wanglab/gogpt-training-data huggingface dataset:
Protein: ESX conserved component EccC2. ESX-2 type VII secretion system protein. Possible membrane protein (O05450)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- ESX-5 secretion system protein EccD5
- ESX-5 secretion system ATPase EccB5
- ESX-2 secretion system ATPase EccB2
- ESX-4 secretion system protein eccD4
- ESX-3 secretion system ATPase EccB3
- ESX-3 secretion system protein EccD3
- ESX-2 secretion system protein eccD2
- Transglycosylase
- Putative 3-methyladenine DNA glycosylase
- ESAT-6-like protein EsxU
Sequence:
MSKKAFPINRVNIDPPKPVRVAPNPPIALPEREPRNIWVMIGVPALIVALIGTIVMLYVSGVRSLATGFFPLMGIGAFSMLAFSGRFGRARKITWGELEKGRRRYLRDLDTNRDEIQTAVCAQREWQNAVHSDPPGLGAIIGGPRMWERGRGDVDFLEVRVGTGVQHAPDSVLSVTWPDISSDEELEPVTGQALRDFILEQRKIRDIAKVVNLRSAPGFSFVSEDLDRVRSLMRSVLCSLAVFHNPRDVKLMVVTRNREVWAWMVWLPHNLHDELFDACGWRRLIFATPEELEAALGAELHMKGKRGAWTPPTVASPTAMGSALETGQVGVDLGPHLVIVDDNTGSPDAWESVVGQVGKAGLTVLRIASRVGTGVGFAEDQVFEMAQRHGAATAVKAGRDGADADDDQRPAPLLRARGTFFAHADQLSIHRAYRYARAMARWSPTSRSEVTDSTSGAAELLRSLGISDPRELDVDRLWAERRGRGDDRWCEIPVGAKPNGELQNIILRAKDFGGFGFHSVVIGTSGSGKSELFLSLVYGIALTHSPETFNVIFVDMKFESAAQDILGIPHVVAALSNLGKDERHLAERMRRVIDGEIKQRYELFKSVGARDANDYEEIRLAGRDLPPVPVLLVIVDEYLELFANHKKWIDLIIHIGQEGRGANVFFMLGGQRLDLSSLQKVKSNIAFRIALRAESGDDSREVIGSDAAYHLPSKENGFALLKVGPRDLEPFRCFYLSAPFVVPKKKEVARTIDMTLTQPRLYDWQYQPLDAADAEALATAAAADAEPDEFLYYDDGFKKKKIVDVLRESLYNVPHRSPRRPWLAPLEDPEPVDRLVAAYRGKPWHVDYGQNPGLMFPVGVMDIPEESQQVVHAVDALRSNIIVVGAKQRGKTTTLMALMCSAATMYTPERVTFFCIGGATMAQIGSLPHVTDIVSPKDAEGIERILSTMDALIDAREEAFRRAKIDMDGFRERRFGIGGDGVGGTDPTDAFGDVFVVLDDYDDLYAKDTLLGDRIISLSSRGPEYGVHLMCSAGGWIHGQRQSLLQNVTARIQLRLADPGESQMGHLSIESREAARRTLNRPGFGLTESLHELRIGVPALADPGTGELVGITDVGARIADVAGVTKHASLQRLPQRVELSAIVEHEAVHQGGDDLSIAFAIGERHELGPVPIKLRESPGLMILGRQGCGKTTALVAIGEAVMNRFSPQQAQLTLIDPKTAPHGLRDLHAPGYVRAYAYDQDEIDEVITELAQQILLPRLPPKGLSQEELRALKPWEGPRHFVLIDDVQDLRPAQSYPQKPPVGAALWKLMERARQVGLHVFSTRNSANWATMPMDPWVKSQTSAKVAQLYMDNDPQNRINRSVRAQTLPPGRGLLVGADGDVEGILVGYPSVPGEQ
Protein: Left-right determination factor 1 (Left-right determination factor B) (Protein lefty-1) (Protein lefty-B) (O75610)
Organism: Homo sapiens (Human)
Function: Required for left-right axis determination as a regulator of LEFTY2 and NODAL.
Subcellular location: Secreted.
Interaction partners:
- Nodal homolog
- Left-right determination factor 2
- Activin receptor type-2B
- Transforming growth factor beta-1 proprotein
- Transforming growth factor beta-3 proprotein
- Protein Cripto
- Pituitary homeobox 2
- Cryptic protein
- Zinc finger protein ZIC 3
- Activin receptor type-2A
Sequence:
MQPLWLCWALWVLPLASPGAALTGEQLLGSLLRQLQLKEVPTLDRADMEELVIPTHVRAQYVALLQRSHGDRSRGKRFSQSFREVAGRFLALEASTHLLVFGMEQRLPPNSELVQAVLRLFQEPVPKAALHRHGRLSPRSARARVTVEWLRVRDDGSNRTSLIDSRLVSVHESGWKAFDVTEAVNFWQQLSRPRQPLLLQVSVQREHLGPLASGAHKLVRFASQGAPAGLGEPQLELHTLDLGDYGAQGDCDPEAPMTEGTRCCRQEMYIDLQGMKWAENWVLEPPGFLAYECVGTCRQPPEALAFKWPFLGPRQCIASETDSLPMIVSIKEGGRTRPQVVSLPNMRVQKCSCASDGALVPRRLQP
Protein: Eukaryotic translation initiation factor 4B (Q5RKG9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Eukaryotic translation initiation factor 4E
- RNA helicase
- Eukaryotic initiation factor 4A-II
- Polyadenylate-binding protein 1
- Ribosomal protein S6 kinase beta-1
- Eukaryotic translation initiation factor 4 gamma 1
- Small ribosomal subunit protein eS6
- Eukaryotic translation initiation factor 4H
- Eukaryotic translation initiation factor 5
- Ribosomal protein S6 kinase
Sequence:
MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVPKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEDSIKDFFRGLNISAVRLPREPSNPDRLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDRSFGRDRNRDSDKTDTDWRARPATDSFDDYPPRRGDDSFGDKYRDRYESDRYRDGYRDGYRDGPRRDMDRYGGRDRYDDRGSRDYDRGYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDYRRDDRGPPQRPKLNLKPRSTPKEDDSSASTSQSSRAASIFGGAKPVDTAAREREVEERLQKEQEKLQRQLDEPKLDRRPRERHPSWRSEETQERERSRTGSESSQTGTSATSGRNTRRRESEKSLENETLNKEEDCHSPTSKPPKPDQPLKVMPAPPPKENAWVKRSSNPPARSQSSDTEQPSPTSGGGKVAPAQPSEEGPSRKDETKVDGVSTTKGQTGHSSRGPGDGGSRDHWKELDRKDGKKDQDSRSAPEPKKSEENRASKFSSASKYAALSVDGEDEDEGDDCTE
Protein: Zinc finger protein 609 (O15014)
Organism: Homo sapiens (Human)
Function: Transcription factor, which activates RAG1, and possibly RAG2, transcription. Through the regulation of RAG1/2 expression, may regulate thymocyte maturation. Along with NIPBL and the multiprotein complex Integrator, promotes cortical neuron migration during brain development by regulating the transcription of crucial genes in this process. Preferentially binds promoters containing paused RNA polymerase II. Up-regulates the expression of SEMA3A, NRP1, PLXND1 and GABBR2 genes, among others.
Subcellular location: Nucleus {ECO:0000269|PubMed:28344082}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:28344082}.
Interaction partners:
- E3 ubiquitin-protein ligase SHPRH
- Eukaryotic translation initiation factor 4 gamma 2
Sequence:
MSLSSGASGGKGVDANPVETYDSGDEWDIGVGNLIIDLDADLEKDQQKLEMSGSKEVGIPAPNAVATLPDNIKFVTPVPGPQGKEGKSKSKRSKSGKDTSKPTPGTSLFTPSEGAASKKEVQGRSGDGANAGGLVAAIAPKGSEKAAKASRSVAGSKKEKENSSSKSKKERSEGVGTCSEKDPGVLQPVPLGGRGGQYDGSAGVDTGAVEPLGSIAIEPGAALNPLGTKPEPEEGENECRLLKKVKSEKMESPVSTPAVLPIHLLVPVVNNDISSPCEQIMVRTRSVGVNTCDVALATEPECLGPCEPGTSVNLEGIVWQETEDGMLVVNVTWRNKTYVGTLLDCTRHDWAPPRFCDSPTSDLEMRNGRGRGKRMRPNSNTPVNETATASDSKGTSNSSKTRAGANSKGRRGSQNSSEHRPPASSTSEDVKASPSSANKRKNKPLSDMELNSSSEDSKGSKRVRTNSMGSATGPLPGTKVEPTVLDRNCPSPVLIDCPHPNCNKKYKHINGLKYHQAHAHTDDDSKPEADGDSEYGEEPILHADLGSCNGASVSQKGSLSPARSATPKVRLVEPHSPSPSSKFSTKGLCKKKLSGEGDTDLGALSNDGSDDGPSVMDETSNDAFDSLERKCMEKEKCKKPSSLKPEKIPSKSLKSARPIAPAIPPQQIYTFQTATFTAASPGSSSGLTATVAQAMPNSPQLKPIQPKPTVMGEPFTVNPALTPAKDKKKKDKKKKESSKELESPLTPGKVCRAEEGKSPFRESSGDGMKMEGLLNGSSDPHQSRLASIKAEADKIYSFTDNAPSPSIGGSSRLENTTPTQPLTPLHVVTQNGAEASSVKTNSPAYSDISDAGEDGEGKVDSVKSKDAEQLVKEGAKKTLFPPQPQSKDSPYYQGFESYYSPSYAQSSPGALNPSSQAGVESQALKTKRDEEPESIEGKVKNDICEEKKPELSSSSQQPSVIQQRPNMYMQSLYYNQYAYVPPYGYSDQSYHTHLLSTNTAYRQQYEEQQKRQSLEQQQRGVDKKAEMGLKEREAALKEEWKQKPSIPPTLTKAPSLTDLVKSGPGKAKEPGADPAKSVIIPKLDDSSKLPGQAPEGLKVKLSDASHLSKEASEAKTGAECGRQAEMDPILWYRQEAEPRMWTYVYPAKYSDIKSEDERWKEERDRKLKEERSRSKDSVPKEDGKESTSSDCKLPTSEESRLGSKEPRPSVHVPVSSPLTQHQSYIPYMHGYSYSQSYDPNHPSYRSMPAVMMQNYPGSYLPSSYSFSPYGSKVSGGEDADKARASPSVTCKSSSESKALDILQQHASHYKSKSPTISDKTSQERDRGGCGVVGGGGSCSSVGGASGGERSVDRPRTSPSQRLMSTHHHHHHLGYSLLPAQYNLPYAAGLSSTAIVASQQGSTPSLYPPPRR
Protein: Oxalate--CoA ligase (EC 6.2.1.8) (Acyl-activating enzyme 3) (Oxalyl-CoA synthetase) (Peroxisomal-coenzyme A synthetase) (P38137)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the first step in a degradation pathway of oxalate to CO(2) to protect the cell against the harmful effects of oxalate derived from endogenous processes or an environmental sources.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:8841414}. Peroxisome membrane {ECO:0000269|PubMed:8841414}; Peripheral membrane protein {ECO:0000269|PubMed:8841414}. Note=Imported in peroxisome via recognition by the peroxisomal targeting signal receptor PEX5. {ECO:0000269|PubMed:26359497}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 7
- Acyl carrier protein, mitochondrial
- Mediator of RNA polymerase II transcription subunit 31
- RQC trigger complex subunit RQT4
- 2-hydroxyacyl-CoA lyase
- Peroxisomal targeting signal receptor
- Long-chain-fatty-acid--CoA ligase 2
Sequence:
MTSAATVTASFNDTFSVSDNVAVIVPETDTQVTYRDLSHMVGHFQTMFTNPNSPLYGAVFRQDTVAISMRNGLEFIVAFLGATMDAKIGAPLNPNYKEKEFNFYLNDLKSKAICVPKGTTKLQSSEILKSASTFGCFIVELAFDATRFRVEYDIYSPEDNYKRVIYRSLNNAKFVNTNPVKFPGFARSSDVALILHTSGTTSTPKTVPLLHLNIVRSTLNIANTYKLTPLDRSYVVMPLFHVHGLIGVLLSTFRTQGSVVVPDGFHPKLFWDQFVKYNCNWFSCVPTISMIMLNMPKPNPFPHIRFIRSCSSALAPATFHKLEKEFNAPVLEAYAMTEASHQMTSNNLPPGKRKPGTVGQPQGVTVVILDDNDNVLPPGKVGEVSIRGENVTLGYANNPKANKENFTKRENYFRTGDQGYFDPEGFLVLTGRIKELINRGGEKISPIELDGIMLSHPKIDEAVAFGVPDDMYGQVVQAAIVLKKGEKMTYEELVNFLKKHLASFKIPTKVYFVDKLPKTATGKIQRRVIAETFAKSSRNKSKL
Protein: Secreted aspartic protease 5 (ACP 5) (Aspartate protease 5) (EC 3.4.23.24) (Candidapepsin-5) (P43094)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000269|PubMed:18384081}.
Interaction partners:
- Hyphal wall protein 1
- Agglutinin-like protein 3
- Agglutinin-like protein 1
- Secreted aspartic protease 4
- Extent of cell elongation protein 1
Sequence:
MFLKNILSVLAFALLIDAAPVKRSPGFVTLDFNVKRSLVDPDDPTVEAKRSPLFLEFTPSEFPVDETGRDGDVDKRGPVAVTLHNEAITYTADITVGSDNQKLNVIVDTGSSDLWIPDSNVICIPKWRGDKGDFCKSAGSYSPASSRTSQNLNTRFDIKYGDGSYAKGKLYKDTVGIGGVSVRDQLFANVWSTSARKGILGIGFQSGEATEFDYDNLPISLRNQGIIGKAAYSLYLNSAEASTGQIIFGGIDKAKYSGSLVDLPITSEKKLTVGLRSVNVRGRNVDANTNVLLDSGTTISYFTRSIVRNILYAIGAQMKFDSAGNKVYVADCKTSGTIDFQFGNNLKISVPVSEFLFQTYYTSGKPFPKCEVRIRESEDNILGDNFLRSAYVVYNLDDKKISMAPVKYTSESDIVAIN
Protein: KAT8 regulatory NSL complex subunit 2 (NSL complex protein NSL2) (Non-specific lethal 2 homolog) (Q8BQR4)
Organism: Mus musculus (Mouse)
Function: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9H9L4}. Mitochondrion {ECO:0000269|PubMed:37813994}.
Interaction partners:
- KAT8 regulatory NSL complex subunit 3
- PHD finger protein 20
- Microspherule protein 1
- KAT8 regulatory NSL complex subunit 1
- WD repeat-containing protein 5
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Host cell factor 1
- Histone acetyltransferase KAT8
- KAT8 regulatory NSL complex subunit 1-like protein
- Male-specific lethal 1 homolog
Sequence:
MNRIRIHVLPTNRGRITPVPRSQEPLSCSFTHRPCSQPRLEGQEFCIKHILEDKNAPFKQCSYVSTKNGKRCPSAAPKPEKKDGVSFCAEHARRNALALHAQMKKSNPGPMGETLLCQLSSYAKTELGSQTPESSRSEASRILDEDSWSDGDQEPITVDQTWRGDPDSEADSIDSDQEDPLKHAGVYTAEEVALIMREKLIRLQSLYIDQFKRLQHLLKEKKRRYLHNRKVEHEALGSSLLTGPEGLLAKERENLKRLKCLRRYRQRYGVEALLHRQLKERRMLATDGAAQQAHTTRSSQRCLAFVDDVRCSNQSLPMTRHCLTHICQDTNQVLFKCCQGSEEVPCNKPVPVSLSEDPCCPLHFQLPPQMYKPEQVLSVPDDLEAGPMDLYLSAAELQPTESLPLEFSDDLDVVGDGMPCPPSPLLFDPSLTLEDHSVTESAGDAGQMQAAGDGCRSQGARSVEKAAFPQRGLATANGKPEPTSIS
Protein: C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain 1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1) (Q9UQF2)
Organism: Homo sapiens (Human)
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus {ECO:0000250}. Endoplasmic reticulum membrane. Mitochondrion membrane. Note=Accumulates in cell surface projections. Under certain stress conditions, translocates to the perinuclear region of neurons. In insulin-secreting cells, detected in both the cytoplasm and nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase 8
- Dual specificity mitogen-activated protein kinase kinase 7
- C-Jun-amino-terminal kinase-interacting protein 2
- Mitogen-activated protein kinase 9
- Transcription factor Jun
- Mitogen-activated protein kinase kinase kinase 11
- Kinesin light chain 1
- Amyloid-beta precursor protein
- Kinesin light chain 2
- Mitogen-activated protein kinase kinase kinase 13
Sequence:
MAERESGGLGGGAASPPAASPFLGLHIASPPNFRLTHDISLEEFEDEDLSEITDECGISLQCKDTLSLRPPRAGLLSAGGGGAGSRLQAEMLQMDLIDATGDTPGAEDDEEDDDEERAARRPGAGPPKAESGQEPASRGQGQSQGQSQGPGSGDTYRPKRPTTLNLFPQVPRSQDTLNNNSLGKKHSWQDRVSRSSSPLKTGEQTPPHEHICLSDELPPQSGPAPTTDRGTSTDSPCRRSTATQMAPPGGPPAAPPGGRGHSHRDRIHYQADVRLEATEEIYLTPVQRPPDAAEPTSAFLPPTESRMSVSSDPDPAAYPSTAGRPHPSISEEEEGFDCLSSPERAEPPGGGWRGSLGEPPPPPRASLSSDTSALSYDSVKYTLVVDEHAQLELVSLRPCFGDYSDESDSATVYDNCASVSSPYESAIGEEYEEAPRPQPPACLSEDSTPDEPDVHFSKKFLNVFMSGRSRSSSAESFGLFSCIINGEEQEQTHRAIFRFVPRHEDELELEVDDPLLVELQAEDYWYEAYNMRTGARGVFPAYYAIEVTKEPEHMAALAKNSDWVDQFRVKFLGSVQVPYHKGNDVLCAAMQKIATTRRLTVHFNPPSSCVLEISVRGVKIGVKADDSQEAKGNKCSHFFQLKNISFCGYHPKNNKYFGFITKHPADHRFACHVFVSEDSTKALAESVGRAFQQFYKQFVEYTCPTEDIYLE
Protein: Dipeptidyl peptidase 1 (Cathepsin C) (Cathepsin J) (Dipeptidyl peptidase I) (Dipeptidyl transferase) (H0YCY8)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGKCCISDTIYELFTCVQLAVVGKGKRMMQ
Protein: Choline/ethanolamine transporter FLVCR2 (Calcium-chelate transporter) (CCT) (Feline leukemia virus subgroup C receptor-related protein 2) (Heme transporter FLVCR2) (Q9UPI3)
Organism: Homo sapiens (Human)
Function: Acts as an importer of heme. Also acts as a transporter for a calcium-chelator complex, important for growth and calcium metabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14729055, ECO:0000269|PubMed:38302740, ECO:0000269|PubMed:38778100}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Note=Present on both luminal (blood-facing) and abluminal (brain-facing) sides of brain endothelial cell plasma membranes, with higher luminal membrane expression (By similarity). Also localizes in mitochondria where it interacts with components of the electron transfer complexes III, IV and V (PubMed:32973183). Colocalizes with ATP2A2 at the mitochondrial-ER contact junction (PubMed:32973183). {ECO:0000250|UniProtKB:Q91X85, ECO:0000269|PubMed:32973183}.
Interaction partners:
Sequence:
MVNEGPNQEESDDTPVPESALQADPSVSVHPSVSVHPSVSINPSVSVHPSSSAHPSALAQPSGLAHPSSSGPEDLSVIKVSRRRWAVVLVFSCYSMCNSFQWIQYGSINNIFMHFYGVSAFAIDWLSMCYMLTYIPLLLPVAWLLEKFGLRTIALTGSALNCLGAWVKLGSLKPHLFPVTVVGQLICSVAQVFILGMPSRIASVWFGANEVSTACSVAVFGNQLGIAIGFLVPPVLVPNIEDRDELAYHISIMFYIIGGVATLLLILVIIVFKEKPKYPPSRAQSLSYALTSPDASYLGSIARLFKNLNFVLLVITYGLNAGAFYALSTLLNRMVIWHYPGEEVNAGRIGLTIVIAGMLGAVISGIWLDRSKTYKETTLVVYIMTLVGMVVYTFTLNLGHLWVVFITAGTMGFFMTGYLPLGFEFAVELTYPESEGISSGLLNISAQVFGIIFTISQGQIIDNYGTKPGNIFLCVFLTLGAALTAFIKADLRRQKANKETLENKLQEEEEESNTSKVPTAVSEDHL
Protein: Ornithine decarboxylase antizyme (ODC-Az) (Q9USQ5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome.
Interaction partners:
- Ornithine decarboxylase
- Large ribosomal subunit protein eL38B
- Probable catechol O-methyltransferase 2
- Uncharacterized protein C19F5.03
- Uncharacterized protein C3C7.01c
- BAG family molecular chaperone regulator 1B
- Double-strand-specific pac1 ribonuclease
- M-factor
- DNA repair and recombination protein rti1
Sequence:
MAFRNRMYQLSNVDDADADILNSHFAPNPRGQNHTHGRRRNTLALCTTKDQMFVYGSTPAGGAEWCSEALERSRPRAAFKQQRRRHVPRWISDSFRTCLPKPSGILKEQTVNEEEGNSRHRGKYDCDERIGVAESMNYWHGIVRTEEDGSKTLFLIPESWEDVHLKEGLVAIIDLAVDRLHCSKLVLFVDKNNSSLPYLVKSLHWVGFEPLPHLNCSDHALFGMEL
Protein: RRM domain-containing protein (Q21900)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSVSSRRVPLPPTSQHRASSNFNTTPSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKVGSTSRHPSFQQFSSLGGPTAFLNGQHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKYFQPMNPQ
Protein: Uncharacterized protein (Q381E9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Centromere/microtubule binding protein cbf5, putative
- Nucleolar protein 10
- H/ACA ribonucleoprotein complex subunit
- Integral membrane bound transporter domain-containing protein
Sequence:
MLTPVFVCTQDDSFVIVAITLSAMCKVMGAAFDITRLQFTFHCAPYYLRLKFDQPIAEGRGERATFDIASSLLTVYIPKENRGEVFTNLDNPAYLIATDMERRRLVQLVGGVCSAVRAENEAANEEERECGDDEGEDTEFRQRLQAPRGHTIDLKEGFGDYGFAASFHGTFAALDADVVADILDLPCNPDETTGEQRRQLRTQREQEDFDEDAVLLSFEDAEGDVECLLRYVPQHQRDYMNALDAEGIRYVRPATAMETVCCPVTSDNSGDNGSVCVNRSDTLEEEDVVLPDGSGLVNIWTGNIADFKRPLIEEVQPTEPSTEDHEAAHAAASSVPDTSGENSTMSSKCLAVPQRRPCANFTTEEQAVLLRITAPRLLFPPVGSAVNALTLDILLAEAYDDIVTEGAGCSESLWNVCKLSPALSWLDSPNTVYDACLAFARRVLVYPLHRNFALVQRAFSLVGIRLLLGKSYVIKALLRVRDILAHAEHRHVLVTLFMSPLIGYWMNVQDVDKRLAQLALEMHGHVTRTAPEWETVPPTPHTALLLQQRRQMFPLHVLNLGLPIS
Protein: BRI1 kinase inhibitor 1 (Q9FMZ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of brassinosteroid signaling. When associated to the membrane, limits the interaction of BRI1 with BAK1 by binding to the kinase-inactive form of BRI1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21289069}. Cytoplasm {ECO:0000269|PubMed:21289069}. Note=Once phosphorylated following brassinosteroid treatment, displaced from the plasma membrane into the cytosol where it is inactive.
Interaction partners:
- Protein BRASSINOSTEROID INSENSITIVE 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Protein BRASSINAZOLE-RESISTANT 2
- Serine/threonine-protein phosphatase BSU1
- Serine/threonine-protein kinase BSK1
- Shaggy-related protein kinase eta
- Protein BRASSINAZOLE-RESISTANT 1
- Serine carboxypeptidase 24
- Steroid 5-alpha-reductase DET2
- Steroid
Sequence:
METNLQQVKNSSQTFSEKQNPKQEASPSPISSTCSSPSHDFSFTISLQPLSSSSKHISPTLRSPSKTTSSYQQTDPFAVDLSPADEIFFHGHLLPLHLLSHLPVSPRTSTGSYNDGFTLPVKDILPDQPTNNNNNTENAITNISTEAKDDNTEDKAEGEIRVKTKPIKSFSLFGLSKWRKGFESNEREQEQQQQKIKKPMSLDLSHAVKKYIRMLFQKRGNGTQFWNRRQTSSYSFSSSLMGPNGNSKTMINGSYNKRDLIRGRRGELFSAPASMRTSPTNSGHLRVSTAGLSSSSGSTSSSSSDSTMEELQAAIQAAIAHCKNSSAVDRDDKVKDS
Protein: Heat shock factor protein 2 (HSF 2) (Heat shock transcription factor 2) (HSTF 2) (P38533)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked. HSF2 is expressed in a form that binds DNA constitutively but loses DNA binding by incubation at greater than 41 degrees C.
Subcellular location: Cytoplasm. Nucleus. Note=Cytoplasmic during normal growth and moves to the nucleus upon activation.
Interaction partners:
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- Heat shock factor protein 1
Sequence:
MKQSSNVPAFLSKLWTLVEETHTNEFITWSQNGQSFLVLDEQRFAKEILPKYFKHNNMASFVRQLNMYGFRKVVHIESGIIKQERDGPVEFQHPYFKQGQDDLLENIKRKVSSSKPEENKIRQEDLTKIISSAQKVQIKQETIESRLSELKSENESLWKEVSELRAKHAQQQQVIRKIVQFIVTLVQNNQLVSLKRKRPLLLNTNGAPKKNLYQHIVKEPTDNHHHKVPHSRTEGLKSRERISDDIIIYDVTDDNVDEENIPVIPETNEDVVVDSSNQYPDIVIVEDDNEDEYAPVIQSGEQSEPAREPLRVGSAGSSSPLMSSAVQLNGSSSLTSEDPVTMMDSILNDNINLLGKVELLDYLDSIDCSLEDFQAMLSGRQFSIDPDLLVDLFTSSVQMNPTDNIKYTKSENKGLEATKSSVVQHVSEEGRKSKSKPDKQLIQYTAFPLLAFLDGNSASAIEQGSTTASSEVVPSVDKPIEVDELLDSSLDPEPTQSKLVRLEPLTEAEASEATLFYLCELAPAPLDSDMPLLDS
Protein: Zeta-carotene desaturase, chloroplastic/chromoplastic (EC 1.3.5.6) (9,9'-di-cis-zeta-carotene desaturase) (Carotene 7,8-desaturase) (Protein CHLOROPLAST BIOGENESIS 5) (Protein PIGMENT DEFECTIVE 181) (Protein SPONTANEOUS CELL DEATH 1) (Q38893)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a crucial role in plant growth and development. Is essential for the biosynthesis of carotenoids. Carotenoids are involved in different physiological processes, including coloration, photoprotection, biosynthesis of abscisic acid (ABA) and chloroplast biogenesis. Catalyzes the conversion of zeta-carotene to lycopene via the intermediary of neurosporene. It carries out two consecutive desaturations (introduction of double bonds) at positions C-7 and C-7'. Shows stereoselectivity toward trans C15-C15'zeta-carotene double bond. The zeta-carotene produced by the phytoene desaturase PDS has a C15-C15' double bond in the cis configuration and it requires isomerization before being recognized as substrate by ZDS. The main product is 7,9,7',9'-tetra-cis-lycopene (pro-lycopene).
Subcellular location: Plastid, chloroplast. Plastid, chromoplast {ECO:0000305}.
Interaction partners:
- 15-cis-zeta-carotene isomerase, chloroplastic
- Prolycopene isomerase, chloroplastic
- Lycopene beta cyclase, chloroplastic
- Lycopene epsilon cyclase, chloroplastic
- Phytoene synthase 1, chloroplastic
- Zeaxanthin epoxidase, chloroplastic
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Violaxanthin de-epoxidase, chloroplastic
- Protein LUTEIN DEFICIENT 5, chloroplastic
- Carotene epsilon-monooxygenase, chloroplastic
Sequence:
MASSVVFAATGSLSVPPLKSRRFYVNSSLDSDVSDMSVNAPKGLFPPEPVPYKGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYDSRTFIGGKVGSFVDRRGNHIEMGLHVFFGCYNNLFRLMKKVGAEKNLLVKDHTHTFINKDGTIGELDFRFPVGAPIHGIRAFLVTNQLKPYDKLRNSLALALSPVVKALVDPDGAMRDIRNLDSISFSDWFLSKGGTRASIQRMWDPVAYALGFIDCDNMSARCMLTIFSLFATKTEASLLRMLKGSPDVYLSGPIKQYITDRGGRIHLRWGCREILYDKSADGETYVTGLAISKATNKKIVKADVYVAACDVPGIKRLLPKEWRESRFFNDIYELEGVPVVTVQLRYNGWVTELQDIELARQLKRAVGLDNLLYTPDADFSCFADLALASPADYYIEGQGTLLQCVLTPGDPYMRMPNDKIIEKVAMQVTELFPSSRGLEVTWSSVVKIAQSLYREAPGKDPFRPDQKTPIKNFFLAGSYTKQDYIDSMEGATLSGRQASSYICDAGEELAELNKKLSSSATAVPDELSLV