wanglab/gogpt-training-data huggingface dataset:
Protein: Period protein homolog lin-42 (Abnormal cell lineage protein 42) (Q65ZG8)
Organism: Caenorhabditis elegans
Function: Transcriptional repressor which interacts with the promoter region of target genes. Has a specific role in developmental timing where it regulates temporal expression of a number of miRNAs and mRNAs. Controls temporal cell fate transition during embryonic and early larval development by restricting the expression of specific miRNAs, including let-7, miR-48, lin-4, miR-35 and miR-58. Restricts the accumulation of lin-29 in the hypodermis to the larval L4 stage, thus controlling terminal differentiation of seam cells. Has a role in the miRNA-mediated specification of asymmetric gene expression patterns in gustatory neurons. May also regulate genes involved in other biological processes including transport, small molecule metabolism, and growth. Inhibits dauer formation, by antagonizing daf-12.
Subcellular location: Nucleus {ECO:0000269|PubMed:10550049, ECO:0000269|PubMed:16300753}. Cytoplasm {ECO:0000269|PubMed:10550049}. Note=Expression is generally more enriched in the nuclei than the cytoplasm (PubMed:10550049). Cytoplasmic expression is enhanced in lateral seam cells during the molt periods of larval development (PubMed:16300753). {ECO:0000269|PubMed:10550049, ECO:0000269|PubMed:16300753}.
Interaction partners:
- Protein timeless homolog
- Casein kinase I isoform delta
- Aryl hydrocarbon receptor nuclear translocator homolog
- Protein lin-41
- Nuclear hormone receptor family member daf-12
- Protein lin-14
- Protein lin-28
- Zinc finger transcription factor lin-29
- non-specific serine/threonine protein kinase
- Hunchback-like protein
Sequence:
MEPAGHSSATHNIVVPNANPTQPQPLAPAMREEGATLSPPNTWSSSSVEFLDDADDNRLLFTCTFTLPHGTVLSSATYADGFHEQYLTIGDNFLARLEPKGQSFILSAAAASVKQRIFARVTMPDGALRACELLCEFETDRAKITVLALRSAFSLQASHVSSNFHVFTFITKHSSTCALTHIDYASIPYLGLLPTDLIGKSLLAFVYSPDVHVVRQAHIDLHNSRGKIVKSIADLRLVAHNGSILRCQTEWSAYVNPWTRKMELVVARHRICSLPIGDSDVISSPPPGIQSNTLPPVMAKTFEDELRTIMNKPVPSTSRHSHHHHHSSLKDQNQGFPANIDLGAYIDKIVEQLVVNSTAQQQQKVAVAAAAAAQAAQAAVVATAQIRKVASAPPTTSTDPPLSYTQINCLENVHRLLKSQSRPESPAKQDEPFDEKKYPPQTPLTREALTLHTKRFEDEYKDTWCRRLKRLSDDVPSSPPAKRTTPIHWTSSSQNHYRTMAPAPPPPPGKNYQITYTPLDDLTDQKSTNTKSDVENVAYPISGSKFSTPMRLSIDGLLPRGATSTGGASPTSGTNSPPVFPKTSSSSSLLMLRDSQN
Protein: Ubiquitin-like modifier-activating enzyme 5 (UFM1-activating enzyme) (E7EQ61)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAESVERLQQRVQELERELAQERSLQVPRSGDGGGGRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELVSEVSEEELKNFSGPVPDLPEGITVAYTIPKK
Protein: Dual oxidase maturation factor 2 (Q9D311)
Organism: Mus musculus (Mouse)
Function: Required for the maturation and the transport from the endoplasmic reticulum to the plasma membrane of functional DUOX2. May play a role in thyroid hormone synthesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- Iodotyrosine deiodinase 1
- Pendrin
Sequence:
MTAWDGVLPFYPQPRHAASFSVPLLIVILVFLSLAASFLFILPGIRGHSRWFWLVRVLLSLFIGAEIVAVHFSGDWFVGRVWTNTSYKAFSPSRVQVHVGLHVGLAGVNITLRGTPRQQLNETIDYNERFTWRLNEDYTKEYVHALEKGLPDPVLYLAEKFTPSSPCGLYHQYHLAGHYAAATLWVAFCFWIIANALLSMPAPLYGGLALLTTGAFTLFGVFAFASISSVPLCHFRLGSAVLTPYYGASFWLTLATGILSLLLGGAVVILHYTRPSALRSFLDLSVKDCSNQAKGNSPLTLNNPQHEQLKSPDLNITTLL
Protein: Prenylated Rab acceptor protein 1 (PRA1 family protein 1) (O35394)
Organism: Rattus norvegicus (Rat)
Function: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10751420}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10751420}. Golgi apparatus {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:12107180}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:10707984}. Note=According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi (PubMed:10751420, PubMed:12107180, PubMed:11096102) and synaptic vesicles (PubMed:10707984). {ECO:0000269|PubMed:10707984, ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:12107180}.
Interaction partners:
- Plasminogen
- Protein YIF1
- Protein piccolo
Sequence:
MAAQKDQQKDAEVEGLSATTLLPKLIPSGAGREWLERRRATIRPWGTFVDQQRFSRPRNVGELCQRLVRNVEYYQSNYVFVFLGLILYCVVTSPMLLVALAVFFGACYILYLRTLQSKLVLFGREVSPAHQYALAGGVSFPFFWLAGAGSAVFWVLGATLVLIGSHAAFHQIEPADGEELQMEPV
Protein: Bruno 3, isoform E (Bruno 3, isoform P) (M9MRU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHIIELVGQPKVEFAQQVTMNRALQLKPAENESRSEHLDRKLFVGMLSKQQTEDDVRQIFHPFGTIEECTILRGPDGASKGCAFVKFGSQQEAQSAITNLHGSQTMPGASSSLVVKYADTEKERQIRRMQQMAGHMNLLNPFVFNQFSPYGAYAQQQQQAALMAAAATAPGSAAAYMNPMAALATQIPHGLNGTGQPPSLPSPTMPNFNMGANTPNGQPGGAAAAAAAAAAADGVFTNGIPQTAFPGHPLHLTIPPQGLPNGDAATLQHAFPGLPPFPGVAFPAVYGQFPQALPPPLAAVAPTQREDFLMFPGCSISGPEGCNLFIYHLPQEFGDAELMQMFLPFGNVISSKVFIDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDASRPY
Protein: IAA-amino acid hydrolase ILR1-like 5 (EC 3.5.1.-) (Q9SWX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Protein LONG AFTER FAR-RED 3
Sequence:
MSFCKLVSFVLILHLLNSCLISCSSNDLSQIPKNFLSLAKREDFFDWMVGIRRRIHENPELGYEEVETSKLVKTELDKMGVSYKNPVAVTGVIGYVGTGHAPFVALRADMDALPIQEMVEWEHKSKIPGKMHACGHDAHTTMLLGAAKLLKEHQEELQGTVILVFQPAEEGGAGAKKIVEAGVLENVGAIFGLHVSNLLGLGQLSSREGLLMAGSGRFKATISGKGGHAALPQFAIDPVLAASNVILSLQHLVSREADPLDSQVVTVATFEGSDAFNVIPDSVTIGGTFRALLPKSFEQLKQRIVQVITTQASVNMCNATVDFLEDETPPFPPTVNNKTLHLFYKNVSVDMLGIENYVETLPVMVSEDFAFYQQAIPGHFSFVGMQNKSHSPMANPHSPFFEVNEELLPYGASLLASLATRYLLDSSSSPNKDEL
Protein: Zinc finger MYND domain-containing protein 11 isoform X1 (Zinc finger, MYND-type-containing 11) (A0A2R8PVB4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRVVKKRQADPKVVQYVWSAIEVIRNQKQIANMDRISKYLSRVYGMHPKDTARQLVLAVKDGLVVETLTVGCKGSKAGIEQEGYWLPGDEMEQMSEGSKDWEAESHDWYCFECHLPGDVMECDGCFRVYHLRCVSEDHRPRDTTSHWQCGICRGSKRKNLNKQEMTTYLKFILGRMKERAVDLHKRGKEAKQPIYKRLIHTPLDVENIQENISDGKYKSFEEFRADAQLIVHNTAILHGVNSDQTEIARLLYNDTCHELNELMLCRTCFYLSNARPDNWFCYPCSPNHELVWARMKGFGYWPAKVMQREGNQVDVRFFGHQHQRAWIPSDNIQDITVSVQQLQVKRSSGWKKACDELELHQRFVREGRTWKGKPEEKNDRSERHERQEERQEEAESSISSTSNEQSRVNQEPKAKKSRRSQVAEPKEEEPEPEMEAVSSSQEIPTAVPHQPERMSVSTQTKKSSSPSSSSSPAPRMIHKGTQTVNEGNCQNMCHDKYSKIFSDVKEMMKAENKRETERVLKEALDKLRGEMEEEKRQAVNKAVSSTQAEMERKCKQVKEKCKEELMEEMKKMVSQHKQLLSQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHADHKRTCRRKR
Protein: Glycoprotein (P03522)
Organism: Vesicular stomatitis Indiana virus (strain San Juan) (VSIV)
Function: Attaches the virus to host LDL receptors, inducing clathrin-dependent endocytosis of the virion.
Subcellular location: Virion membrane {ECO:0000269|PubMed:1850035, ECO:0000269|PubMed:36216930, ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein {ECO:0000269|PubMed:8144707}. Host membrane {ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein {ECO:0000269|PubMed:8144707}.
Interaction partners:
Sequence:
MKCLLYLAFLFIGVNCKFTIVFPHNQKGNWKNVPSNYHYCPSSSDLNWHNDLIGTAIQVKMPKSHKAIQADGWMCHASKWVTTCDFRWYGPKYITQSIRSFTPSVEQCKESIEQTKQGTWLNPGFPPQSCGYATVTDAEAVIVQVTPHHVLVDEYTGEWVDSQFINGKCSNYICPTVHNSTTWHSDYKVKGLCDSNLISMDITFFSEDGELSSLGKEGTGFRSNYFAYETGGKACKMQYCKHWGVRLPSGVWFEMADKDLFAAARFPECPEGSSISAPSQTSVDVSLIQDVERILDYSLCQETWSKIRAGLPISPVDLSYLAPKNPGTGPAFTIINGTLKYFETRYIRVDIAAPILSRMVGMISGTTTERELWDDWAPYEDVEIGPNGVLRTSSGYKFPLYMIGHGMLDSDLHLSSKAQVFEHPHIQDAASQLPDDESLFFGDTGLSKNPIELVEGWFSSWKSSIASFFFIIGLIIGLFLVLRVGIHLCIKLKHTKKRQIYTDIEMNRLGK
Protein: LP06937p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9VE49)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Leucine-rich tendon-specific protein, isoform C
Sequence:
MKHKLLLLFLAGAALLLATEVRSQHEDIPYQPVSNICQTCLCLSTQDVDHRTHFNLDCSVRNFEHILARWPEQFGSQAIASGAASEIVVSYSGNRIKLLQQLPATNASLTLSCRHCGLQDLQAPLFMDVPNVQALYISWNDITDDALVPDLFRGPFRNTRYEPIGLRDLDLSHNRIVRLDRRLFEHTPHLTKLNLAYNKLSSLDEATTASIGSVATLQRLDLSHNGLMTLPAQLFSKLTSLRFLDVSGNEFSTMPASLQLLGKSLVQLNLAGNAFLSLKENSLQGLVSLKRLNISSMPSLRSLEKGALNLPALEHLDCSRNSKLERLELADLLSSRNLSQLDLSWNALTTLVINATGSSNNSSNSTNETWPRLRRMSISGNPWYCSCELFKALELIGLNHIDREWDGTEARCETPYLLAGSPLSNLTAERICKMVIPKKYREVDEEPPRFLRRHYIILTAIIASIVLVIGLVIGFVVVCVRRRLKGSDYGVQPIRYTSVRGSNLSQFSQLQPVSVASKFNNVHAGSSSGVTTGAANA
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (E7ETK5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03156}.
Interaction partners:
Sequence:
MADYLISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMAKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
Protein: Protein tweety homolog 2 (hTTY2) (Volume-regulated anion channel subunit TTYH2) (Q9BSA4)
Organism: Homo sapiens (Human)
Function: Probable large-conductance Ca(2+)-activated chloride channel. May play a role in Ca(2+) signal transduction. May be involved in cell proliferation and cell aggregation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18260827, ECO:0000269|PubMed:18577513, ECO:0000269|PubMed:34385445}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MQAARVDYIAPWWVVWLHSVPHVGLRLQPVNSTFSPGDESYQESLLFLGLVAAVCLGLNLIFLVAYLVCACHCRRDDAVQTKQHHSCCITWTAVVAGLICCAAVGVGFYGNSETNDGAYQLMYSLDDANHTFSGIDALVSGTTQKMKVDLEQHLARLSEIFAARGDYLQTLKFIQQMAGSVVVQLSGLPVWREVTMELTKLSDQTGYVEYYRWLSYLLLFILDLVICLIACLGLAKRSKCLLASMLCCGALSLLLSWASLAADGSAAVATSDFCVAPDTFILNVTEGQISTEVTRYYLYCSQSGSSPFQQTLTTFQRALTTMQIQVAGLLQFAVPLFSTAEEDLLAIQLLLNSSESSLHQLTAMVDCRGLHKDYLDALAGICYDGLQGLLYLGLFSFLAALAFSTMICAGPRAWKHFTTRNRDYDDIDDDDPFNPQAWRMAAHSPPRGQLHSFCSYSSGLGSQTSLQPPAQTISNAPVSEYMNQAMLFGRNPRYENVPLIGRASPPPTYSPSMRATYLSVADEHLRHYGNQFPA
Protein: At1g49510 (Embryo defective 1273) (F13F21.5 protein) (Q9XIB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAMSHLFLSSSPQSSLALRLHSTTQFTLSYSKNNKDCSFQSANEAKVSKRSLLCRAIHMESGHSGEQPKKLNFDNLLRRTKHVWDNSPQPVKEFPWNRAFGNFIQLVLDLAISVVKFLFVPILAVSSISEMSYCAHERKLALVPFPLVIGMVVAGVLQETALKISPRLKEAEVPWHLIAMMMFFTLIKLPGPYYPYWGRLLVPHFANGVLLRALWSMFFWYKKTRNTSGNPLQNHSLETE
Protein: Osmotin-like protein I (Protein P21-like) (Q2HPG3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Pathogenesis-related protein PR-4A-like
- Pathogenesis-related protein PR-4A-like
- Pathogenesis-related protein PR-4A-like
- Endochitinase 1
Sequence:
MSYLTISQISSLLFFSVLFISAHAARFEIRNECSYTVWAAASPGGGRRLDPRQSWTIDVPAGTAMARIWGRTNCNFDASGRGHCQTGDCGGLLQCKGWGVPPNTLAEYALNQFGNMDFYDISLVDGFNIPMVFGPTNGGCHNIRCTADINGQCPNELRAPGGCNNPCTVFKTNEYCCTQGYGTCGPTRYSRFFKDRCRDSYSYPQDDPSSTFTCPAGSNYRVVFCPRGSPHIEMVGSKSQEK
Protein: Autophagy related 16 like 2 (H0YF72)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
AGRSRASPVSGREGGSSRPLEEGTGSSPACVRGAAPGSQDAFYPTRAKQARVSQELKKAAKRTVSISEGPDTLGDGMRERRETLALAPEPEPLEKEACEKWKRPFRSASATSLTLSHCVDVVKGLLDFKKRRGHSIGGAPEQRYQIIPVCVAARLPTRAQDVLDAHLSEVNAVRFGPNSSLLATGGADRLIHLWNVVGSRLEANQTLEGAGGSITSVDFDPSGYQVLAATYNQAAQLWKVGEAQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVCGDHIIISGHNDQKIRFWDSRGPHCTQVIPVQGRVTSLSLSHDQLHLLSCSRDNTLKVIDLRVSNIRQVFRADGFKCGSDWTKAVFSPDRSYALAGSCDGALYIWDVDTGKLESRLQGPHCAAVNAVAWCYSGSHMVSVDQGRKVVLWQ
Protein: Immediate early response gene 2 protein (B7SXM5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA-binding protein that seems to act as a transcription factor (By similarity). Mediates with FIBPB FGF-signaling in Kupffer's vesicle ciliogenesis and in the establishment of laterality in the embryo.
Subcellular location: Nucleus {ECO:0000269|PubMed:19164561}. Cytoplasm {ECO:0000250|UniProtKB:Q9BTL4}.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 16
Sequence:
MDVTAEAKQIMVQALGKMYSSRSQRGGLRLHRSLLLTLVMKSARDIYHSARLMSEKSGQSVTEECTSHTQEPMDTSSSTATPLRETSGQSSEDGQRSGLEGHPHPLNPAADKENCGPSRPDRHSRKRRSKTATDSDFIPCKKAKLECAEVRGVLQNSSANCGRALDSLSLVPMPRTIVTF
Protein: Melanin-concentrating hormone receptor 1 (MCH receptor 1) (MCH-R1) (MCHR-1) (G-protein coupled receptor 24) (MCH-1R) (MCH1R) (MCHR) (SLC-1) (Somatostatin receptor-like protein) (Q99705)
Organism: Homo sapiens (Human)
Function: Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10421367, ECO:0000305|PubMed:15340116}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-MCH
- Melanin-concentrating hormone receptor 2
- BBSome complex member BBS1
- BBSome complex member BBS2
- BBSome complex member BBS4
- Pro-opiomelanocortin
- BBSome complex member BBS7
- Pro-neuropeptide Y
- Somatostatin receptor type 3
- BBSome complex member BBS5
Sequence:
MDLEASLLPTGPNASNTSDGPDNLTSAGSPPRTGSISYINIIMPSVFGTICLLGIIGNSTVIFAVVKKSKLHWCNNVPDIFIINLSVVDLLFLLGMPFMIHQLMGNGVWHFGETMCTLITAMDANSQFTSTYILTAMAIDRYLATVHPISSTKFRKPSVATLVICLLWALSFISITPVWLYARLIPFPGGAVGCGIRLPNPDTDLYWFTLYQFFLAFALPFVVITAAYVRILQRMTSSVAPASQRSIRLRTKRVTRTAIAICLVFFVCWAPYYVLQLTQLSISRPTLTFVYLYNAAISLGYANSCLNPFVYIVLCETFRKRLVLSVKPAAQGQLRAVSNAQTADEERTESKGT
Protein: Calmin (Calponin-like transmembrane domain protein) (Q8C5W0)
Organism: Mus musculus (Mouse)
Subcellular location: [Isoform 1]: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 4]: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Shows a reticular pattern in the cytoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
Sequence:
MAAQEWDWFQREELIGQISDIRVQNLQVERENVQKRTFTRWINLHLEKCDPPLEVTDLFVDIQDGKILMALLEVLSGRNLLHEYKSSSHRIFRLNNIAKALKFLEDSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKELTGNLSRSSPSSSLSPGSGGTDSDSSYPPTPTTERSVAVAVKDQRKAIKTLLSWVQRKTRKYGVAVQDFAGSWRSGLAFLAVIKAIDPSLVDMKQALEDSTRDNLEKAFSIAHDSLHIPRLLEPEDIMVDMPDEQSIVTYVAQFLERFPELEPEDFVNPDKEAPIESTFVRIKESPSEQGSRVLLLSENGERAYTVNQETSYPPPDKVFVCDQLESPTGFCLDSAPSHKLSDSSTEFMHEIIDQVLQGSTGKTGSIAEPTPESSILSTRKDGRRSNSLPVKKTVHFEADLHKDASCSKDPFYSSDFRFEGSPKATKELSKQDGHVSLAEVSKEKKKSEQEARLVLEAASDKVPESTVDGLDAVPQDAQPSQDSSFCNGTVESPSSQGEKGPPPSSPGDHTLLANSTELKVQLLTVEPMDKEDYFECIPLKASKFNRDLVDFASTSQAFGEDPSSHEKTRGEEEGSENHAEKPGKRKSKSPRAETEAAESRLEPKKLEPPPKDPEQEDQGHALPPETPADKKPKVYEKAKRKSTRHHSEEEGEAESGFSAVCEEEIPSAPPSTSVSLETLRSHSEEGLDFKPSPPLSKISVIPHDLFYYPHYEVPLAAVLEAYAEGGEDLKSEDTDLEHPEDSYLQDSREEEADEDEEEAQSSQSSCSFSLPVDNSYPSVSEHVSHVDGSSEGPTSALGPGSPPSHEDHQPKETKENGPVESQQSQEPPNPELPTKPLEEKLTEASTSSKKKEKRKHMDHVESSLFIAPGTVRSSDDLEENSSEHKVPSRNSHSDSSIYIRRHTNRSLELDHFSYVQLRNAADLDDRRNRVLNRYNSQKLTELILQFYGIRADMKREYKHARLSMTGTNSSGEAVPLGNQSPPNDSLTQFVQQPDVIYFILFLWLLVYCLLLFPQLDVSRL
Protein: 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC 2.3.1.174) (EC 2.3.1.223) (P0C7L2)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA.
Interaction partners:
- 3-hydroxyadipyl-CoA dehydrogenase
- 2,3-dehydroadipyl-CoA hydratase
- 1,2-epoxyphenylacetyl-CoA isomerase
- Bifunctional protein PaaZ
- Phenylacetate-coenzyme A ligase
- 1,2-phenylacetyl-CoA epoxidase, subunit B
- 1,2-phenylacetyl-CoA epoxidase, subunit C
- 1,2-phenylacetyl-CoA epoxidase, subunit A
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
Sequence:
MREAFICDGIRTPIGRYGGALSSVRADDLAAIPLRELLVRNPRLDAECIDDVILGCANQAGEDNRNVARMATLLAGLPQSVSGTTINRLCGSGLDALGFAARAIKAGDGDLLIAGGVESMSRAPFVMGKAASAFSRQAEMFDTTIGWRFVNPLMAQQFGTDSMPETAENVAELLKISREDQDSFALRSQQRTAKAQSSGILAEEIVPVVLKNKKGVVTEIQHDEHLRPETTLEQLRGLKAPFRANGVITAGNASGVNDGAAALIIASEQMAAAQGLTPRARIVAMATAGVEPRLMGLGPVPATRRVLERAGLSIHDMDVIELNEAFAAQALGVLRELGLPDDAPHVNPNGGAIALGHPLGMSGARLALAASHELHRRNGRYALCTMCIGVGQGIAMILERV
Protein: N-alpha-acetyltransferase 11 (EC 2.3.1.255) (N-terminal acetyltransferase complex ARD1 subunit homolog B) (hARD2) (NatA catalytic subunit Naa11) (Q9BSU3)
Organism: Homo sapiens (Human)
Function: Displays alpha (N-terminal) acetyltransferase activity. Proposed alternative catalytic subunit of the N-terminal acetyltransferase A (NatA) complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16638120}. Nucleus {ECO:0000269|PubMed:16638120}.
Interaction partners:
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- N-alpha-acetyltransferase 60
- Huntingtin-interacting protein K
Sequence:
MNIRNAQPDDLMNMQHCNLLCLPENYQMKYYLYHGLSWPQLSYIAEDEDGKIVGYVLAKMEEEPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRPALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLSQMADELRRQMDLKKGGYVVLGSRENQETQGSTLSDSEEACQQKNPATEESGSDSKEPKESVESTNVQDSSESSDSTS
Protein: Negative elongation factor B (NELF-B) (Cofactor of BRCA1) (Q8WX92)
Organism: Homo sapiens (Human)
Function: Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. May be able to induce chromatin unfolding. Essential for early embryogenesis; plays an important role in maintaining the undifferentiated state of embryonic stem cells (ESCs) by preventing unscheduled expression of developmental genes (By similarity). Plays a key role in establishing the responsiveness of stem cells to developmental cues; facilitates plasticity and cell fate commitment in ESCs by establishing the appropriate expression level of signaling molecules (By similarity). Supports the transcription of genes involved in energy metabolism in cardiomyocytes; facilitates the association of transcription initiation factors with the promoters of the metabolism-related genes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11739404}.
Interaction partners:
- Negative elongation factor E
- Negative elongation factor A
- Transcription elongation factor SPT5
- Negative elongation factor C/D
- Transcription elongation factor SPT4
- Nuclear cap-binding protein subunit 1
- Cyclin-dependent kinase 9
- RNA polymerase-associated protein CTR9 homolog
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MFAGLQDLGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGEVVQRLTRMVGKNVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMSLHDLDVGEICTVDPCHKFTWCLDACIRERFVDSKRARELQGFLDGVKKGQEQVLGDLSMILCDPFAINTLALSTVRHLQELVGQETLPRDSPDLLLLLRLLALGQGAWDMIDSQVFKEPKMEVELITRFLPMLMSFLVDDYTFNVDQKLPAEEKAPVSYPNTLPESFTKFLQEQRMACEVGLYYVLHITKQRNKNALLRLLPGLVETFGDLAFGDIFLHLLTGNLALLADEFALEDFCSSLFDGFFLTASPRKENVHRHALRLLIHLHPRVAPSKLEALQKALEPTGQSGEAVKELYSQLGEKLEQLDHRKPSPAQAAETPALELPLPSVPAPAPL
Protein: Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) (P41764)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis (By similarity).
Interaction partners:
- 6-phosphogluconolactonase
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconate dehydrogenase, decarboxylating
- Phosphoglucomutase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate kinase
- Glucosamine-6-phosphate isomerase
Sequence:
MSATIARAEEQQNGSTVELKDDTVIVVLGASGDLAKKKTFPALFGLFRNKFLPKGIKIVGYARTQMDHNEYLKRVRSYIKTPTKEIEEQLNSFCELCTYISGQYDQDDSFKNLAKHLEEIEKNQKEQNRVFYMALPPSVFITVSEQLKRNCYPKNGVARIIVEKPFGKDLQSSRDLQKALEPNWKEEEIFRIDHYLGKEMVKNILIMRFGNEFFNATWNRHHIDNVQITFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQVLTLLAMERPISFSAEDIRDEKVRVLRAMDPIQPKDVIIGQYGRSLDGSKPAYKEDDTVPQDSRCPTFCALVAHIKNERWDGVPFIMKAGKALNEQKTEIRIQFKDVTSGIFKDIPRNELVIRVQPNESVYIKMNSKLPGLSMQTVVTELDLTYRRRFSDLKIPEAYESLILDALKGDHSNFVRDDELDASWRMFTPLLHYLDDNKEIIPMEYPYGSRGPSVLDDFTASYGYKFSDAAGYQWPLTHTTPNRL
Protein: Ap3d1 protein (Q5RK16)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
DKKKAKRKQVVQLENGAPAEEEEEEEEPIPPMSSYCLLAENPYIKVTYDVQASLQKDSQVTVSIILENQSSSFLKNMELNVLDSLNTKMARPEGSSVHDGVPVPFQLPPGVSNEAQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISISFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLSQC
Protein: Creatine kinase B-type (EC 2.7.3.2) (Brain creatine kinase) (B-CK) (Creatine kinase B chain) (Creatine phosphokinase B-type) (CPK-B) (P12277)
Organism: Homo sapiens (Human)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04447}. Mitochondrion {ECO:0000250|UniProtKB:Q04447}. Cell membrane {ECO:0000269|PubMed:18566107}. Note=Localizes to the mitochondria of thermogenic fat cells via the internal MTS-like signal (iMTS-L) region. {ECO:0000250|UniProtKB:Q04447}.
Interaction partners:
- Ankyrin repeat and SOCS box protein 9
- Creatine kinase M-type
- Guanidinoacetate N-methyltransferase
- Sodium- and chloride-dependent creatine transporter 1
- Elongin-B
- Calmodulin-1
- Elongin-C
- Alpha-enolase
- L-lactate dehydrogenase A-like 6B
- L-lactate dehydrogenase A-like 6A
Sequence:
MPFSNSHNALKLRFPAEDEFPDLSAHNNHMAKVLTPELYAELRAKSTPSGFTLDDVIQTGVDNPGHPYIMTVGCVAGDEESYEVFKDLFDPIIEDRHGGYKPSDEHKTDLNPDNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLAVEALSSLDGDLAGRYYALKSMTEAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWVNEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKDYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFSEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEQRLEQGQAIDDLMPAQK