wanglab/gogpt-training-data huggingface dataset:
Protein: Syntaxin binding protein 1 (A0A1B0GVQ5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGEWPFRTLAR
Protein: Calpastatin (Calpain inhibitor) (P51125)
Organism: Mus musculus (Mouse)
Function: Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue.
Interaction partners:
- Calpain-2 catalytic subunit
- Calpain-1 catalytic subunit
- Calpain small subunit 1
- Calpain-3
- Calpain-8
- Calpain-9
- Calpain-10
- Calpain-11
- Calpain-13
- Calpain-5
Sequence:
MSQPGPKPAASPRPSRGAAARHTQEHVNEKNIGSSSKPGEKKGSDEKKAASLGSSQPSRPHVGEAATATKVTASSAATSKSPSMSTTETKAIPVNKQLEGPDQKRPREQAVKTESKKPQSSEQPVVHEKKSKGGPKEGSEPKNLPKHTSSTGSKHAHKEKALSRSNEQMVSEKPSESKTKFQDVPSAGGESVAGGGTVATALDKVVGKKKEQKPFTPASPVQSTPSKPSDKSGMDAALDDLIDTLGGHEDTNRDDPPYTGPVVLDPMYSTYLEALGIKEGTIPPEYRKLLEKNEGITQPLPDSPKPMGTDQAIDALSSDFTCSSPTGKQSEKEKSTGEIFKAQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKEAKAKEERQEKCGEDEDTVPAEYRLKPAKDKDGKPLLPEPEETSKSLSESELIGELSADFDRSTYQDKPSTPAEKKSNDTSQTPPGETVPRASMCSIRSAPPKLASLKGVVPEDAVETLAGSLGTREADPEHEKTVEDKVKEKAKEEEHEKLGEKEETVPPDYRLEEVKDKDGKPLLPKESQEQLAPLSDDFLLDALSQDFSSPANISSLEFEDAKLSAAISEVVSQTPAPSTHAAAPLPGTEQKDKELDDALDELSDSLGQRPPDPDENKPLDDKVKEKIKPEHSEKLGERDDTIPPEYRHLLDNDGKDKPEKPPTKKTEKPDQDRDPIDALSEDLDSCPSTTETSKNTAKGKSKKTSSSKASKDGEKTKDSSKKTEEVSKPKAKEDARHS
Protein: Transcriptional repressor CcpN (Catabolite control protein N) (Control catabolite protein of gluconeogenesis) (O34994)
Organism: Bacillus subtilis (strain 168)
Function: Transcription repressor that binds to the promoter of gapB and pckA genes, preventing their expression. Acts as a regulator for catabolite repression of gluconeogenic genes.
Interaction partners:
- Putative pyruvate, phosphate dikinase regulatory protein
- Phosphoenolpyruvate carboxykinase
- Catabolite control protein A
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Uncharacterized HTH-type transcriptional regulator YkuM
- Central glycolytic genes regulator
Sequence:
MSTIELNKRQEHILQIVKENGPITGEHIAEKLNLTRATLRPDLAILTMSGFLEARPRVGYFYTGKTGTQLLADKLKKLQVKDFQSIPVVIHENVSVYDAICTMFLEDVGTLFVVDRDAVLVGVLSRKDLLRASIGQQELTSVPVHIIMTRMPNITVCRREDYVMDIAKHLIEKQIDALPVIKDTDKGFEVIGRVTKTNMTKILVSLSENEIL
Protein: Glycerophosphodiester phosphodiesterase domain-containing protein 5 (Glycerophosphocholine phosphodiesterase GDPD5) (EC 3.1.4.2) (Glycerophosphodiester phosphodiesterase 2) (Phosphoinositide phospholipase C GDPD5) (EC 3.1.4.11) (Q8WTR4)
Organism: Homo sapiens (Human)
Function: Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (By similarity). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (By similarity).
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q640M6}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q640M6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q640M6}. Note=In a punctate perinuclear pattern. {ECO:0000250|UniProtKB:Q640M6}.
Interaction partners:
- Peroxiredoxin-1
- Insulin gene enhancer protein ISL-2
- Sulfiredoxin-1
- Motor neuron and pancreas homeobox protein 1
- Glycerol-3-phosphate dehydrogenase, mitochondrial
Sequence:
MVRHQPLQYYEPQLCLSCLTGIYGCRWKRYQRSHDDTTPWERLWFLLLTFTFGLTLTWLYFWWEVHNDYDEFNWYLYNRMGYWSDWPVPILVTTAAAFAYIAGLLVLALCHIAVGQQMNLHWLHKIGLVVILASTVVAMSAVAQLWEDEWEVLLISLQGTAPFLHVGAVAAVTMLSWIVAGQFARAERTSSQVTILCTFFTVVFALYLAPLTISSPCIMEKKDLGPKPALIGHRGAPMLAPEHTLMSFRKALEQKLYGLQADITISLDGVPFLMHDTTLRRTTNVEEEFPELARRPASMLNWTTLQRLNAGQWFLKTDPFWTASSLSPSDHREAQNQSICSLAELLELAKGNATLLLNLRDPPREHPYRSSFINVTLEAVLHSGFPQHQVMWLPSRQRPLVRKVAPGFQQTSGSKEAVASLRRGHIQRLNLRYTQVSRQELRDYASWNLSVNLYTVNAPWLFSLLWCAGVPSVTSDNSHALSQVPSPLWIMPPDEYCLMWVTADLVSFTLIVGIFVLQKWRLGGIRSYNPEQIMLSAAVRRTSRDVSIMKEKLIFSEISDGVEVSDVLSVCSDNSYDTYANSTATPVGPRGGGSHTKTLIERSGR
Protein: Vitamin D3 receptor (1,25-dihydroxyvitamin D3 receptor) (Nuclear receptor subfamily 1 group I member 1) (F8VRJ4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAMAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMILKRKEEEALKDSLRPKLSEEQQRIIAILLDAHHKTYDPTYSDFCQFRPPVRVNDGGGSHPSRPNSRHTPSFSGDSSSSCSDHCITSSDMMDSSSFSNLDLSEEDSDDPSVTLELSQLSMLPHLADLVSYSIQKVIGFAKMIPG
Protein: Acyltransferase (EC 2.3.1.-) (Q9XUW0)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367023}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367023}.
Interaction partners:
- O-acyltransferase
- Very long-chain fatty acid transport protein
- Abhydrolase domain-containing protein abhd-5.2
- Abhydrolase domain-containing protein lid-1
- Protein dhs-3
Sequence:
MLNYQIHKKLTDIKWVNIFSPWDRQRAYFALVVWFGLIYPFCCLCQVAPFVLFFTGQWIILGLYAVWYLYDRESPRRGGYRDNWFRNLSLHKWFAEYFPVKLHKTAELDPNQNYLFGYHPHGILGVGAWSCFGFDACNVKQVFKGIRFNICTLPGNFTAMFRREILLSIGMIESSKESIEHVLNSEEKGRAVVIVVGGAAEALEAHPGKHTLTLANRKGFVREAVKTGAHLVPVYAFGENDIYKQIDNPEGSKLRKIQEWGKKKMGISLPLIYGRGYFQMALGLLPMSRAVNVVVGAPIQVEKELDPSKEVIDEIHGVYMEKLAELFEEHKAKFGVSKDTRLVFQ
Protein: L-cysteate sulfo-lyase (EC 4.4.1.25) (Q5LL69)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Function: Catalyzes the desulfonation and deamination of L-cysteate, yielding pyruvate, sulphite and ammonium. Is involved in a L-cysteate degradation pathway that allows Silicibacter pomeroyi to grow on L-cysteate as the sole source of carbon and energy. To a lesser extent, can also act on D-cysteine in vitro, leading to the production of pyruvate, sulfide and ammonium. L-cysteine, L-cysteine sulfinate, and 1-aminocyclopropane-1-carboxylate (ACC) are not substrates for the enzyme.
Interaction partners:
Sequence:
MHLARYPRRFIAHLPTPLERLDRLTAELGGPEIWIKRDDCTGLSTGGNKTRKLEFLMAEAELQGADMVMTQGATQSNHARQTAAFAAKLGMDCHILLEDRTGSNNANYNNNGNVLLDHLHGATTEKRPGSGLDMNAEMEKVAEKFRADGRKVYTIPGGGSNPTGALGYVNCAFEMLNQFNERGLKVDHIVHATGSAGTQAGLITGLQAMNAQIPLLGIGVRAPKPKQEENVYNLACATAEKLGCPGVVAREDVVANTDYVGEGYGIPTESGLEAIRMFAELEAILLDPVYSAKGAAGFIDLIRKGHFKKGERVVFLHTGGAVALFGYDNAFDYSGRWVA
Protein: isochorismate synthase (EC 5.4.4.2) (Isochorismate mutase) (E0SLE3)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- isochorismatase
- 2,3-dihydroxybenzoate-AMP ligase, chrysobactin biosynthesis
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
- Chrysobactin synthetase cbsF
- anthranilate synthase
- Isochorismate synthase MenF
- Nonribosomal peptide synthetase
- Dimodular nonribosomal peptide synthetase
- Indigoidine synthase
Sequence:
MSTLAATSSSLDARTLQHDDFLFLSPDNSLHARGCYAALPAAVADGGHLQGDVQQQVKALFARARQDGIARPLLVGAIPFDKRQPARLFVPQQSRWFARDTLQHEPLPATPLAVRQIREIPEHDAFCQMVSAGVAATRSGELNKIVLSRLLDIDTDQPLDSIRLLLQLNQQNPWSYNFHVPLEQGALLGASPELLLHKQGNQIVSQPLAGSARRSDDPVEDQRLRRTLMASAKDRHEHRLVTDDIQRVLAPRCRTLTIPDTPELLSTPVLWHLATRVQGEVLDTQENALSIACLLHPTPALCGVPFEAARDRIAQLEPFSRGLFGGIVGWCDDEGNGQWVVTIRCGEVRQNRVRLFAGAGIVPDSQPVSEWHETGVKLSTMLRAFGLRQDQECAA
Protein: Mitochondrial coenzyme A transporter SLC25A42 (Solute carrier family 25 member 42) (Q86VD7)
Organism: Homo sapiens (Human)
Function: Mitochondrial carrier mediating the transport of coenzyme A (CoA) in mitochondria in exchange for intramitochondrial (deoxy)adenine nucleotides and adenosine 3',5'-diphosphate.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:19429682}; Multi-pass membrane protein {ECO:0000269|PubMed:19429682}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Thymidylate synthase
- Ribonucleoside-diphosphate reductase large subunit
- Proliferating cell nuclear antigen
- Replication factor C subunit 3
Sequence:
MGNGVKEGPVRLHEDAEAVLSSSVSSKRDHRQVLSSLLSGALAGALAKTAVAPLDRTKIIFQVSSKRFSAKEAFRVLYYTYLNEGFLSLWRGNSATMVRVVPYAAIQFSAHEEYKRILGSYYGFRGEALPPWPRLFAGALAGTTAASLTYPLDLVRARMAVTPKEMYSNIFHVFIRISREEGLKTLYHGFMPTVLGVIPYAGLSFFTYETLKSLHREYSGRRQPYPFERMIFGACAGLIGQSASYPLDVVRRRMQTAGVTGYPRASIARTLRTIVREEGAVRGLYKGLSMNWVKGPIAVGISFTTFDLMQILLRHLQS
Protein: FI05619p (Rho guanine nucleotide exchange factor 3, isoform A) (Rho guanine nucleotide exchange factor 3, isoform F) (Q9W0R9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTYHFRSSLTQFSVPQLEAPSGESAKRSKVRKEGNKSNMNTNSPSKNVTVKSSQLYRYIAPRNRSMLVMKDPRSMRTLRRMPKPGSNEMGTTSDCAASLSQQIKAVSSPTLSEPCLEEQPQKGTESTDVANTGSSAGSGGLGVLQKFKRTLNNFNNKNQLHISPLSPAAVGNNAPKTKTSPTTTTASIAPMITTTTASDPGSEAGDTSSGKYRFGPLIWRSSKERRKTKYNRRDKCNSGDSGIQIELEQDEQYSRATMAVSRQDEPRAFALTNGSCGVALSKMRAIRRTNSAKASSILGPFIVKTKIAKHLNIGESDKAERKAPESLPTRSLSQPNGLESYGMGRPDLEDSDSDSVASNEEAISFYPTTYAEVLYNFTAGGPQELGLERGMLIEILRKEVGPWWFGRIKKEETNLVEDILGPELGWFPKEFVRIIHCPETDNFFIAHRAAADEAAAEEATARAEEGSVPVPVAAFAEDTDVTVTTDQSNVTLIVIESPPTPSAPSVDFVAQPDHSTIIRRSAVRELLDTEVNYVKLLAAICDGYLPAMSKRIDIFSPNSIRLIFSNITAIYKFQRKFLEALRRGIEQNQVAKVFLKMHKGFLCYSTYCNAYPRALIELETYDRVKDARTILENCRESQNLAELPLSAHLLAPVQRICRYPLHLNEIIKSALEKGAKEGNDTDGAKSAGKTTDYEQLDVTELDIPDSQDTVNLALEAMRGITEAVNEGKRHSETIARHQASFQNFKGPPLHLHSARFFLQVDATRQKQNLWNSSYTLFLFDNQLVYCKRDIIKRSHFIYKGRIFLDRCRVVNVRDGKMFGHTIKNSLRIYSESRDKWYDFSFRSANRKHRFLSTLALERQFGGKALYVSEMTGFEYNYEERPGDYSDQSDYDAQDFELATGVTSGESSLPESPAKSTSRLCETLPKKSQSRDGISSAENSQIVTTTSTGSLGRRHFGNWFRKPKSANCTPSQSPTHKPSFDADATLTEARVAAMELAEAAAALVPTDSSSA
Protein: Protein GndA (P0DQD7)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:29039649}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLLLIPSNHISIKETSSLMVVTPSSRTLFVVIVSFQQRALTSSVPVFLAVKRGR
Protein: Cilia- and flagella-associated protein 65 (Coiled-coil domain-containing protein 108) (Q3V0B4)
Organism: Mus musculus (Mouse)
Function: Plays a role in flagellar formation and sperm motility.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:31571197}; Single-pass membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000250|UniProtKB:Q6ZU64}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:31571197}. Note=Expressed in the cytoplasm of the spermatogonia, round spermatids, early elongating spermatids and late elongating spermatids and in the flagella of epididymal spermatozoa. {ECO:0000269|PubMed:31571197}.
Interaction partners:
- Cilia- and flagella-associated protein 70
- Tetratricopeptide repeat protein 29
- Cilia- and flagella-associated protein 69
- Cilia- and flagella-associated protein 43
- Cilia- and flagella-associated protein 251
- Cilia- and flagella-associated protein 44
- Cilia- and flagella-associated protein 91
Sequence:
MLIQKNQCHITRTRENCDCTMNTVNEDLCLSASTLGSSSVTTQLVDPLDRKICLIRRQNDVKKRVIWGIEVAEKLHWKGWELGKETTRTLVLKNLSLKTQKMKYRPPKTKFFFTIIPQPIFLSPGITLTLPIVFRPLEAKEYTDQLWFEKEEGVFCVTLKATLPCYKLDCPSSLQLPMCALGDTVETWFCLNNVGDLPTFFTWEVPAPFQILPTTGLLEPGLGCKIKVTFEPLIAVIHEVEALCWYGKGNKQKNSINIQAAAKCAQLLVSIKHKGLEDQDQEGFQKVVHFGYVSVGSVAERQIRLYNPSAVNAPFKIEMAEHVLTKDPSFSCSTSQGIVPPGEKKCLSLFFHPKTLDSRAIDYFSIIPSGCATKTLLQVVGFCRGPDAVLQHSCVNFHWVKLGERREQTLWIENQSDCQAHFQFDIDCQESVFSIRPAFGTLAGKTRMTLHCAYQPTHPIISFRRVACLIHHQDPLFLDLIGTCHSDSIKPAILTPQHLTWYRTHLARGLTLYPPDILAAMLKEKKLERDEDGALILPIESLPMQELEDLPDQKYPNIPPMTEYFFDGTRDLAIFPPAVCLEPIDVDFGACPGPEAPNPVPLCLRNYTKGKITVVWTGRSDCPFWVTPVTSDVPPLKSIALRLYFQPSSPNCLYAVELEAFAVYKVLQCYSNIEEDCTVVPSWCLKVRARGHSYSPALEHHIPHYSLDSPQTFPAVSPGKPSYRSLFLVNKGSMLMTFSLAPNSSSDITLRPSSGLIGPGAHQVFLISTYPKGTSWRQHIFYLNFNFYPQYLKEVSMQSREEPLDLKLDTHKSIYFKPTWVGCSSTSNFTFHNPSRLPLQFEWRVSQEHQKVLAVQPSKGTIHPNENLTLTWIFSPLEEIKYLFRVGIWVWEARQSQKTKPQATVHYRIRLVGMGVTGCLSAKPVELDFGNVLVNSQEVKPLVLLNDGNCTLYYRLVLEQHRPKGLHSDPCALEFDHSEGTMPPHSQDTIYLTARPKVRSQYSWTISYCLLSQRAPPTNSMDGKKKALCHVSLAAAYPLLSVLDICSMGSTEGITRKHLWHLFSLDTLNSYLARDPTAKELTYKVPTRHSMSRTPPIFTPLKLDFNFGAAPHNALPSVVLLVLKNCGLVPLDWAFLFPSDQQLDLDLWVEQEDLNSNELHQMRAEDNSLFSINPKTGSLNPGQEQMVEFTYRHLFVGTDRLSVLFKVSHGREILLQFIGVTVKLEQKYVHFTSTIHQFIPVPIGDTLPPRQIYELYNGGSVPVTYEVQVSVLSKVQEKNFDHPIFCCLNPKGDIQPGTTARILWIFSPIEAKTYTVEVPIHIIGWNSAVVCFQGVGYDPCVMGDTAPFHSISSWDSSSISSRLMVPGQNVFLSQSHISLGNIPVQSKCSRLFFLNNISKNETIVFTWKPRSLDFGEVTVSPMEGEVGPEEGAPILVTLKASVHASFYSIDLICKVYQRELMRQYHKELQEWNEEKARQEVEFTITDRKVKRRAYCAAHEPPKKYKTLPPITNQPPLNRPATWNLKLAKKETSWPCPQPPVPGLLCLGLTARAHATDYYLANFFSEFPCHFLYRELPKKKSSKEESKSSEELPDKKGPVSRQKQQLLVDCLTSIIRGLLEDKNFHNAVDQNLVEQVPYFCQFWNEQSARFLAQKSSLYLVPILSLPPSYEGRKSKEQEEDLFGKMPGGQEDDEEEEEDEEEAEEEEEEIEEEMSKDEEDIDKDAKMTWSGIKVTETSQHSLQWQWQQDLKTIIKEETESDEKEAIGRLPAFANLQEAILENMIQNILVEASRGEVVLTSRPRIIALPPVSMHRTDNLLQMSQGDVLCSGMQHPDCLLVSASSPSNMTT
Protein: Meiotic driver SPOK3 (Spore killer 3) (A0A516F180)
Organism: Podospora anserina (Pleurage anserina)
Function: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system, leading to poisoning of progeny that do not inherit the allele.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:B2AFA8}. Nucleus {ECO:0000250|UniProtKB:B2AFA8}.
Interaction partners:
Sequence:
MSDKDRITQLLRELEEAKAREAQERCEKERLQLEHRKTTFLEYLRNCHRHLYNALRLTDTSRSSTGYTKVVGKYYPKRLRPWTNFTNVLHPHYFNLVQQICGQRQLFESASTTKNLGTIISDHLAGNEKAIDRFEVDAVERPVQGILKVLATHEEAGKASICPEFRFSANLRELTQKDDGSSGADDNTSDRSLERRQQAGPNKRPTSKSKYICSNRQPDGVGIRMQPDGGQTQAFIYDYKAAHKVAIEHVRSATAKEHLFHEVVARINDDKLSRDEEVQHREQAEAFIAMALTQVFDYMITYGVSYGYVAAGRCLLLLYVDRDDWQTLYCHPCLPADDVGEPTNDWTDRLSHTAVAQLVSFCLSSFQSEALEGQSLETALSVAKATLKTWSESYADVAYLGLEPAELSSAPSSQNTDISEYTSKAKPTGRKVTLRSCKPAAVLPQGNEHDEHDEEDHSEPGASRLAKRERGPSSGGKDDGRSMVDPQPTRQYCTQACLLGLKRGKDLDENCPNVSLHRFDGSSRHPVNAHSFTDMVEQQLLLSPYKGCRMVDFWGKRGAMGWLFKLELLPYGYTFVGKGTVEDRLNRLEHEGRVYARLDHLQGDVVPVHLGLVRLDRGYILPGLEFAVYMMLMSWAGQTPSANMDDAETLKSESLTAIWSEGVDHGDNNRANYLWNAERCRIMIIDFDRAHLFPPLKARAVSRLSKPKRKRETLNSYLTEITGREARHVFKQMDRSPMATPSHGG
Protein: Aurora kinase (EC 2.7.11.1) (Serine/threonine-protein kinase ark1) (O59790)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the spindle checkpoint attachment response during spindle formation, kinetochore microtubule interactions and chromosome segregation during anaphase. Ark1 activity depends upon cut17 function and phosphorylation. Ark1 with bir1 is required for full-scale association with kinetochores and formation of a complex with mad3. Ark1 is also required for phosphorylation of histone H3 that accompanies chromosome condensation and condensin recruitment to mitotic chromatin. Ark1 with pic1 is required for the execution of cytokinesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}. Note=Associates with the elongating spindle during anaphase.
Interaction partners:
- Chromosomal passenger complex protein bir1
- Inner centromere protein pic1
- Inner kinetochore subunit mis6
- Outer kinetochore KNL1 complex subunit spc7
- Inner kinetochore subunit fta3
- Inner kinetochore subunit fta2
- Kinetochore protein mis13
- Meiotically up-regulated gene 118 protein
- Meiotic recombination protein rec8
- Inner kinetochore subunit mal2
Sequence:
MSDSKLADSLNCLSVSTPSTTANPGRQQLLRLAVSNQRQVNNVSLANGKENKRTSNSKFNSSLRKIEEPIAGVPSSAGPQWREFHIGMFEIGKPLGKGKFGRVYLAKEKKTGFIVALKTLHKSELVQSKIEKQVRREIEIQSNLRHKNILRLYGHFHDEKRIYLILEFAGRGELYQHLRRAKRFSEEVASKYIFQMANALSYLHKKHVIHRDIKPENILLGIDGEIKLSDFGWSVHAPSNRRTTLCGTLDYLPPEMVEGKEHTEKVDLWSLGVLTYEFLVGAPPFEDMSGHSATYKRIAKVDLKIPSFVPPDARDLISRLLQHNPEKRMSLEQVMRHPWIVKYKDSWTRKSSESS
Protein: CAAX prenyl protease 1 homolog (EC 3.4.24.84) (Farnesylated proteins-converting enzyme 1) (AtFACE-1) (FACE-1) (Prenyl protein-specific endoprotease 1) (Zinc metalloproteinase Ste24 homolog) (AtSTE24) (Q8RX88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proteolytically removes the C-terminal three residues of farnesylated proteins. The substrate specificity is only partially overlapping with that of FACE2.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12039957, ECO:0000269|PubMed:18641086}; Multi-pass membrane protein {ECO:0000269|PubMed:12039957, ECO:0000269|PubMed:18641086}.
Interaction partners:
- CAAX prenyl protease 2
- Protein-S-isoprenylcysteine O-methyltransferase A
- Protein-S-isoprenylcysteine O-methyltransferase B
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1
- Protein farnesyltransferase subunit beta
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Farnesol kinase, chloroplastic
- NAD
Sequence:
MAIPFMETVVGFMIVMYIFETYLDLRQLTALKLPTLPKTLVGVISQEKFEKSRAYSLDKSYFHFVHEFVTILMDSAILFFGILPWFWKMSGAVLPRLGLDPENEILHTLSFLAGVMTWSQITDLPFSLYSTFVIESRHGFNKQTIWMFIRDMIKGTFLSVILGPPIVAAIIFIVQKGGPYLAIYLWAFMFILSLVMMTIYPVLIAPLFNKFTPLPDGDLREKIEKLASSLKFPLKKLFVVDGSTRSSHSNAYMYGFFKNKRIVLYDTLIQQCKNEDEIVAVIAHELGHWKLNHTTYSFIAVQILAFLQFGGYTLVRNSTDLFRSFGFDTQPVLIGLIIFQHTVIPLQHLVSFGLNLVSRAFEFQADAFAVKLGYAKDLRPALVKLQEENLSAMNTDPLYSAYHYSHPPLVERLRAIDGEDKKTD
Protein: Succinate/fumarate mitochondrial transporter (Regulator of acetyl-CoA synthase activity) (P33303)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transports cytoplasmic succinate, derived from isocitrate by the action of isocitrate lyase in the cytosol, into the mitochondrial matrix in exchange for fumarate.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Malate synthase 1
- Isocitrate lyase
- Fructose-1,6-bisphosphatase
- Isocitrate dehydrogenase cytoplasmic
- Carnitine O-acetyltransferase, mitochondrial
- Phosphoenolpyruvate carboxykinase
- Carnitine O-acetyltransferase YAT2
- Citrate synthase 3, mitochondrial
- Carboxylic acid transporter protein homolog
- Acetyl-coenzyme A synthetase 1
Sequence:
MSQKKKASHPAINLMAGGTAGLFEALCCHPLDTIKVRMQIYRRVAGIEHVKPPGFIKTGRTIYQKEGFLALYKGLGAVVIGIIPKMAIRFSSYEFYRTLLVNKESGIVSTGNTFVAGVGAGITEAVLVVNPMEVVKIRLQAQHLTPSEPNAGPKYNNAIHAAYTIVKEEGVSALYRGVSLTAARQATNQGANFTVYSKLKEFLQNYHQMDVLPSWETSCIGLISGAIGPFSNAPLDTIKTRLQKDKSISLEKQSGMKKIITIGAQLLKEEGFRALYKGITPRVMRVAPGQAVTFTVYEYVREHLENLGIFKKNDTPKPKPLK
Protein: Aminoacyl carrier protein (A9CHM9)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Aminoacyl carrier protein. Can be charged with L-alanine, L-glycine or L-serine, via the formation of a thioester bond between the amino acid and the 4'-phosphopantetheinyl prosthetic group, catalyzed by the Atu2573 ligase.
Interaction partners:
- Amino acid--[acyl-carrier-protein] ligase
- Acyl-CoA dehydrogenase
- Peptide synthetase
- Peptide synthetase, siderophore biosynthesis protein
- Malonyl CoA-acyl carrier protein transacylase
- NADH-quinone oxidoreductase subunit C
- beta-mannosidase
- Uncharacterized protein
- Serine aminopeptidase S33 domain-containing protein
- NADH-quinone oxidoreductase subunit B
Sequence:
MNATIREILAKFGQLPTPVDTIADEADLYAAGLSSFASVQLMLGIEEAFDIEFPDNLLNRKSFASIKAIEDTVKLILDGKEAA
Protein: Profilin-1 (Profilin I) (P62962)
Organism: Mus musculus (Mouse)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR (By similarity).
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Toll-like receptor 11
- Toll-like receptor 12
- Vasodilator-stimulated phosphoprotein
- Actin, cytoplasmic 1
- Protein diaphanous homolog 1
- Cofilin-1
- Actin nucleation-promoting factor WAS
- Actin, cytoplasmic 2
- Protein diaphanous homolog 2
- Profilin-4
Sequence:
MAGWNAYIDSLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVSITPAEVGVLVGKDRSSFFVNGLTLGGQKCSVIRDSLLQDGEFTMDLRTKSTGGAPTFNVTVTMTAKTLVLLMGKEGVHGGLINKKCYEMASHLRRSQY
Protein: Zinc finger protein 20 (Zinc finger protein KOX13) (P17024)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMFQDSVAFEDVAVSFTQEEWALLDPSQKNLYRDVMQETFKNLTSVGKTWKVQNIEDEYKNPRRNLSLMREKLCESKESHHCGESFNQIADDMLNRKTLPGITPCESSVCGEVGTGHSSLNTHIRADTGHKSSEYQEYGENPYRNKECKKAFSYLDSFQSHDKACTKEKPYDGKECTETFISHSCIQRHRVMHSGDGPYKCKFCGKAFYFLNLCLIHERIHTGVKPYKCKQCGKAFTRSTTLPVHERTHTGVNADECKECGNAFSFPSEIRRHKRSHTGEKPYECKQCGKVFISFSSIQYHKMTHTGEKPYECKQCGKAFRCGSHLQKHGRTHTGEKPYECRQCGKAFRCTSDLQRHEKTHTEDKPYGCKQCGKGFRCASQLQIHERTHSGEKPHECKECGKVFKYFSSLRIHERTHTGEKPHECKQCGKAFRYFSSLHIHERTHTGDKPYECKVCGKAFTCSSSIRYHERTHTGEKPYECKHCGKAFISNYIRYHERTHTGEKPYQCKQCGKAFIRASSCREHERTHTINR
Protein: Kalirin RhoGEF kinase b (EC 2.7.11.1) (A0A2R8RHL8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MMNSAEAAEEGPTDPDTEPFFKTVSSFSSGSLRNDGIKAADVLTVLREKVAFVSGGRDKRGGPILTFPARSNHDRIKQEDLRKLVTYLSTVPSEDVSKRGFTVIVDMRGSKWDLIKPLLKTLQESFPAEICVALIIKPDNFWQKQKTNFGSAKFTFETSMVSVEGLTKLVDPSQLTGDLEGTLEYDHVEWTELRVSLEEFTGGALHLLSRLEELQEVLSRQELASSAEEARKLLEDHARLRKTMAKAPVDELDQEGQRLLQKIRDGGDGRLSGGADFQSLVPKISALLDKLQVTRQHLLQGWHNRKQQLDQCFQLRLYEQDAEKMFEWIGHNKELFLQTHTDIGVSYQHAADLQTQHDHFAMNSMNAYVNISRIVSVATRLCEAGHYAATQIQQISGQLDHDWKSFASGLEERSAILAMSSVFHQKSEQFLSSMEGWVKSCGEVGLPTVTQELELAIHNHQNLYEQVTTAYTEVSQKGKTLLDVLQRPPPPADSGSLTAGADYSQAVRGVLEVVHEVVHQYRRLEGLLQHHKLRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSVHRARALQKRHDDFQEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYAAAHHLEVRVQEFVRRVEQRKLLLDISVSFHTHTKELWSWMEDLQKSLVEPVVNSESVDAVQELIRQFQQQQSSTLDATLNVIKEGEELIQHLRDSALACNKLPHASSVAHIEGVLQQLDEAQAHMEELFHERRIKLDIFLQLRIFEQYALEVMGELDAWKQDLMRQATDFNTEELTLAEQRLHRHTERKLAMNNMTYEVIQQGQDLHQYIMEVQASGMELTGEKDVDLAAKVQELLEFLNEKQHELEVSAEHTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLTASTTNAGPLSEVEQLQREHEQFQLAIESLLHADSLQRTHQSALQLQQRAELLLQAGHYDPDAVRACAETVALHWQTLMLKMEDRLKLVNASVAFYKTSEQVCNVLESLELEYRREEDWCGGHDKLGSTAETDHVSPLINKHLEQKEAFLKACTLARRNAEVFLKYIHRNNVSMPGVVTHNRATESQVKAILSELLQRENRVLHFWTMKKRRLDQCQQYVLFERHAKQAIDWLQETGEYFLSTHTSSGETSEKAQELLKEYEDFRVSAKQTQEKVKLLIQLAGSLVEKGHVHVTELKRWVSTVDRRYRDFSMRMGHYRCSLDRALGVCSEDNKDLELDIIPANLTHTDPEVNLNDPDHEVNEEKKKSARKKEYIMAELLQTERAYVRDLQECLETFFWEMTSGVEVPSGIANKEHVIFGNIQEIYDFHNNIFLKELENYEQLPEDVGHCFVTWADKFHMYVTYCKNKPDSSQLIQGQAGRFFDEIQRRHGLANSISSYLIKPVQRITKYQLLLKELLTCCEEGKGEIKEGLEVMLSVPKRANDAMHVSMLEGFDENLAVQGELILQDTFQVWDPKSLIRKGRDRHLFLFEISLVFSKEMKDSSGRTKYVYKNRLLTSELGVTEHIEGDPCKFALWAGRTPTSDNKTVLKASSIEVKQEWIRNIREVIQERTVHLKGALKEPIHAPKTPARQRSISKRETTEDADSQGDASSQPDTISIASRTSQNTVDSDKLSGGCEQTVVLQDFVAGSVGELSIQSGQTVELLERSGERPGWCLVRTTENSPPQEGLVPSSTLSVSHSRSSVDMDCFFPPGKENYPVGSSEVKSESAASLQPQTSVTSLPTGSPGPKRSGTTGNTLKKWLTSPVRRLSHGKGDNANAKKPNNKQRKRDGRKSVELGPHHQDSTEERGRRGTNSGGEEEAEDEPHTPLPPPMEIIKDPSAQEDKTPERGSFPVLGSDTPSDQTPRDPETEQKNKALRGRMFVLNEMVQTERDYVKDLGVTVEGFMRRIGEKGVPEDMTGKDKIVFGNIHQIYDWHKEFFLCELEKCLQDHDKLAELFIKHERRLHMYVIYCQNKPRSEFVVAEYDKYFEGVQQEINSRLAISDYLIKPIQRITKYQLLLKDFLKYSTKAGLDCKEIEKAVELMSLVPKQCNDMMNLGRLQGYEGKLTAQGKLLQQDTFFVTEQDSGVLSRSKERRVFLFEQIVIFSELLRKGSSTPGYQFKKSIKVSYLSMEEQVESDPYKFVLLCRGSSERLTLQAANVDIKKEWVQSIRELLDMQINFLTALQNPQAALTSQLSNSNRSSSSQPSTPLKPNTAPNGSPAQKNNKHAEEDLDEGECNGLSSVLVTQDYNAVKEDEICVVVGEKVQIMASNQQNMCLVYRPANSQSPAAEGWVPGHVLSSTR