wanglab/gogpt-training-data huggingface dataset:
Protein: StAR related lipid transfer domain containing 10 (F5H8G1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAEVGWNLTYSRAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDP
Protein: Antitoxin HicB (P67697)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents HicA-mediated cessation of cell growth and inhibition of cell proliferation.
Interaction partners:
- Probable mRNA interferase toxin HicA
- Antitoxin HigA
- mRNA interferase toxin HigB
- Antitoxin MazE
- mRNA interferase toxin RelE
- Antitoxin RelB
- Antitoxin MqsA
- Endoribonuclease toxin MazF
- Antitoxin ChpS
- Antitoxin DinJ
Sequence:
MRYPVTLTPAPEGGYMVSFVDIPEALTQGETVAEAMEAAKDALLTAFDFYFEDNELIPLPSPLNSHDHFIEVPLSVASKVLLLNAFLQSEITQQELARRIGKPKQEITRLFNLHHATKIDAVQLAAKALGKELSLVMV
Protein: Acireductone dioxygenase 1 (Acireductone dioxygenase (Fe(2+)-requiring) 1) (ARD' 1) (Fe-ARD 1) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring) 1) (ARD 1) (Ni-ARD 1) (EC 1.13.11.53) (O48707)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}.
Interaction partners:
- Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- Aromatic aminotransferase ISS1
- At1g77670
- Acireductone dioxygenase 4-requiring) 4)
- Acireductone dioxygenase 2-requiring) 2)
- Acireductone dioxygenase 3-requiring) 3)
- Thioredoxin superfamily protein
- Guanine nucleotide-binding protein subunit beta
- Probable plastidic glucose transporter 3
- Protein NDL1
Sequence:
MGEAAKDQTEEVIQAWYLDNKEEDQKLPHHKDPKEFVSLDKLAELGVLCWRLDADNYETDEELKRIRESRGYSYMDLCEVCPEKLPNYEEKVKMFFEEHLHIDEEIRYCLAGSGYFDVRDLNDIWIRVWVKKGGLIVFPAGIYHRFTVDSDNYMKAMRLFVGGPVWTAYNRPHDHLPARKAYMKKFLKVIGDRNIDASA
Protein: Ras2p (Q5ANJ9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Adenylate cyclase
- cAMP-dependent protein kinase
- cAMP-dependent protein kinase
- Gpr1p
- Rga2p
- Ras-like protein 1
- Ras GTPase activating protein
- Cell division control protein 42 homolog
- Guanine nucleotide-binding protein subunit alpha
- Cell division control protein 25
Sequence:
MSLLLDSLHALTKNYDMCVIGSSNVGKSTLVLHYVYHHFDESLYDLDAVYTKRIITPDTNGKFREITIFESDFHIDMYTLTRERHVLNANTIVLVYAIDDYQSFTALEDYYERINQLRPSIPISVIASKLDLDTNREVSYYEGAEFAKRIGAVSFNECTRANVMGVNQAFESIANVAVKIQLDKDNTVPTVDNEIQQKENDQDSNITTTPTSTTTQSQTSNYSPQRSLQESIPVNNFTQYDNNPHQVNSNKNQFDAEQNTPLSTLTRESTMLTSDLNGSTPIAQTPSTSSRQRKTRLKQSSGPSAKSSQIHAENKCCIIT
Protein: Inositol-1-monophosphatase (EC 3.1.3.25) (Q57ZU5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 3'
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Inositol-3-phosphate synthase
- Phosphoinositide phospholipase C
Sequence:
MPINNCELDAALQLALRAAHGVACTIDKAMEERDTTLLDIQTRENGEGLITQYDKQCEEEIIAILRLGAPSYDIISEELHSDTVLTDAPTWMVSTINGTSSFIHGLFDCCVSIALVVDKEPVIGVVNAPRLHEVYSAIRGRGAYLNGQRIRVSETRSINQSVVYLHNPCGEGEVVVNTVIEMQKEFTRMPVHALRVHGSVALDMCFIATGRAELFLKVGVHPWDVAAATVIVREAGGVVHDIDNLNILDLTTCTVCCANSSEISNIGVGVAAKHGYKKSVLGC
Protein: Ribonucleoside-diphosphate reductase small chain (EC 1.17.4.1) (Ribonucleotide reductase small subunit) (P42170)
Organism: Caenorhabditis elegans
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Adenylate kinase
- Uroporphyrinogen-III synthase
- Nucleoside diphosphate kinase
- guanylate kinase
- Probable adenylate kinase isoenzyme ZK673.2
- UMP-CMP kinase 2
- UMP-CMP kinase 1
- Adenylate kinase isoenzyme 1
- Nucleoside-diphosphatase mig-23
Sequence:
MTLTEIQNVEKENAGASVPKHSSNKLKLEKELEKLEIVDQTKAASAEETNNESEVNELDADEPMLQDLDNRFVIFPLKHHDIWNFYKKAVASFWTVEEVDLGKDMNDWEKMNGDEQYFISRILAFFAASDGIVNENLCERFSNEVQVSEARFFYGFQIAIENIHSEMYSKLIETYIRDETERNTLFNAVDEFEFIKKKADWALRWISDKKASFAERLIAFAAVEGIFFSGSFASIFWLKKRGLMPGLTHSNELISRDEGLHRDFACLLYSKLQKKLTQQRIYDIIKDAVAIEQEFLTEALPVDMIGMNCRLMSQYIEFVADHLLVELGCDKLYKSKNPFDFMENISIDGKTNFFEKRVSEYQRPGVMVNEAERQFDLEADF
Protein: Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (ENR) (EC 1.3.1.9) (NADH-dependent enoyl-ACP reductase) (P0AEK4)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Acyl carrier protein
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Pimeloyl-[acyl-carrier protein] methyl ester esterase
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Sequence:
MGFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQNDKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKVWPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISSYSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGLAKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIKDFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGISGEVVHVDGGFSIAAMNELELK
Protein: Probable splicing factor, arginine/serine-rich 6 (CeSRp20) (RNA-binding protein srp-1) (Q18409)
Organism: Caenorhabditis elegans
Function: Plays a functionally redundant role in shifting germ cell sexual differentiation in hermaprodites. Required for the development of somatic gonad structures and for progression from larval stage to adulthood.
Subcellular location: Nucleus {ECO:0000269|PubMed:10906451}.
Interaction partners:
- Probable splicing factor, arginine/serine-rich 4
- RNA-binding protein rnp-4
- Probable splicing factor, arginine/serine-rich 3
- Probable splicing factor, arginine/serine-rich 2
- Probable splicing factor, arginine/serine-rich 7
- Probable splicing factor, arginine/serine-rich 5
- Splicing factor U2AF 65 kDa subunit
- RRM domain-containing protein
- RNA helicase
- Splicing factor U2AF 35 kDa subunit
Sequence:
MDAKVYVGGLPSDATSQELEEIFDRFGRIRKVWVARRPPGFAFVEYDDVRDAEDAVRALDGSRICGVRARVELSTGQRRGGGGRGGGFGGRGGGGRDRSPYRGDRGRSRSRSRDRGRDRSRDRSRDRSRDRSRDRSRERSRERERTRSRSRSPQERDRSHSKSRSRSRSRSRSRSASPH
Protein: Transmembrane protein (Q38FI7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRIRRTAFSFLGGFAIADFYVNCTNLDDIQNELGVQGVERVASPNYFSWIFRSTPVKPQQPAFGSTLREDVELLFQKSPLSGAALVFTAVSLGGIWSLLGSCAAVVLDGDEGSERYDALKRWLNG
Protein: Aquaporin-3 (Q9XW36)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Aquaporin
- AQuaPorin or aquaglyceroporin related
- Aquaporin
- Probable glycerol kinase
- Heme peroxidase 2
Sequence:
MLSDSSCSSSDRSFKFPFDTTDALSIHELAVKDLPKPDAENPFSVAMHSPPGSPPFAVDRKSVDNSVVAVTDTPFEFAPSQKSSQHTNRPPPFVKPEEEMMYINHVERLKPKFAIGNELIRAFLAELFCTGFLVFGGECVNAQYVLSQGKNNEWIGISVGWGLVLMLAVLMGSKISGAHLNPAVSFFQLTQGKINLIRFLVYAVAQNIGAFLGAFGVFCVYYDAINVFEGGNRTVTGPTATASIFATYPGPFLGTFNAIVDQIAGTLVLCLGVAAITDRRNGIPAFLQPAWIGALLAFLGMSLALNAGYAINPARDFAPRLFNLCAGYGWEVFSYRNYKWFWIPIICPMIGGVLGAWLYEFFIGFHIQDEDAVSLDSESDKQLKTMIDNMVDIENQLPEYTDKKQLSDIASIHQNPSLRNI
Protein: ADP-ribosylation factor-like protein 3A (Q57XJ4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNNSLKKGSQSGRCCRCGAAFDHRNARRAVKCTKCQRIFHTKCFLAETGLSAAVDSHCVVCLCGISQTPYPLTIQQNTLARKFLRDGFVVVPLTRKPKSKQTTLEKLATFRANAERYFGAFIRAYENELEISSKAPSLQSGYSNFRERGKGRYEVIFPSIREEVLSIIENCDEVTMTLDLLLAPTGKRGDMQRKLMSCGCFYSLPGSLRQDVHTDGPALSTVEDLFPYAINVFVPLVPLNKTNGTEFFPGSHRVNYSSKPVSQQRPVTPTVPLGKVLLFDYRVLHRGLGNRLGFHRPCYYATYARSWYEDKFNFSSTRYRTALHVPSYLLERRCDREVSKRCKVE
Protein: Protein PET111, mitochondrial (P08468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for translation of the mitochondrial gene for cytochrome c oxidase subunit II (COX2).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- COX3 mRNA-specific translational activator PET494
- Protein PET54
- Mitochondrial COX1 translation regulator PET309
- Protein PET122
- Mitochondrial inner membrane protease subunit 1
- Cytochrome c oxidase subunit 2
- Mitochondrial translation factor ATP22
- ATPase expression protein 3
- Mitochondrial translation factor 2
- Cytochrome c oxidase assembly protein COX18, mitochondrial
Sequence:
MLQRRFISSSGIKRLLHRESNKVMHTVFFKVRYYSTELIKKKHKEDIEDWVKAQLKDSSTISGVYESRNKLDWMDSITKSPSSLDILKNQYNIVKDKDFGILWKQKFESADPDILMTIISLSTNQKVLFSIQQLLILINSLHFLKRDYDIGQIYTTYEQFTPLLASHTDKGTYGQFIEIMLVVQHNLHHFDVCETLFAEYIKYCKVKPQMISLGLNSFIRSNNTQLAVEFYTQAITNPDTFPITEKQLFEFLRCMERYLDMSSMKHIFYLWLKVKCGDEQSSSTNLPSFKTLAIIHRMLLRFSNTDELNDFLTNPVVLSTGYTSSVQFELIEFCHSLYCIKGDRTKSIDDSILMERVDKFITRLNNNISTRKELYMSVVQAYVSTNNFENLKVILEKIQRDNDISIDGSFHLCISRYFVNTNQFEGLFKYYRSVVKTTDGKTRLRPAFIQQLWSCAVNVYPMLAKEITNDLLVTLKRSQYSKCLTWVYTFLQENAHIHTRKINGGEDSSLSGFNAVDFERFEEFKKKVSHNDVYGAELVISNSLKEGIAPQFSFLYSVLALCLRNSLTGLARVVDVILRTRFRYIPLKVDILWLKWEIISNYRSFEKLSAEHLKELEFKLKEFERVHQKELSVQNYLQLTQICFHTRDFKYACYLISQARKNLDTSNNKQWMMYYMTSLKLASRMHESERFSRILKDWNCNHRASLITPGCIRQIKGFMKYFEKRPAYISTAASIDNKEIKDRIDELVLRYVDYKYQGLENMRKLTLFLKEWFDEEISLLKLEQNERKMKLFEENKKEEE
Protein: Membrane-associated protein gex-3 (Gut on exterior protein 3) (P55163)
Organism: Caenorhabditis elegans
Function: Rac effector required for tissue morphogenesis, cell migrations and egg laying. May play a role in egg laying and in yolk protein clatherin-mediated endocytosis by oocytes during oogenesis. Plays a role in the formation of gap junctions between EA and EP endodermal precursor cells in embryos.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11877381}. Note=Enriched at cell boundaries.
Interaction partners:
- Cytoplasmic FMR1-interacting protein homolog
- Wiskott-Aldrich syndrome protein family member
- SH3 domain-containing protein
- Protein BRICK1
- Ras-related protein ced-10
- CRIB domain-containing protein
- Actin-related protein 2
- Nucleosome assembly protein 1-like 1
- NCK adaptor protein family
- Ras-related protein rac-2
Sequence:
MAYKDARQVKIAEKLVILNDRAAGMMTRIYNIKKSSGDSKVKPQFLSDKKMEGAIKHIVRKFPVVDCRSNSSTFEYVQEKSTEITKSLSLYYYTFADILDLKDHIMQVLTTMESCQCQLDVTLNYDLTTSYLNLVVHLVTMMILLSRIEDRKAVLGLFNAAYDLQHGQSEASFPRLGQMILDYENPLKKLHEDLGPLNRLIYSALSSVTHTYQRRNKTADSWRTSNVFSLTAAPAQILYAAQTETIACEYLSLDVIDRWIVFCGTVCHSTLLNDDNIRHMWQLALQMNLCLRVFRDETFIVHQEIQAFLESSKEKSKRLQDVKDAFNHASVTAVAVHADRRRFLRSSLRELSLLLRDQPGLLGPKILYVWMALGAGRDEVIWLLRHQVEVPAISKKGSRMVEELVDRQLPELLFYMLELRDLVTKYYAVIQRYYLQYVSSYDSIVVSEEINQANGLTQEEAVLLTDFANEIGNINSDTDLRALRLDWFRFQAWTSAARSHFQLSRHKKLAIYMNTSVFHLKMIDLQDEMLRETSDLSLYCFYPKLAEKHWLNCLQLPAQARYVLSFARLAAHFTSALHDMCPEEKAFITEKALAQCNSVIEETCKQLSYILEKVAEHEFGLAYQMTPSAVAVRVVAQVVQQKGSGKAAAAAAAAARDYFIAGEESYRVDRQALTMPDKLQTTLLEISAALGAHRQIYVADHTFAPRTYLAQSLETKFVELLHGMFWEGQPHASNPKRPSEMLLALQAYMTVLQNLDTAISVDISNTMQTTLLQQTQLVDSKNKDTIAALYTKWYLEVLLRRASSGHMVWSEHLRTMLSSGQEQLSFMPDHYSDPQELRALVQIIGPYGVKLMTERLIWHVASQIMEMSKIVATYKDALQIARSNFDNAEKMKDVLNLLSVEPKDKKTPNATCAADAILQRTIIIGQICLFRDALHDALRHIVESKLPFLQASFDMLYHNLDDVDKVKIGEMSAAMGVTGPVDMSLVNAVRAQNPNIHPQEHYVNSCLLMVAVAICIPRIGMSDLSSYKPSIQASLNNSHCVPMAINTIGSALFHLHEQNDIQSRMKEFLALASSGILRTIHERDNSRQISDDVLRSHTTLYIILEQMVRKNRWLSMDVLETCFPYNLVRTAYQQCYEADAQ
Protein: Epididymis secretory sperm binding protein (A0A384MDV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFMLWDQQHKFPVFMGRVYDPRA
Protein: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) (E2K) (P36957)
Organism: Homo sapiens (Human)
Function: Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex. The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:29211711}. Nucleus {ECO:0000269|PubMed:29211711}. Note=Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. {ECO:0000269|PubMed:29211711}.
Interaction partners:
- 2-oxoadipate dehydrogenase complex component E1
- 2-oxoglutarate dehydrogenase complex component E1
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Sequence:
MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFFRTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
Protein: Wiskott-Aldrich syndrome protein family member (WASP family protein member) (A8JR42)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU367034}.
Interaction partners:
Sequence:
MPFVQRVVQPVNVAQATAASLGHASGRFHCTPGKCRNNNCINKQSPDVEVPNGHGSPTSLTRVLVHQAPEDQPVPPAPAPMKKLKHHVEFLSTSPTRHQSQSLPNSRHPSQQRPALGRIASAPQSPTAGSSKVVSGHEFDSISNITLSNALRQLASLVLIASDIFDDLQRDLQAVGERAGRVQRKIAAVERRVCAYDPKTVTVPESDLLTFAQRKHHFETDKSFQQELFTGETRPLSVRQLYTEAGKELPVATGATATALASLAHSQSLIPSRSISFNGEVLSSDHEVLQLNGSTDTEDHLLCVSDFGNANRKLRTRIDAEIEIRLPAAIEDLRKWTSSEALGDVTVTPDCMHHVDTSVSTSLAIGENGILTPALSPSVLSADAVDALYAQNLSQAADSSRHNHHTQALIPNDINKDVPLNHRLPSPEEQTKQIALKYPAEVISVNTSGKHFQRMCAARKSTSGGYAGGATAGSSSSTSPENAGQTEGNNLDDNVQTVSRRSRSRKVRGKRRNTIAGIDQKEIQDAANGNGESKNASNATSPVAPAQQAETTSSDAKKSKKFGRSKSSDILKKESAALPYDKGKSTLTRLNSLKQWGRNRFKFMHRTGELGDQLDTSGCSSQNSSAEKADSHHGSPAGDNSKRDIDDECVVHHLVAQKSESRFSHERKPSYSSSEKSISVSSSGQLRGRLQLSSGPMAAAHVKMRETATLNRQRRNGLHALAGKEEQPHSSSGNWSASSESGRASIGSEITMQPKSSASSTSLNVSSFQPGGAGSGPPSSMLSRRRFLNTSASSSVTSEGTATPELQAEAGAYPGHLDDETSSAYSCDTEGYYTSFHMDSGLRTLKEEEPSVMPGTPLQTSLHTSSYSFGSQSNQTVLNAESEYELFGRGSTSTTTSSAGTVCTALMSGAASGPDVPERSSSLGKHSGQSRSQSTSASSSTLERSYSSSTIGSTLERTGTIKRNVKMSPTKAGGEVTEKDDQQDQDQQQQLEFSESSDLEGVERIERIKQKTALTSKRIPSMCIITPTTSDDDEHQTNDPNRTLTSLTIDVEHGEQDEDEAEQKTPTNSKDHNLNELKQTPTKALSGMFEKLRVKLVPGKSSPAKNQMQPKPANSSAVNDDELYDLAGEYVTIADISNNNNNNKNIGRRNTGMGIYYSNDIVSKRVEPSTSAVSEYVSLNELPQHLRRHAVSSRSAPAAESESCAQQQLPVEPAAATSQPPPLPLGGRTQGVGDGVPMYAEIGELSEEKPLASAANRRLRPNAEGKLVYDSDSLKRRKGAHTTFAPGPYVKETESALHSAESAAAAIASSQDPSAASGAISSTKSAKLLLLTSGGLISGNRKVANVRPIVAKSPLSRNVSEMATYQATSYQDQKQLLANRTNPFYETIAAPVANLMMPSPSGKSNSSTGSTATSSSSSASGQSGEEGKPERLPSASSRPSACLPTTKSQSESLSLSASGFPVNNTATTETSAKSTLNHHIATKSAGSISSVREHQPQHPNQNPKDGESKVRVVEMETTTLGDAFEMGEQQGPPLPPRAKVNDKQHPTKPLSIDPIALHFSIAGNPGQPRTALKRNNSYRLANDELKLEMNKENLSVSFGSERAPSSGAMPLSSVHQQHATSSLRLRNLSNHLPTNTHSPGGERRIAKSFERLVDEFSLSLTTGNDSSYLKNKSLENFDDSPALLSVASPEQRPDKNASNSSDSESEDDEEELAPPLSQSLPAPKYHKSFVDSVLLRPFKIILPSDENGNRRQRILQKFEVTEIW
Protein: Aromatase (EC 1.14.14.14) (CYPXIX) (Cytochrome P-450AROM) (Cytochrome P450 19A1) (Estrogen synthase) (P28649)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P11511}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000250|UniProtKB:P11511}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- 17-beta-hydroxysteroid dehydrogenase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 17-beta-hydroxysteroid dehydrogenase type 3
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Estradiol 17-beta-dehydrogenase 2
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Very-long-chain 3-oxoacyl-CoA reductase
Sequence:
MFLEMLNPMQYNVTIMVPETVTVSAMPLLLIMGLLLLIWNCESSSSIPGPGYCLGIGPLISHGRFLWMGIGSACNYYNKMYGEFMRVWISGEETLIISKSSSMFHVMKHSHYISRFGSKRGLQCIGMHENGIIFNNNPSLWRTIRPFFMKALTGPGLVRMVEVCVESIKQHLDRLGEVTDTSGYVDVLTLMRHIMLDTSNMLFLGIPLDESAIVKKIQGYFNAWQALLIKPNIFFKISWLYRKYERSVKDLKDEIAVLVEKKRHKVSTAEKLEDCMDFATDLIFAERRGDLTKENVNQCILEMLIAAPDTMSVTLYFMLLLVAEYPEVEAAILKEIHTVVGDRDIKIEDIQNLKVVENFINESMRYQPVVDLVMRRALEDDVIDGYPVKKGTNIILNIGRMHRLEYFPKPNEFTLENFEKNVPYRYFQPFGFGPRGCAGKYIAMVMMKVVLVTLLRRFQVKTLQKRCIENIPKKNDLSLHPNEDRHLVEIIFSPRNSDKYLQQ
Protein: GTP-binding protein 8 (Q8N3Z3)
Organism: Homo sapiens (Human)
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- Mitochondrial assembly of ribosomal large subunit protein 1
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL17m
- rRNA methyltransferase 3, mitochondrial
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL29m
Sequence:
MAAPGLRLGAGRLFEMPAVLERLSRYNSTSQAFAEVLRLPKQQLRKLLYPLQEVERFLAPYGRQDLHLRIFDPSPEDIARADNIFTATERNRIDYVSSAVRIDHAPDLPRPEVCFIGRSNVGKSSLIKALFSLAPEVEVRVSKKPGHTKKMNFFKVGKHFTVVDMPGYGFRAPEDFVDMVETYLKERRNLKRTFLLVDSVVGIQKTDNIAIEMCEEFALPYVIVLTKIDKSSKGHLLKQVLQIQKFVNMKTQGCFPQLFPVSAVTFSGIHLLRCFIASVTGSLD
Protein: ALF transcription elongation factor 4 (A0A8I6GE44)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDYIGDRSIPKLVAIPKPAVPTTTDEKANPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRSSAGGSGASGSGQRHDRDSYSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLSSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSSQSFPPSLMSKSSSMLQKPTAYVRPMDGQESVEPKLSSEHYSSQSHGSNMTELKPSSKAHLTKLKIPSRPLDASVSGDVSCVDEILKESQQSNFGSGEQKRYSTSAKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQAYKKEGREQGTASNYTDPGGAKEASSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKTEKSAAEEPRGGLKIESETPVDMATSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSASKSSQKSREIIETDSSSSDSDERESLPPSSQTPKYPESNRTPVKPSSAEEDDSFFRQRMFSPMEEKELLSPLSDPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHSREVQKQASEKASNKGKRKHKNDDDNRASESKKPKTEDKNSSAHKPSSSKESSKQSSTKEKDLLPSPAGPVPSKDSKTEHGSRKRTVSQSSSLKSSSTSNKENSGSSKSTSSTAKQKKTEGKVSSSSKEAKEKAPNSSSNCPPSTPTPDSSKPRRTKLAFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSDTVELIKYTMKLKNYLAPDATAADKRLTVLCLRCQSLLYLRLFKLKKENALKYSKTLTEHLKNSYSNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGSYSSGGSSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLARYTRQGLHWLRQDAKLIS
Protein: Kinesin-like protein (A0A1D8PIH0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Kinesin-like protein
- Very long-chain fatty acid transport protein
- Dynein heavy chain, cytoplasmic
- Kinesin-like protein
- Tubulin beta chain
- Microtubule-binding protein
- ADP-ribosylation factor
- ADP-ribosylation factor
- Transcription regulator
- Kinesin-like protein
Sequence:
MSDENTKHKFLNVSQPSNLLGGSSSSNSLRRPLNDNTVSVSNKMRKTTSQIPVAKDTVPTLTISESNRLRQLVNEKKIDLEQLKLNATTLRNELEKQTYENFTIQSNYQNLERILNDLNLKIGELNSYKQSSLDALIKNFELNNHQLKMNHQEKLNNLKEDITKQVDKILTEKQHKYEVEISNLNKEINKIKSDRKNTESDLNRRLIQLKEDQHKQELMMVGRVNDDINNMKKEIADINSLLESKTKQIELIKSVEIEGASNKVDKFTLLLDQLTSKNKSKQEDIQALEKKVATTKESVKAIFEKSTARTSEVHRLQFEVGRMKTELVDQETKRRKLHAQLQDLKGNIRVFCRIRNVSSSSSSSSSSSSEDIIQYEAPQDINDESKQELVITRNINNNFSNLRFSFDKIFEREQSNDLVFEELSQLIQCSLDGTNVCVFAYGQTGSGKTFTMSHPTNGMIPLSLKKIFNDIEELKEKGWSYTVRGKFIEIYNEAIIDLLNPKIDPNTKYEIKHDDIAGKTTVTNVSTIDIKSPEQAITILNQANKKRSTAATKSNDHSSRSHSIFIIDLQGYNSLTKESSCGTLNLIDLAGSERLNNSRAEGDRLKETQAINKSLSCLGDVIHSLNLKDGSHVPYRNSKLTYLLKHSLGGNSKTLMFVNISPLTKDLNETINSLRFATKVNNTRINK