISAIELRPESSLPVPRDTTEIQQPNGTFSSNNQASGGNSFSYMDTTNDQGDNDAVNPQAGSPADSLFGGADSLFGDADGTAGDGLGTATNSFGIDDDDEFGKALTNGVAPDADAAGEPDTVQQKNLFDSKDPSNDAPGVDSNTLVPNQPLDSHSTDAVNNQSQPLVNGLPHAEELEPPSQSQEHTQSTPTEASNDNDNTFLAASIDGTIRVWDRRQPSAIARITPRNSPPWCMNACWSPDGNYIYAGRRNGTVEEYSLHKGLREPERTFKFPQGSGPVTALKAMPNGRHLLCASHDILRLYDLKHEQATRHSTVPFLIIPGHRTGTVSQLYVDQACRFLVSTSGNRGWEGSTTEVLLGYEIGVPVVR
Protein: Uncharacterized protein 2 (P86735)
Organism: Haliotis asinina (Donkey's ear abalone) (Ass's ear abalone)
Subcellular location: Secreted {ECO:0000269|PubMed:21050442}.
Interaction partners:
Sequence:
PLGAATSNIPPQYARSTLQPTGLTSRAQSYPTNTNPGPSAKGNLVLPLNWQLLNSPASQIPTQSTTTFRSNPPLPPVVPGRRNTSPFFFPKPTRPLSFRQILDFLGRIRATKELDCKTVSEALSLNLPKFYYPLSCDDKCPPPSVCRHVGLVGFCCPPHVTDQLIWMVGLAERFKVLGG
Protein: Toll-like receptor (G3V695)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU363040}.
Interaction partners:
- Toll-like receptor 2
- Toll-like receptor 4
- Myeloid differentiation primary response protein MyD88
- Platelet glycoprotein 4
- Lysosome membrane protein 2
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-like receptor 1
- T-cell surface glycoprotein CD4
- Stress-70 protein, mitochondrial
- Scavenger receptor class B member 1
Sequence:
MVKSLWDSLCNMSQDREPIVESFHFVCTLALIVGSMTQFSDEFESVVDYSNKNLTHVPKDLSPSTKSLSLSQNSISDLQMSDISFLSELRVLRLSHNRIRRLDFGVFLLNRDLEYLDVSHNQLQNISCCPMVNLKHLDLSFNDFEVLPVYKEFGNLMKLSFLGLSAAKFRQLDLLPISHLHLSCVLLDLVNYQIKDGETESLQVPNTNVLHLVFHPNSLFSVQVNISVNALGCLQLSNIKLNDKNCQSLIIFLSELTRGPTLLNLTLQHIETNWKCFVRLLQFLWPRPVEYLNIYNLTITESISRETFIYVETVLKSLKIEHVTNQVFLFVKDALYSVFAEMNIRMLTLSDTPFIHMVCPEFPSTFAFLNFTQNVFTDSIFQGCSTLKRLETLILQRNGLKNLFKVALMTKTMSSLETLDVSLNSLNSHVYDRTCAWAESIRVLNLSSNVLSDSVFRCLPPKVKVLDLHNNRIVSIPKDVTHLQALQELNVASNFLTDLPGCGAFSSLSVLVIDHNSVSHPSSDFFQSCQNIRSITAGNNPFRCTCELREFVKNIGQASREVVEGWPDSYRCDYPDSIKGTPLQDFHMSPLSCDTILLTVTIGATLLLLAAIGASLCLYFDLPWYLRMLWQWTQTRHRARNIPLEELQRNLQFHAFVSYSEHDSAWVKNELLPNLEKDDIRVCLHERNFVPGKSIVENIIHFIEKSYKSIFVLSPHFIQSEWCHYELYFAHHNLFHEGSDNLILILLEPIQQNNIPSRYHKLRALMAQRTYLEWPIEKGKNFENIKAATRTSPWEAEEDISLSLRLVWSTQ
Protein: Herf (H6UNZ8)
Organism: Streptomyces chromofuscus
Interaction partners:
Sequence:
MITGDRKDSEMSRSTEETPWTTEEVGHRYDRLSRVPELLAFGESLHFGYWEDPEDEGGLSDAMGRLTDLVIGGLDAGPGSRVLDLGCGVGGPAVKLASATGAEVVGITVSREQITKATGLARAEGLTGQVVFQYADAMDLPFEEGEFDAVFGLESIMHMDRPAVLAQIAKVLRPGGRLVLTDEVLRAPIPADRAEDDETVAGYLRANMIRSLATPEAYPELLTGAGLDPEAITDITDRTVRPTFRTLWRQANDRLDTILNDLGSPPAAVAEELRGWQRLAEIPEFGYLLISAHRPGR
Protein: RNA-binding protein 47 (RNA-binding motif protein 47) (Q91WT8)
Organism: Mus musculus (Mouse)
Function: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing. Functions as an enzyme-substrate adapter for the cytidine deaminase APOBEC1. With APOBEC1 forms an mRNA editing complex involved into cytidine to uridine editing of a variety of mRNA molecules. Through the binding of their 3'UTR, also stabilizes a variety of mRNAs and regulates the expression of genes such as the interferon alpha/beta receptor and interleukin-10. Also involved in the alternative splicing of several genes including TJP1. Binds the pre-mRNA (U)GCAUG consensus sequences in downstream intronic regions of alternative exons, regulating their exclusion and inclusion into mRNAs (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:A0AV96}. Cytoplasm {ECO:0000250|UniProtKB:A0AV96}.
Interaction partners:
- C->U-editing enzyme APOBEC-1
Sequence:
MTAEDSATAMNSDPTVGSSTKVPEGVAGAPNEAALLALIERTGYTMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFETVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKRGEILEEIAKVTEGVLNVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMQTVKILYVRNLMIETTEETIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVDKEQYSRYQKAAKGGGGSAEAVAQQPSYVYSCDPYTLAYYGYPYNALIGPNRDYFVKTGSIRGRGRGAAGNRTPGPRGSYLGGYSAGRGIYSRYHEGKGKQQEKGYELVPNLEISPVNPVAIKPGTVAIPAIGAQYSMFQAAPAPKIIEDGKIHTMEHMISPIAVQPDPATAAAAAAAAAAAAVIPAVSTPPPFQGRPITPVYTVAPNVQRIPTAGIYGASYVPFAAPATATIATLQKNAAAAVYGGYAGYIPQAFPAALQVPIHDVYQTY
Protein: Malonyl-[acyl-carrier protein] O-methyltransferase (Malonyl-ACP O-methyltransferase) (EC 2.1.1.197) (Biotin synthesis protein BioC) (P12999)
Organism: Escherichia coli (strain K12)
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes.
Interaction partners:
- 8-amino-7-oxononanoate synthase
- ATP-dependent dethiobiotin synthetase BioD 1
- Biotin synthase
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Heme exporter protein B
- Bifunctional ligase/repressor BirA
- ATP-dependent dethiobiotin synthetase BioD 2
Sequence:
MATVNKQAIAAAFGRAAAHYEQHADLQRQSADALLAMLPQRKYTHVLDAGCGPGWMSRHWRERHAQVTALDLSPPMLVQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPKGVVAFTTLVQGSLPELHQAWQAVDERPHANRFLPPDEIEQSLNGVHYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHLFLGVIARE
Protein: Ribonucleoside-diphosphate reductase large subunit (R1) (EC 1.17.4.1) (Ribonucleotide reductase large subunit) (U5TQE9)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Interaction partners:
Sequence:
MASRPAASSPVEARAPVGGQEAGGPSAATQGEAAGAPLAHGHHVYCQRVNGVMVLSDKTPGSASYRISDSNFVQCGSNCTMIIDGDVVRGRPQDPGAAASPAPFVAVTNIGAGSDGGTAVAAFGGTPRRSAGTSTGTQTADVPAEALGGPPPPPRFTLGGGCCSCRDTRRRSAVFGGEGDPVGPAEFVSDDRSSDSDSDDSDDTDSETLSHASSDVSGGATYDDALDSDSSSDDSLQIDGPVCRPWSNDTAPLDVCPGTPGPGADAGGPSAVDPHAPTPEAGAGLAADPAVARDDAEGLSDPRPRLGTGTAYPVPLELTPENAEAMARFLGDAVNREPALMLEYFCRCAREETKRVPPRTFCSPHRLTEDDFGLLNYALVEMQRLCLDVPPVPPNAYMPYYLREYVTRLVNGFKPLVSRSARLYRILGVLVHLRIRTREASFEEWLRSKEVALDFGLTERLREHEAQLVILAQALDHYDCLIHSTPHTLVERGLQSALKYEEFYLKRFGGHYMESVFQMYTRIAGFLACRATRGMRHIALGREGSWWEMFKFFFHRLYDHQIVPSTPAMLNLGTRNYYTSSCYLVNPQATTNKATLRAITSNVSAILARNGGIGLCVQAFNDSGPGTASVMPALKVLDSLVAAHNKESARPTGACVYLEPWHTDVRAVLRMKGVLAGEEAQRCDNIFSALWMPDLFFKRLIRHLDGEKNVTWTLFDRDTSMSLADFHGEEFEKLYQHLEVMGFGEQIPIQELAYGIVRSAATTGSPFVMFKDAVNRHYIYDTQGAAIAGSNLCTEIVHPASKRSSGVCNLGSVNLARCVSRQTFDFGRLRDAVQACVLMVNIMIDSTLQPTPQCTRGNDNLRSMGIGMQGLHTACLKLGLDLESAEFQDLNKHIAEVMLLSAMKTSNALCVRGARPFNHFKRSMYRAGRFHWERFPDARPRYEGEWEMLRQSMMKHGLRNSQFIALMPTAASAQISDVSEGFAPLFTNLFSKVTRDGETLRPNTLLLKELERTFSGKRLLEVMDSLDAKQWSVAQALPCLEPTHPLRRFKTAFDYDQKLLIDLCADRAPYVDHSQSMTLYVTEKADGTLPASTLVRLLVHAYKRGLKTGMYYCKVRKATNSGVFGGDDNIVCTSCAL
Protein: Proteasome subunit beta type-5-B (EC 3.4.25.1) (20S proteasome beta subunit E-2) (Proteasome epsilon-2 chain) (Q9LIP2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-6
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-4-A
- Proteasome subunit beta type-7-B
- Proteasome subunit beta type-7-A
- Proteasome subunit beta type-2-A
- Proteasome subunit alpha type-2-A
- Proteasome subunit beta type-2-B
Sequence:
MKLDTSGLETTMPVIGFGSNSEMLDGFSSAPSFDLPRTTDFDGFQKKAVEMVKPAKGTTTLAFIFKEGVMVAADSRASMGGYISSQSVKKIIEINPYMLGTMAGGAADCQFWHRNLGIKCRLHELANKRRISVSGASKLLANMLYSYRGMGLSVGTMIAGWDETGPGLYYVDNEGGRLKGDRFSVGSGSPYAYGVLDSGYKFDMSVEEASELARRSIYHATFRDGASGGVASVYHVGPQGWTKLSGDDVGELHYHYYPVAPITAEHVMEEAAE
Protein: Uncharacterized protein (Q585D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDVLAILDGAAARVAALLMSEGINALLAFLRGEAWEESPSTVLNRADGDGDTKSDSLQIPNTLLGCYGFLPLAIAAEVSLAPSTSHQERVALVQDFERRGFRVFTVNLMPDCRGLEDSSRGASAYNASASVLRLNCIEAARNWCDAVYAEDGKEGEGDTGVDCSNIYLSGAKRRRDDDEKSGLAERVAHTDFHNPRRRAQVQLHGRGCGLCVKYALFIVRCCANAGNAQRAAVGGGNCSSATERSRRTKDPLTLLLYDISSLSALCRVRQSTRRTRIRFSVLLLPDDLAYGGALLEESLRGPMSCHYCVKLFQGSADRMLHRRQDVDSGGGEENECVPFLERLKLWLSAPMESRGVEADGSCDGNSVNHGKNEQENAAKLQGSKPSLFFVRYENLPFCCFLREALRRFPVILPPLLLRQLQSLWAFRHQLSDVVVGLHSLLSPFALSSSMHATMSEANDVTTSPANVVQGTSRGYHENMTQLSNSIELLNILFAAACEWADGHLLNEAVAFAVLYEDLVFGRLTRLKRIPGLTAYVERLSPKSVGPTDLSKALTSCVPVFVPNALTGSGAYIRDELSQEQQYVMRRPLSLPPIMAVPGAKVSLATELLRSTLLAVLPPHDSLEEVQKAVRAFPCAGGKCDEGTPSEALRHGDTYCGVTYNNFFSPLIPDSVRVLHLLTSHAMASSNVKQQFVPLSLIQRICQLSDESLIRSLVELQLTGMATVNMREFKARSSLLALS
Protein: Acyl carrier protein (Q39798)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASIAGSSISMQPCPFAKGSVSGLKLGSFMNQGRSTLSFTMRPMPARLQICCAAKQETVDKVCEVVKRQLPLHNDKPITGESTFLDLGADSLDTVEIVLGLEEEFGITVEEDNAQSITTVQDAAELLEKLCSEKSA
Protein: Centrin-3 (O35648)
Organism: Mus musculus (Mouse)
Function: Plays a fundamental role in microtubule-organizing center structure and function.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O15182}. Nucleus, nucleolus {ECO:0000250|UniProtKB:O15182}. Nucleus envelope {ECO:0000250|UniProtKB:O15182}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:O15182}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O15182}. Note=Centrosome of interphase and mitotic cells. Localizes to centriole distal lumen (By similarity). Localization at the nuclear pore complex requires NUP153 and TPR (By similarity). {ECO:0000250|UniProtKB:O15182}.
Interaction partners:
- Germinal-center associated nuclear protein
- Transcription and mRNA export factor ENY2
- PCI domain-containing protein 2
- Nuclear pore complex protein Nup153
- Centrosomal protein POC5
- Nucleoprotein TPR
- Centrin-2
- Protein SFI1 homolog
- Mitotic spindle assembly checkpoint protein MAD2A
- 26S proteasome complex subunit SEM1
Sequence:
MSLALRGELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDQAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEINQEEFIAIMTGDI
Protein: Protochlorophyllide reductase B, chloroplastic (PCR B) (EC 1.3.1.33) (NADPH-protochlorophyllide oxidoreductase B) (POR B) (P21218)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
Subcellular location: Plastid, chloroplast outer membrane. Plastid, chloroplast thylakoid membrane.
Interaction partners:
- Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase, chloroplastic
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Chlorophyllase-1
- Chlorophyllase-2
- Geranylgeranyl diphosphate reductase, chloroplastic
- Protochlorophyllide reductase A, chloroplastic
- Protochlorophyllide reductase C, chloroplastic
- Glutamyl-tRNA reductase 1, chloroplastic
Sequence:
MALQAASLVSSAFSVRKDAKLNASSSSFKDSSLFGASITDQIKSEHGSSSLRFKREQSLRNLAIRAQTAATSSPTVTKSVDGKKTLRKGNVVVTGASSGLGLATAKALAETGKWNVIMACRDFLKAERAAKSVGMPKDSYTVMHLDLASLDSVRQFVDNFRRTETPLDVLVCNAAVYFPTAKEPTYSAEGFELSVATNHLGHFLLARLLLDDLKKSDYPSKRLIIVGSITGNTNTLAGNVPPKANLGDLRGLAGGLNGLNSSAMIDGGDFDGAKAYKDSKVCNMLTMQEFHRRFHEETGVTFASLYPGCIASTGLFREHIPLFRALFPPFQKYITKGYVSETESGKRLAQVVSDPSLTKSGVYWSWNNASASFENQLSEEASDVEKARKVWEISEKLVGLA
Protein: Protein phosphatase 1E (EC 3.1.3.16) (Ca(2+)/calmodulin-dependent protein kinase phosphatase N) (CaMKP-N) (CaMKP-nucleus) (CaMKN) (Partner of PIX 1) (Partner of PIX-alpha) (Partner of PIXA) (Q8WY54)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that inactivates multifunctional CaM kinases such as CAMK4 and CAMK2 (By similarity). Dephosphorylates and inactivates PAK. May play a role in the inhibition of actin fiber stress breakdown and in morphological changes driven by TNK2/CDC42. Dephosphorylates PRKAA2 (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15496589, ECO:0000269|PubMed:16269004}. Cytoplasm {ECO:0000269|PubMed:15496589, ECO:0000269|PubMed:16269004}. Note=A truncated form, major form, with the C-terminal part missing, is mostly found in the cytoplasm and a little in the nucleus. The full-length, minor form, is found in the nucleus. {ECO:0000269|PubMed:15496589, ECO:0000269|PubMed:16269004}.
Interaction partners:
- Calcium/calmodulin-dependent protein kinase type IV
- Calmodulin-1
Sequence:
MAGCIPEEKTYRRFLELFLGEFRGPCGGGEPEPEPEPEPEPEPESEPEPEPELVEAEAAEASVEEPGEEAATVAATEEGDQEQDPEPEEEAAVEGEEEEEGAATAAAAPGHSAVPPPPPQLPPLPPLPRPLSERITREEVEGESLDLCLQQLYKYNCPSFLAAALARATSDEVLQSDLSAHYIPKETDGTEGTVEIETVKLARSVFSKLHEICCSWVKDFPLRRRPQLYYETSIHAIKNMRRKMEDKHVCIPDFNMLFNLEDQEEQAYFAVFDGHGGVDAAIYASIHLHVNLVRQEMFPHDPAEALCRAFRVTDERFVQKAARESLRCGTTGVVTFIRGNMLHVAWVGDSQVMLVRKGQAVELMKPHKPDREDEKQRIEALGGCVVWFGAWRVNGSLSVSRAIGDAEHKPYICGDADSASTVLDGTEDYLILACDGFYDTVNPDEAVKVVSDHLKENNGDSSMVAHKLVASARDAGSSDNITVIVVFLRDMNKAVNVSEESDWTENSFQGGQEDGGDDKENHGECKRPWPQHQCSAPADLGYDGRVDSFTDRTSLSPGSQINVLEDPGYLDLTQIEASKPHSAQFLLPVEMFGPGAPKKANLINELMMEKKSVQSSLPEWSGAGEFPTAFNLGSTGEQIYRMQSLSPVCSGLENEQFKSPGNRVSRLSHLRHHYSKKWHRFRFNPKFYSFLSAQEPSHKIGTSLSSLTGSGKRNRIRSSLPWRQNSWKGYSENMRKLRKTHDIPCPDLPWSYKIE