wanglab/gogpt-training-data huggingface dataset:
Protein: RNase P protein subunit (Q54W23)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- RNase P protein subunit
- Ribonuclease P protein subunit p29
- Probable ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit drpp30
- RNase P protein subunit
- RNase P protein subunit
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS5
- Casein kinase I
- Small ribosomal subunit protein eS7
Sequence:
MSIINNEVPNNKILLKRITVDPNDKEQIENFNKNFITNHVFNQKVEIILPIKKGANEEVEEDNNNESDKKSQQKPKAKGSLLSQASSSYLLVEGEFTSLFQEQSITPLPSSSNNKSLDGINTKQLYYQIETTLDLLLSHEFIDKYIKNGGFYAISQLNFIDSGNVVAFLPNSKIILNVDKETYQELGLLGKSSVFKNLQRYIITLDMTSKEYQRGSKSYTRLIWSLKDRLSSINLICFYQKLNSTQLQSIDFPQGVKVLPSYNQPTQEILNLRLPTLNIINENLNINNSNNDIKMIYNDFINEWVEVLGFASLGINLNQVKDFEIGNSLLSQCPIATKCLKATQKGLVSNSFILELIEKIKLMLSKGLIEYGVLNIYGFADTPISWNSIEHNFLYGGENDQSLLILPNNKFISSNLIGTYDYYC
Protein: WAS/WASL-interacting protein family member 3 (Corticosteroids and regional expression protein 16) (Q9Z0G8)
Organism: Rattus norvegicus (Rat)
Function: May have a role in spermatogenesis (By similarity). May be a regulator of cytoskeletal organization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11553796}. Note=In hippocampal neurons colocalizes with WASL in the cell body, axons and the growth cone.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Actin nucleation-promoting factor WASL
- Actin-related protein 3
- Actin-related protein 2
Sequence:
MPVPPPPPPPLPPPPPPLGAPPPPPPPGPPISTDAPSLRKSDLKGRSALLADIQQGTRLRKVTQINDRSAPQIESSKGTSKEGGAAGSNARGGSTPPALGDLFAGGFPVLRPAGQRDVAGGKTGQGPGSRAPSPRLPTKAISGPLPAPASPRLGNASDTHSSARPVPPRPSVPAPPPPTTPPPPPPPPPPPPPPPLPPASPIKAPSVSPPVPPTKGNPSAVPAPIPCVPPLPPPPPTPPPLPPASALSEKAVRPQLAPLHLPPIPPPLPLLPPYGYPALHSEPSSPAQDVREPPAPPPPPPPPPPPPPPPLPTYASCSPRAAVAPPPPPLPGSSNSGSETPPPLPPKSPSFQTQKALPTPPGAPGPQIILQKKRRGPGAGGGKLNPPPAPPARSPTTELSSKTQQPGGQLRNGGQHVIDDFESKFTFHSMEDFPPPDEYKPGQKIYPSKVPRSRTPGSWLQAEAAGQSSDDIKTRNSQLSLKALR
Protein: Dynein light chain roadblock (Q7JQ02)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|PIRNR:PIRNR009998}.
Interaction partners:
- Dynein light chain roadblock
- IP01982p
- Dynein light chain 2, cytoplasmic
- Dynein light chain Tctex-type
- Dynein light chain 1, cytoplasmic
- Dynein light chain
- Cytoplasmic dynein 2 light intermediate chain 1
Sequence:
MNRILEKVIHQNGTIVDRILSEHTIGYVVSDNTANAVAETSFDNTSAQAILKHLHGLLVSTCQSVVRDIDPSNKLCFMRLGTRKFEYLVAPEEYFTITVVQ
Protein: Protein odd-skipped-related 1 (zOsr1) (Q5XJQ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional repressor (By similarity). Regulates mesoderm versus endoderm differentiation during gastrulation to regulate kidney versus vascular cell fate. Acts upstream of pax2a in kidney development and functions in glomerular maturation, after podocyte specification.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P86413}.
Interaction partners:
Sequence:
MGSKTLPAPVPLHPSLQLANYSFLQTSNGLHLPADHMPSIYSFSALHAVHLHQWTLGYPPFTLPRCTFSKLPGLVDARFPLPSIPLFPHLVQPAKQESSGPGSGASSKSKPRFDFANLAAAATQDDALKAEDLSTNNGHVRSPSLGCLLDVAKLSSPERKPSRGRLPSKTKKEFVCKFCGRHFTKSYNLLIHERTHTDERPYTCDICHKAFRRQDHLRDHRYIHSKEKPFKCQECGKGFCQSRTLAVHKTLHMQVKELKPAKIK
Protein: Protein PHLOEM PROTEIN 2-LIKE A5 (AtPP2-A5) (EC 3.2.2.6) (Q9C5Q9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cysteine/Histidine-rich C1 domain family protein
- F-box protein PP2-A11
- Putative glucuronosyltransferase PGSIP8
- 2-oxoglutarate
- Heat shock protein 70
- Defensin-like protein 205
Sequence:
MSGASSVSSICSSNVSLIPTGPQVFINFRGKDLRKGFMSFLKPALKKEKINVFIDEQEERGKYLISLFDTIGESKIALVIFSEGYCESHWCMDELVKIKEYMDQNRLIIIPIFYRLDLDVVKDLTGKFGDNFWDLVDKYQPEPKKLHKWTEALFSVCELFSLILPKHSDISDRDFVKSIVKAVKKVQKNFFQRRNGEIEYQDFSVPACKLTITMHESPNEEAVQVTVLNEFYQMKNQSPVPSYEFKFWVDLTRPKGNVFMIDARDLSIAWSEDSNHWTWLPLPNQNSNESVMEIAFLKSASWLDVAGKFDTRYLTPRTRYEVVFVVKLEYTFEWETLVKLKLDLPNTWEKPQEQSVDMFDYISDQWLDIPVGEFTTSKKNVGEISFAMYEHECQLWKSGLFVKGVTIRPKY
Protein: Aromatic-amino-acid:2-oxoglutarate transaminase (A0A1D8PMC5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Phenylpyruvate decarboxylase
- prephenate dehydratase
- Prephenate dehydrogenase [NADP
- aromatic-amino-acid transaminase
- Transaminase A
- Aspartate aminotransferase
- Aspartate aminotransferase
- 4-hydroxyphenylpyruvate dioxygenase
- histidinol-phosphate transaminase
- Aro80p
Sequence:
MSDPTHLISKRAAGRTSVHFTNAPSDKPPANFKPHEKPLALSYGMPNHGFFPIDSIDVNLVDYPFQKITTPSTTSSTAEEEPPSSSLNGSENGHQTKTPPSSIHTPQSTVHISRHTTDPKLIDLARGLQYAAVEGHAPLLQFARDFIIRTHKPNYDDWNVFITTGASDGLNKAADVFLDDGDVILVEEFTFSPFLRFSDNAGAKAVPVKINFDNDSDGIDLTQFVDLLENWEKHYPNLPKPKALYTIATGQNPTGFTQSLEFRKKIYDLAVKYDFAIIEDDPYGYLTLPKYEKPNIGGSGSGNNELKNDLEIDDYLKNHLTPSYLELDTTGRVLRVETFSKLFAPGLRLGFIVGHKEVIDAVKNYSDVVNRGASGLTQTIVNNVIQENFKGVDGWLEWILKMRLNYSYRKDLLLYSIFESQAYKKGYVDVIDPKAGMFVTFKINLPKDVDVLQKMKLLLWKLISYGILVVPGYNMTVDLEFSKDRSNFFRLCYALANNDEEILESGKRLTDAVYEFFSNGLEF
Protein: Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) (P9WFU3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL16
- Polyribonucleotide nucleotidyltransferase
- HTH-type transcriptional regulator Cmr
- DNA-directed RNA polymerase subunit beta
- Threonine--tRNA ligase
- Adenylate cyclase
- Small ribosomal subunit protein uS7
- Elongation factor Tu
Sequence:
MLSPEALTTAVDAAQQAIALADTLDVLARVKTEHLGDRSPLALARQALAVLPKEQRAEAGKRVNAARNAAQRSYDERLATLRAERDAAVLVAEGIDVTLPSTRVPAGARHPIIMLAEHVADTFIAMGWELAEGPEVETEQFNFDALNFPADHPARGEQDTFYIAPEDSRQLLRTHTSPVQIRTLLARELPVYIISIGRTFRTDELDATHTPIFHQVEGLAVDRGLSMAHLRGTLDAFARAEFGPSARTRIRPHFFPFTEPSAEVDVWFANKIGGAAWVEWGGCGMVHPNVLRATGIDPDLYSGFAFGMGLERTLQFRNGIPDMRDMVEGDVRFSLPFGVGA
Protein: Protein-tyrosine sulfotransferase (EC 2.8.2.20) (Q7ZT02)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MRKQTCNVLLVCGVISSITVFYLGLSTIECPNARSRASQHGWVVNLHAGRNLSDPLQLPEEYNEETPLIFVGGVPRSGTTLMRAMLDAHPIVRCGEETRVIPRLLAMQATWSHSARERVRLDEAGVTDDVLDSAVRAFLLEIIVGHGEPAPRLCNKDPFALKSMSYLSKLFPKAKFILMLRDGRATVHSMISRKVTITGFDLTSYRDCLVKWNRAVEVMYDQCLAAVDGNCLPVHYEQLVLHPERVMRRLLQFLDLPWDTAVLHHEQLIGKVGGVSLSKVELSTDQVVKPVNTEALSKWVGKIPADVVKDMPSLAPMLSRLGYDPLANPPNYNKPDLLYLNNTKIVRPI
Protein: ATP citrate lyase (K7ESG8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPDQLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEP
Protein: Patched family protein (F4I9G5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Transcription factor bHLH35
- Transcription factor bHLH27
- At5g17540
- Cytochrome P450 76C3
- Cytochrome P450 76C1
- Cytochrome P450 76C4
- Cytochrome P450 76C2
- Phosphomethylpyrimidine synthase, chloroplastic
- Cytochrome P450, family 76, subfamily C, polypeptide 5
- Cytochrome P450 monooxygenase-like protein
Sequence:
MQILFVGYGVEAKQSAGYCAMYDICGARSDGKVLNCPFNIPSVKPDDLLSSKIQSLCPTITGNVCCTETQFDTLRSQVQQAIPFIVGCPACLRNFLNLFCELTCSPDQSLFINVTSTTKVKNNSTVDGIQYYITDDFGAGMYESCKNVKFGSSNSRALDFLGAGAKNFKEWFTFIGQKAGVNLPGSPYGIAFLPTPPVSSGMRPMNVSIYSCGDESLGCSCGDCPSAATCSSKAEVPTQKKHSCSIKIGSLEVKCVDFILAILYIVLVSLFLGGGLLHPVRGKKKTSQMGTLSEASGERNSVNQQKPDTIQSQMLQNTPQRNWGQLSTVQGHLANFYGKYGIWVARHPTLVLCLSVSVVLLLCVGLIRFKVETRPDKLWVGSGSRAAEEKQFFDTHLAPFYRIEQLIIATVQTSSHEKAPEILTDDNIKLLFDIQKKVDGLRANHSGSMVSLTDICMKPLGEDCATQSVLQYFKMKPENYDDYGGVDHVKYCFEHFTSTESCLSAFKGPLDPTTALGGFSGNSFSEASAFLVTYPVDNFVDNKGNKTEKAVAWEKAFIQLAKDELLPMVQAKNLTLSFSSESSIEEELKRESTADVITIAISYLVMFAYISLTLGDSPRLKSFYITSKVLLGLSGVLLVMLSVLGSVGFFSAVGMKSTLIIMEVIPFLVLAVGVDNMCILVHAVKRQEQELPLERRISNALMEVGPSITLASLAEILAFAVGAFIKMPAVRVFSMFAALAVLLDFLLQITAFVALIVFDFRRTEDKRVDCFPCIKTSKSSISAEKGVGQRKAGLLTRYMKEVHAPVLSHWIVKIVVIAFFFGLAMAGIALSTRIEPGLEQQIVLPQDSYLQGYFNNISTYLRIGPPLYFVLKNYNYSSESRHTNQLCSINKCNPNSLLNEIARASLTPELSYIAKPAASWLDDFLVWLSPEAFGCCRKFTNGTFCPPDDQPPCCPPGQTSCGLSEVCKDCTTCFRHADLSSDRPSTTQFKEKLPWFLNALPSADCAKGGHGAYSSSVDLQGYANGIIQASSFRTYHTPLNKQVDFVNSMRAAQEFSAKVSRSLKMEIYPYSVFYMFFEQYLDIWKTALINLSIAIAAVFVVCLIITCSFWSSAIILLVIAMIIIDLLGVMAVFHIQLNALSVVNLIMSVGIAVEFCVHITHAFSISTGDRNHRMKEALGGMGASVFSGITLTKLVGVIVLGFSRSEVFVVYYFKMYLALVLLGFLHGLVFLPVFLSMFGPAPRHVEGERQDHRPSVSSVP
Protein: Homeobox protein six1a (Homeobox protein six1b) (Sine oculis homeobox homolog 1a) (Sine oculis homeobox homolog 1b) (Q6DHF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development. Depending on context, functions as transcriptional repressor or activator. Plays an important role in the development of the inner ear, where it promotes hair cell proliferation and inhibits proliferation of neural progenitor cells (By similarity). Required for normal myogenesis. Plays a role in the development of fast muscle fibers throughout the body, as well as the development of craniofacial muscles.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15475}. Cytoplasm {ECO:0000250|UniProtKB:Q15475}.
Interaction partners:
- Eyes absent homolog
- Cbp/p300-interacting transactivator, with Glu/Asp-rich carboxy-terminal domain, 1.
- Forkhead box D1
- Forkhead box D2
- Protein Wnt
- Paired box protein Pax-2a
- LIM/homeobox protein Lhx1
Sequence:
MSILPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESYQFSTHNHPKMQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRSVLREWYTHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENGENNGVGGKQSQRSPLDGVKSLMSSSEDEFSPPQSPEHSSVLLLQGTMNNPAAPAYPMPGLGAPHPLHGMQGHPHQIQDSLLGSLTSSLVDLGS
Protein: Long chain acyl-CoA synthetase 8 (EC 6.2.1.3) (Q9SJD4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitate, palmitoleate, oleate and linoleate.
Interaction partners:
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 1, chloroplastic
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Acyl-coenzyme A oxidase 2, peroxisomal
- Acyl-coenzyme A oxidase 4, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Acyl-coenzyme A oxidase 3, peroxisomal
- Diacylglycerol O-acyltransferase 2
Sequence:
MEDSGVNPMDSPSKGSDFGVYGIIGGGIVALLVPVLLSVVLNGTKKGKKRGVPIKVGGEEGYTMRHARAPELVDVPWEGAATMPALFEQSCKKYSKDRLLGTREFIDKEFITASDGRKFEKLHLGEYKWQSYGEVFERVCNFASGLVNVGHNVDDRVAIFSDTRAEWFIAFQGCFRQSITVVTIYASLGEEALIYSLNETRVSTLICDSKQLKKLSAIQSSLKTVKNIIYIEEDGVDVASSDVNSMGDITVSSISEVEKLGQKNAVQPILPSKNGVAVIMFTSGSTGLPKGVMITHGNLVATAAGVMKVVPKLDKNDTYIAYLPLAHVFELEAEIVVFTSGSAIGYGSAMTLTDTSNKVKKGTKGDVSALKPTIMTAVPAILDRVREGVLKKVEEKGGMAKTLFDFAYKRRLAAVDGSWFGAWGLEKMLWDALVFKKIRAVLGGHIRFMLVGGAPLSPDSQRFINICMGSPIGQGYGLTETCAGATFSEWDDPAVGRVGPPLPCGYVKLVSWEEGGYRISDKPMPRGEIVVGGNSVTAGYFNNQEKTDEVYKVDEKGTRWFYTGDIGRFHPDGCLEVIDRKKDIVKLQHGEYVSLGKVEAALGSSNYVDNIMVHADPINSYCVALVVPSRGALEKWAEEAGVKHSEFAELCEKGEAVKEVQQSLTKAGKAAKLEKFELPAKIKLLSEPWTPESGLVTAALKIKREQIKSKFKDELSKLYA
Protein: N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (N-acetylglucosaminyltransferase) (EC 2.4.1.150) (I-branching enzyme) (IGNT) (Large I antigen-forming beta-1,6-N-acetylglucosaminyltransferase) (P97402)
Organism: Mus musculus (Mouse)
Function: Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells.
Subcellular location: Golgi apparatus membrane; Single-pass type II membrane protein.
Interaction partners:
Sequence:
MPPSVRYFFIVSVTTVIVFIVLYVLSFGGDQSYQKLNISDSVMLAQVCSSFIDGKSRFLWRNKLMIHEKPSCTEYVTQSHYITAPLSQEEVDFPLAYVMVIHHNFDTFARLFRAIFMPQNIYCVHVDEKATAEFKGAVEQLVSCFPNAFLASKMEPVVYGGISRLQADLNCIKDLSTSEVPWKYAINTCGQDFPLKTNKEIVQYLKGLKGKNLTPGVLPPAHAIGRTRYVHREHLSKELSYVIRTTALKPPPPHNLTIYFGSAYVALSREFANFVLRDPRAVDLLHWSKDTFSPDEHFWVTLNRIPGVPGSMPPNASWTGNLRAVKWMDMEAKHGGCHGHYVHGICIYGNGDLQWLINSQSLFANKFELNTYPLTVECLELRLRERTLNQSEIAIQPSWYF
Protein: Misfire, isoform E (B7Z0F1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MIYVGRLLMELRSEMLTDSQPTHTLSSKTVPGLDETRFWHDDVYLIEFLPLMGHHILTSGTAYKISARLAEHTSNVLEGQLRTPLDRFKSAMNSKNFRREAPFQSCMFRVRLPDNRAKYESDFFMLDIVNYMRSELDTFKLFQRKYPLQDDEQAKCLKVIVNNILTRIKEGLDAHRFDHDVQPQRTTWDINRQLYLLDYFAKLPLELQNLKQKLRSCFLEHLDTSIGDVVNELQRLVAEIGSLSSMARTQDEWPELVLSLSASGKDVGVCRLNAKLFLNLRNQDADQDQETLCWRLKSFSFKSAGCSHTCPNCGCTTAIVSGCLSIVVERERKRFLAVVNKEWANIEPMLWQLNPEQTHFLCHVYIHQAKVRPGGEKKNICDSHLRVLFADQACETYTSPGTLSPIWNAVITFNWVSLPGGIGLYLKNPPLLSLEFYNSERSLPEDLVGMGSVAMSVISEDRASDSNWEDAGVFGCSKNPLRKLQRLKYLTPPPLKWVPIARKGTLQAEVLMSAEIIQISMESLTTGQNDKKEPQLATGIPMAIRPTMQNFVLEVFFVGLRNYSKSSMSSAGKRKINLMMGDLVLSSGPSTARIRNSINFLVAYASGVVVSSYRRKVRSHLYSTPIRVCQINRITGRRS
Protein: Pituitary homeobox 3 (Homeobox protein PITX3) (Paired-like homeodomain transcription factor 3) (O35160)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:17184956}.
Interaction partners:
- Nuclear receptor subfamily 4 group A member 2
- Forkhead box protein E3
- Tyrosine 3-monooxygenase
- Synaptic vesicular amine transporter
- Hepatocyte nuclear factor 3-beta
- Phakinin
Sequence:
MEFGLLGEAEARSPALSLSDAGTPHPPLPEHGCKGQEHSDSEKASASLPGGSPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERSQQAELCKGGFAAPLGGLVPPYEEVYPGYSYGNWPPKALAPPLAAKTFPFAFNSVNVGPLASQPVFSPPSSIAASMVPSAAAAPGTVPGPGALQGLGGAPPGLAPAAVSSGAVSCPYASAAAAAAAAASSPYVYRDPCNSSLASLRLKAKQHASFSYPAVPGPPPAANLSPCQYAVERPV
Protein: 3CxxC-type domain-containing protein (Q38DX3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLTITALLLLRPRHIMFTPPPLARRPGIFRCRVCSNTWTSSHVWVTRTTQRVYQGESCEECGTTTKPYYIGRPEETIFNRTRTPHPVKPGASTSRHGKKLRHIRYDKRVQRGRK
Protein: Eukaryotic translation initiation factor NCBP (Novel cap-binding protein) (nCBP) (mRNA cap-binding protein) (Q9FK59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures.
Interaction partners:
- Eukaryotic translation initiation factor 4G
- Eukaryotic translation initiation factor isoform 4G-1
- Eukaryotic translation initiation factor isoform 4G-2
- GYF domain-containing protein
- GYF domain-containing protein
- Protein ESSENTIAL FOR POTEXVIRUS ACCUMULATION 1
- Protein PIR
- Eukaryotic translation initiation factor 3 subunit K
- Transcription regulator
- CCR4-NOT transcription complex subunit 11
Sequence:
MEVLDRRDDEIRDSGNMDSIKSHYVTDSVSEERRSRELKDGDHPLRYKFSIWYTRRTPGVRNQSYEDNIKKMVEFSTVEGFWACYCHLARSSLLPSPTDLHFFKDGIRPLWEDGANCNGGKWIIRFSKVVSARFWEDLLLALVGDQLDDADNICGAVLSVRFNEDIISVWNRNASDHQAVMGLRDSIKRHLKLPHAYVMEYKPHDASLRDNSSYRNTWLRG
Protein: ATP synthase peripheral stalk subunit F6, mitochondrial (ATPase subunit F6) (ATP synthase peripheral stalk subunit F6) (P21571)
Organism: Rattus norvegicus (Rat)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MTVQRIFRLSSVLRSAVSVHLRRNIGVTAVAFNKELDPVQKLFLDKIREYKAKRLASGGPVDTGPEYQQEVDRELFKLKQMYGKGEMDKFPTFNFEDPKFEVLDKPQS
Protein: Alpha/beta-Hydrolases superfamily protein (At5g65400) (Q0V802)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLGYSYPCFQTGLRLTTAMAPEIHLKPKNPRILCLHGFRTSGRILQAGIGKWPDTILRDLDLDFLDAPFPATGKSDVERFFDPPYYEWYQANKGFKEYRNFEECLAYIEDYMIKNGPFDGLLGFSQGAFLTAAIPGMQEQGSALTKVPKVKFLVIISGAKIPGLMFGEPKAAVNAFSSPVRCPSLHFIGERDFLKIEGEVLVESFVEPVVIHHSGGHIIPKLDTKAEETMLSFFQSIRQMLSDESGSVRSLM
Protein: Phosphomevalonate kinase (EC 2.7.4.2) (P24521)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway. ERG8 converts 5-phosphomevalonate to 5-diphosphomevalonate. The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1846667}.
Interaction partners:
- Diphosphomevalonate decarboxylase
- Mevalonate kinase
- Hydroxymethylglutaryl-CoA synthase
- Acetyl-CoA acetyltransferase
- Isopentenyl-diphosphate delta-isomerase
- Squalene synthase ERG9
- Farnesyl pyrophosphate synthase
- Lanosterol synthase ERG7
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase 1
- Squalene epoxidase ERG1
Sequence:
MSELRAFSAPGKALLAGGYLVLDTKYEAFVVGLSARMHAVAHPYGSLQGSDKFEVRVKSKQFKDGEWLYHISPKSGFIPVSIGGSKNPFIEKVIANVFSYFKPNMDDYCNRNLFVIDIFSDDAYHSQEDSVTEHRGNRRLSFHSHRIEEVPKTGLGSSAGLVTVLTTALASFFVSDLENNVDKYREVIHNLAQVAHCQAQGKIGSGFDVAAAAYGSIRYRRFPPALISNLPDIGSATYGSKLAHLVDEEDWNITIKSNHLPSGLTLWMGDIKNGSETVKLVQKVKNWYDSHMPESLKIYTELDHANSRFMDGLSKLDRLHETHDDYSDQIFESLERNDCTCQKYPEITEVRDAVATIRRSFRKITKESGADIEPPVQTSLLDDCQTLKGVLTCLIPGAGGYDAIAVITKQDVDLRAQTANDKRFSKVQWLDVTQADWGVRKEKDPETYLDK
Protein: Luminescence regulatory protein LuxO (A7MVC2)
Organism: Vibrio campbellii (strain ATCC BAA-1116)
Function: Acts negatively to control the expression of luminescence. At low cell density, LuxO is phosphorylated, and together with sigma-54, causes repression of the luxCDABEGH operon. This repression could be indirect, LuxO could activate a negative regulator of luminescence. At high cell density, LuxO is dephosphorylated and inactive, therefore the luxCDABEGH operon is not repressed and light is emitted. LuxO and sigma-54 have also a role in activating the production of siderophore and in regulating the rugose colony morphology phenotype.
Interaction partners:
Sequence:
MVEDTASVAALYRSYLTPLGIDINIVGTGRDAIESLNHRIPDLILLDLRLPDMTGMDVLHAVKKSHPDVPIIFMTAHGSIDTAVEAMRHGSQDFLIKPCEADRLRVTVNNAIRKATKLKNEADNPGNQNYQGFIGSSQTMQQVYRTIDSAASSKASIFITGESGTGKEVCAEAIHAASKRGDKPFIAINCAAIPKDLIESELFGHVKGAFTGAANDRQGAAELADGGTLFLDELCEMDLDLQTKLLRFIQTGTFQKVGSSKMKSVDVRFVCATNRDPWKEVQEGRFREDLYYRLYVIPLHLPPLRERGKDVIEIAYSLLGYMSHEEGKSFVRFAQDVIERFNSYEWPGNVRQLQNVLRNIVVLNNGKEITLDMLPPPLNQPVVRQSVAKFIEPDIMTVSDIMPLWMTEKMAIEQAIQACEGNIPRAAGYLDVSPSTIYRKLQAWNSKDEKQNV
Protein: Putative N-acetylmannosamine-6-phosphate 2-epimerase (EC 5.1.3.9) (ManNAc-6-P epimerase) (P0A761)
Organism: Escherichia coli (strain K12)
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Interaction partners:
- N-acetylmannosamine kinase
- N-acetylglucosamine-6-phosphate deacetylase
- N-acetylneuraminate lyase
- Sialic acid transporter NanT
- Glucosamine-6-phosphate deaminase
- N-acetylneuraminate anomerase NanQ
- N-acetyl-D-glucosamine kinase
- PTS system N-acetylglucosamine-specific EIICBA component
- N-acetylmuramic acid 6-phosphate etherase
- HTH-type transcriptional repressor NanR
Sequence:
MSLLAQLDQKIAANGGLIVSCQPVPDSPLDKPEIVAAMALAAEQAGAVAIRIEGVANLQATRAVVSVPIIGIVKRDLEDSPVRITAYIEDVDALAQAGADIIAIDGTDRPRPVPVETLLARIHHHGLLAMTDCSTPEDGLACQKLGAEIIGTTLSGYTTPETPEEPDLALVKTLSDAGCRVIAEGRYNTPAQAADAMRHGAWAVTVGSAITRLEHICQWYNTAMKKAVL
Protein: Cobalt import ATP-binding protein CbiO (EC 7.-.-.-) (Energy-coupling factor transporter ATP-binding protein CbiO) (ECF transporter A component CbiO) (Q05596)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity. Presumably responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01710}.
Interaction partners:
- Cobalt transport protein CbiM
- Cobalt transport protein CbiN
- Cobalt transport protein CbiQ
- Cobalt-precorrin-5B C
- Sirohydrochlorin cobaltochelatase
- Cobalt-precorrin-5A hydrolase
- Probable cobalt-factor III C
- Cobalt-precorrin-8 methylmutase
- Cobalt-precorrin-6A reductase
- Cobalt-precorrin-2 C
Sequence:
MLATSDLWFRYQNEPVLKGLNMDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEHAGLTQPWLVKLHTQLGLPLCKTETEFFHRMQKCAFREAS