wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein 10-6 (High sulfur keratin-associated protein 10.6) (Keratin-associated protein 10.6) (Keratin-associated protein 18-6) (Keratin-associated protein 18.6) (P60371)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MAASTMSVCSSDLSYGSRVCLPGSCDSCSDSWQVDDCPESCCEPPCCAPAPCLSLVCTPVSRVSSPCCPVTCEPSPCQSGCTSSCTPSCCQQSSCQLACCASSPCQQACCVPVCCKTVCCKPVCCVSVCCGDSSCCQQSSCQSACCTSSPCQQACCVPVCCKPVCSGISSSCCQQSSCVSCVSSPCCQAVCEPSPCQSGCTSSCTPSCCQQSSCQPTCCTSSPCQQACCVPVCCVPVCCVPTCSEDSSSCCQQSSCQPACCTSSPCQHACCVPVCSGASTSCCQQSSCQPACCTASCCRSSSSVSLLCHPVCKSTCCVPVPSCGASASSCQPSCCRTASCVSLLCRPMCSRPACYSLCSGQKSSC
Protein: Valerianol synthase TPS1F (EC 4.2.3.204) (Terpene synthase 1f) (ChTps1f) (A0A348AUW0)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNCEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVEGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAGLTKIMLLLSVTDDTYDAYGTYNELKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRAYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIINDHVISLFEDPIPM
Protein: Transcription elongation factor SPT6 homolog (AtSPT6) (A8MS85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription elongation factor that enhances the transcription elongation by RNA polymerase II (RNAPII) (By similarity). Plays an important role in regulating embryo apical and basal patterning during early embryogenesis, partly through negative regulation of the transcription factors PHABULOSA and PHAVOLUTA.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- FACT complex subunit SPT16
- Protein IWS1 homolog 1
- FACT complex subunit SSRP1
- Protein IWS1 homolog 2
- FACT complex subunit
- Transcription elongation factor SPT4 homolog 2
- Protein CTR9 homolog
- Transcription elongation factor SPT4 homolog 1
- Protein CDC73 homolog
- Protein LEO1 homolog
Sequence:
MARNAISDDEEDHELEDDDGEPVHGDPAEHDENDDEEDDDDVGNEYENDGFIVNDEDEEEEEEEDEERKDSDEERQKKKKKRKKKDEGLDEDDYLLLQDNNVKFKKRQYKRLKKAQREQGNGQGESSDDEFDSRGGTRRSAEDKIKDRLFDDVDVDDPPDDVGDEEDLVVEEDVVGSEDEMADFIVDEDDEHGPPKRGNSKKKKYRQGSDITAMRDANEIFGDVDELLTIRKKGLASNQRMERRLEDEFEPTVLSEKYMTGNDDEIRQLDIPERMQISEESTGSPPVDEISIEEESNWIYAQLASQLRESDGTFDGRGFSVNKDDIAKFLELHHVQKLEIPFIAMYRKEQCRSLLDTGDFDGANQGKKPETKWHKVFWMIHDLDKKWLLLRKRKMALHGYYTKRYEEESRRVYDETRLNLNQYLFESVIKSLKVAETEREVDDVDSKFNLHFPPGEIGVDEGQYKRPKRKSQYSICSKAGLWEVANKFGYSAEQLGLALSLEKLVDELEDAKETPEEMAKNFVCAMFENSLAVLKGARHMAAVEISCEPSVKKYVRGIYMENAVVSTSPTADGNTVIDSFHQFSGIKWLREKPLSKFEGAQWLLIQKGEEEKLLQVTFKLPENYMNRLISDCNEHYLSVGVSKYAQLWNEQRKLILEDALHAFLLPSMEKEARSLLTSRAKSRLLSEYGQALWNKVSAGPYQKKEMDINLDEEAAPRVMACCWGPGKPPNTFVMLDSSGEVLDVLYAGSLTSRSQNVNDQQRKKSDQDRVLKFMMDHQPHVVALGAVNLSCTRLKDDIYEVIFQMVEEKPRDVGHGMDDLSIVYVDESLPRLYENSRISGEQLPQQSGNVRRAVALGRYLQNPLAMVATLCGPGREILSWKLHPLENFLQLDEKYGMVEQVMVDITNQVGIDINLAASHDWFFSPLQFISGLGPRKAASLQRSLVRAGSIFVRKDLIMHGLGKKVFVNAAGFLRIRRSGLAASSSQFIDLLDDTRIHPESYSLAQELAKDIYDEDVRGDSNDDEDAIEMAIEHVRDRPASLRKVVLDEYLASKKRENKKETYSNIIRELSCGFQDWRIPFKEPSPDEEFYMISGETEDTIAEGRIVQASVRRLQNGRAICVLDSGLTGMLMKEDFSDDGRDIVDLADQLKEGDILTCKIKSIQKQRYQVFLICKESEMRNNRHQHNQNVDAYYHEDRNSLQLVKEKARKEKELVRKHFKSRMIVHPRFQNITADQATEYLSDKDFGESIVRPSSRGLNFLTLTLKIYDGVYAHKEIAEGGKENKDITSLQCIGKTLTIGEDTFEDLDEVMDRYVDPLVSHLKTMLNYRKFRKGTKSEVDDLLRIEKGENPSRIVYCFGISHEHPGTFILSYIRSTNPHHEYIGLYPKGFKFRKRMFEDIDRLVAYFQRHIDDPLQESAPSIRSIAAKVPMRSPADHGSSGGSGWGSSQSEGGWKGNSDRSGSGRGGEYRNGGGRDGHPSGAPRPYGGRGRGRGRGRRDDMNSDRQDGNGDWGNNDTGTADGGWGNSGGGGWGSESAGKKTGGGSTGGWGSESGGNKSDGAGSWGSGSGGGGSGGWGNDSGGKKSSEDGGFGSGSGGGGSDWGNESGGKKSSADGGWGSESGGKKSDGEGGWGNEPSSRKSDGGGGGW
Protein: Glycine N-acyltransferase (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase) (AAc) (Aralkyl acyl-CoA N-acyltransferase) (Aralkyl acyl-CoA:amino acid N-acyltransferase) (Benzoyl-coenzyme A:glycine N-acyltransferase) (Glycine N-benzoyltransferase) (EC 2.3.1.71) (Q2KIR7)
Organism: Bos taurus (Bovine)
Function: Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate a multitude of substrates to form a variety of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:1445276, ECO:0000269|PubMed:457678}.
Interaction partners:
- Glycine N-acyltransferase-like protein
- Histidine-rich glycoprotein
- Cytochrome P450 2E1
- Flavin-containing monooxygenase 3
- Phosphoenolpyruvate carboxykinase, cytosolic
Sequence:
MFLLQGAQMLQMLEKSLRKSLPMSLKVYGTVMHMNHGNPFNLKALVDKWPDFQTVVIRPQEQDMKDDLDHYTNTYHVYSEDLKNCQEFLDLPEVINWKQHLQIQSTQSSLNEVIQNLAATKSFKVKRSKNILYMASETIKELTPSLLDVKNLPVGDGKPKAIDPEMFKLSSVDPSHAAVVNRFWLFGGNERSLRFIERCIQSFPNFCLLGTEGTPVSWSLMDQTGEMRMAGTLPEYRAQGLVTHAIYQQAQCLLKRGFPVYSHVDPKNQIMQKMSQSLNHVPMPSDWNQWNCEPL
Protein: Sprouty-related, EVH1 domain-containing protein 2 (Spred-2) (Q924S7)
Organism: Mus musculus (Mouse)
Function: Negatively regulates Ras signaling pathways and downstream activation of MAP kinases. Recruits and translocates NF1 to the cell membrane, thereby enabling NF1-dependent hydrolysis of active GTP-bound Ras to inactive GDP-bound Ras (By similarity). Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2. Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11493923}; Peripheral membrane protein {ECO:0000269|PubMed:11493923}; Cytoplasmic side {ECO:0000269|PubMed:11493923}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q7Z698}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q7Z698}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7Z698}. Cytoplasm {ECO:0000269|PubMed:11493923}. Note=Detected in the cytoplasm of the stratum spinosum cells, where it is associated with cytoplasmic vesicles that are supposed to be secretory granules. {ECO:0000250|UniProtKB:Q7Z698}.
Interaction partners:
- Neurofibromin
- Sprouty-related, EVH1 domain-containing protein 1
- GTPase HRas
- GTPase KRas
- Fibroblast growth factor receptor-like 1
Sequence:
MTEETHPDDDSYIVRVKAVVMTRDDSSGGWFPQEGGGISRVGVCKVMHPEGNGRSGFLIHGERQKDKLVVLECYVRKDLVYTKANPTFHHWKVDNRKFGLTFQSPADARAFDRGVRKAIEDLIEGSTTSSSTLHNEAELGDDDVFTTATDSSSNSSQKREPTTRTISSPTSCEHRKIYTLDPYPMDHYHPDQRLPRSYPQVTFPEDDEEIVRINPREKIWMTGYEDYRHAPVRGKYLDTTEDADSYVRFAKGEVPKHEYTYPYVDSSDFGFGEDPKGSVIKTQPPRAKSRRRKENGERSRCVYCRDMFNHEENRRGHCQDAPDAVRTCIRRVSCMWCADSMLYHCMSDPEGDYTDPCSCDTSDEKFCLRWMALIALSFLAPCMCCYLPLRACHRCGVMCRCCGGKHKAAA
Protein: Cytochrome P450 4A12 (EC 1.14.14.1) (CYPIVA12) (CYPIVA8) (Cytochrome P450-KP1) (Cytochrome P450-PP1) (P24464)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of saturated and unsaturated fatty acids. May act as a major omega-hydroxylase for dodecanoic (lauric) acid in kidney. At preglomerular arteries, may participate in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure. Can also catalyze the oxidation of the penultimate carbon (omega-1 oxidation) of fatty acids with lower efficiency, displaying a preference for the (R)-stereoisomer. 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 (NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15618658}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:15618658}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome P450 3A1
- Cytochrome P450 2E1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Cytochrome P450 3A18
- Cytochrome P450 1A2
- Cytochrome P450 3A9
- Cytochrome P450 1A1
- Cytochrome P450 2U1
- UDP-glucuronosyltransferase 2B37
- UDP-glucuronosyltransferase 1A1
Sequence:
MSGSALSFTIFPGSILGFLQIATVLTVLLLLFKTAQFYLHRRWLLRATQQFPSPPSHWFFGHKIPKDQEFQDILTRVKNFPSACPQWLWGSNVRIQVYDPDYMKLILGRSDPKSHHSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDTLKPYVGIMADSVRIMLDKWEQIVGQDSTLEIFQHITLMTLDTIMKCAFSQEGSVQLDRKYKSYIKAVEDLNNLSFFRIRNIFHQNDIIYSLSSNGRKARSAWQLAHEHTDQVIKSRKAQLQDEEELQKVKQKRRLDFLDILLFARIENGSSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQGCRKEIQSLLGDGASITWDDLDKMPYTTMCIKEALRIYPPVTAVSRMLSTPVTFPDGRSLPKGITVMLSFYGLHHNPTVWPNPEVFDPYRFAPESSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRIPIPIPRLVLKSKNGIYLRLKKLQ
Protein: Bifunctional lycopene cyclase/phytoene synthase [Includes: Lycopene beta-cyclase (EC 5.5.1.19) (Carotene cyclase) (Lycopene cyclase); Phytoene synthase (EC 2.5.1.32)] (Q8X0Z1)
Organism: Gibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium fujikuroi)
Function: Bifunctional enzyme; part of the car gene cluster that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation. CarAR catalyzes the first step of the pathway by converting geranylgeranyl diphosphate to phytoene, as well as the later cyclization step that transforms the carB product lycopene into gamma-carotene. CarAR also converts part of gamma-carotene into beta-carotene. Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma-carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'-carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MGWEYAQVHLKYTIPFGVVLAAVYRPLMSRLDVFKLVFLITVSFFWVVKGLEANSCRLLLFLPCMLILRGVLLRLTNADSPWDSYLIKNRIWTYPPGVVVGLTAWDIPAEELFFFVIQTFNTSLLYMILSKPTFHPIYLSKKTGWGKIAGQILFASAIIFGLVSVSSGGEGMYMGLILIWACPFLLFLWSISYQFIVNLPWTNTALPIALPTLYLWVVDTFALRRGTWSITSGTKYGVVLWDGLEIEEAVFFLLTNTLIVFGLIACDNNLAILDTFPEHFPRTKGVPSLLTIIRTLILPKEKYDEERIQGLVSAVALLRKKSRSFYLASGTFEGRLRIDLIRLYAFCRAADDLVDEAPSVDDSRASIEKLRKFLDLAYEENQEEPSQRLREYVTSSIPEMFHMALLQLPTYYLPKQPLDDLLKGFDTDLLFDRKSGAFPIETTEDLDIYGSRVAGTVAELCNHLILYHTPEAVPEDIQREVVASGQEMGIALQYVNIARDIKTDAEIDRVYLPLSWLKEAQLTPEDVIQQPHGPTIEALRHKLLDRAFEKYNMAKGAIDKLPSEGKGPIRVAVESYMEIGRVLREKGPTMKKGRATVPKMRRIRVAWSALNK
Protein: Protein STRICTOSIDINE SYNTHASE-LIKE 4 (AtSSL4) (Q9SD07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole {ECO:0000250}.
Interaction partners:
- D-alanine-D-alanine ligase family
- Probable polygalacturonase At1g80170
- Probable pectinesterase/pectinesterase inhibitor 32
- Pectin lyase-like superfamily protein
- Disease resistance protein RRS1
Sequence:
MVLFFSTRFLFFSIFFPCLISITLYQLDSFEPASLPADSLITSPTSIPPLLNDRFLTGAEFIGVGLLNNPEDIAYHKDSNLIYTGCVDGWVKRVSVHDSANDSIVEDWVNTGGRPLGIAFGLHGEVIVADANKGLLSISDGGKKTELLTDEADGVRFKLTDAVTVADNGVLYFTDASSKYDFYQFIFDFLEGKPHGRVMSFDPTTRATRVLLKDLYFANGISMSPDQTHFVFCETIMRRCSKYYISEERVEVFIQGLPGYPDNIRYDGDGHYWIALISEVTTSWKLSMKYLFLRKLIYMAAKYGVELLSIKNAAVLQVDLDGNPIAMYHDHPFSHITSGVKIGNHLYFGSLLHSYITRLDLLKYPAQKKL
Protein: Protein fem-1 homolog A (FEM1a) (FEM1-alpha) (Prostaglandin E receptor 4-associated protein) (Q9BSK4)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1A) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. Promotes ubiquitination and degradation of SLBP. Involved in PGE2-EP4-mediated inhibition of inflammation of macrophages via interaction with NFKB1 and PTGER4 (By similarity). Promotes inflammation in brain microglia through MAP2K4/MKK4-mediated signaling (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19406122}. Cytoplasm {ECO:0000305|PubMed:16424369}.
Interaction partners:
- Cullin-2
- Elongin-B
- Amyloid protein-binding protein 2
- Kelch domain-containing protein 2
- Kelch domain-containing protein 10
- Kelch domain-containing protein 3
- E3 ubiquitin-protein ligase RBX1
- Protein fem-1 homolog B
- Protein zyg-11 homolog B
- Protein zer-1 homolog
Sequence:
MDLRTAVYNAARDGKLQLLQKLLSGRSREELDELTGEVAGGGTPLLIAARYGHLDVVEYLVDRCGASVEAGGSVHFDGETIEGAPPLWAASAAGHLDVVRSLLRRGASVNRTTRTNSTPLRAACFDGHLEVVRYLVGEHQADLEVANRHGHTCLMISCYKGHREIARYLLEQGAQVNRRSAKGNTALHDCAESGSLEILQLLLGCKARMERDGYGMTPLLAASVTGHTNIVEYLIQEQPGQEQVAGGEAQPGLPQEDPSTSQGCAQPQGAPCCSSSPEEPLNGESYESCCPTSREAAVEALELLGATYVDKKRDLLGALKHWRRAMELRHQGGEYLPKPEPPQLVLAYDYSREVNTTEELEALITDPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFERCIRLWKYALDMQQSNLEPLSPMTASSFLSFAELFSYVLQDRAAKGSLGTQIGFADLMGVLTKGVREVERALQLPREPGDSAQFTKALAIILHLLYLLEKVECTPSQEHLKHQTVYRLLKCAPRGKNGFTPLHMAVDKDTTNVGRYPVGRFPSLHVVKVLLDCGADPDSRDFDNNTPLHIAAQNNCPAIMNALIEAGAHMDATNAFKKTAYELLDEKLLARGTMQPFNYVTLQCLAARALDKNKIPYKGFIPEDLEAFIELH
Protein: Kunitz-type serine protease inhibitor LmKTT-1b (Delta-KTx 2.2) (SdPI) (P0DJ45)
Organism: Lychas mucronatus (Chinese swimming scorpion)
Function: Dual-function toxin that completely inhibits trypsin activity at a molar ratio of 1:1 (dissociation constant of 160 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents (1 uM inhibits 50% of currents). It is thermostable.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKSFLLIALVLFFLFVSYASAKNKCQLPSDVGKGKASFTRYYYNEEGGKCETFIYGGVGGNSNNFLTKEDCCRECAQGSC
Protein: Brother of CDO (Q8UVD6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSGTLNWIPWERKRKIRVLCSLCVLLFCLQDSNAVTDDVPVFTEEPFSVVQKLGGSVTLRCSALPNHVNISWHLNGRELPAGGDEELGVLVRPGSLYIPSLTNLTVGRYQCVATTSVGSCASVPANVTAAKLRDFEPDDQQEIEVDEGNTAVIECHLPESQPKAQVRYSVKQEWLETSKGNYLIMPSGNLQIANATRDDEGPYICAAYNPVTQEIKTSTSTDRLRIRRSTSEAARIIYPPASRSIMVNKGQRLVLECVASGIPTPQVTWAKDGLDLRNHNNTRFLLSNLLIDAASESDSGTYVCLADNGIGSTSSAQVLYDVQVFEPPQVRVELQQQDVAWGDTVRFSCQVRGKPAPTVVWLHNAQPLSPSPRHRVSAQVLRVLNVGPQDDGMYQCMAENGVGSSQAATRLLTLPTVPSRKMPMIRPLSPDKVLREQPPLKPPVSTSAVLPFDCSEVRVSPAEAPVILSQPRTGKADYYELTWKPRHDGGAPVLEYIIKYRKAGESPGEWTTNTISGSQHKLILTKLQPASLYEVEMAARNCAGLGQPAMMTFRTGKWRRGGPIGPPKTPVVQPRLSPPEAPDRPTVSMATETSAYVTWIPRGNRGFPIQSFRVEHKKLRKGSGDWEVAVNNIPPSRLSVEVTGLEKGTSYKFRVLAVNVLGASPPSAPSKAYTVVGSGPPNRRPIDGPYITYNEAINETTIILKWTYTPLNNTPIYGFYIFYRPTDSDNDSDYKKDVVEGDRYWHSITDLQPETAYDIKMQCFNEGGESEFGNVVILETKARPHQRTTPPETASSRPEHPGNPVPRPGDLPYLIVGVVLGAFVFIIVAFIPICLWRVWAKQKQTLDMRFPTLAATVSPCQYTMVPLQGLALGRACPVDPHLSPSHTVYAPKAEYIPNGKHAAQRLPPGHQEDPNYELECDALLPQDLPNQQQNIHNYCNGVPGCPEEGFCVSDDSPLRLFSLSDAPLESQDDHSLNECIHTEEELTADLTLLSIAEASINRLLQQAEPQQEGTTENTKQLEEQGTHDPEDG
Protein: Nucleoporin NUP188 (Nuclear pore protein NUP188) (P52593)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP188 probably plays an important role in NPC assembly and organization.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NUP170
- Nucleoporin NUP53
- Nucleoporin NUP192
- Nucleoporin NUP157
- Nucleoporin NIC96
- Nucleoporin POM152
- Nucleoporin ASM4
- Nucleoporin NUP57
- Nucleoporin NUP145
- Nucleoporin NUP120
Sequence:
MATPSFGNSSPQLTFTHVANFMNDAAADVSAVDAKQLAQIRQFLKANKTNLIESLNTIRQNVTSSGDHNKLRSTIANLLQINVDNDPFFAQSEDLSHAVEFFMSERSSRLHIVYSLLVNPDIDLETYSFIDNDRFNVVGKLISIISSVIQNYDIITASSLAHDYNNDQDMFTIVSLVQLKKFSDLKFILQILQILNLMILNTKVPVDIVNQWFLQYQNQFVEFCRNINSTDKSIDTSSLQLYKFQNFQDLSYLSETLISRISSLFTITTILILGLNTSIAQFDIQSPLYMDTETFDTVNSALENDVATNIVNEDPIFHPMIHYSWSFILYYRRALQSSESFDDSDITKFALFAESHDVLQKLNTLSEILSFDPVYTTVITVFLEFSLNFIPITASTSRVFAKIISKAPEQFIENFLTNDTFEKKLSIIKAKLPLLNESLIPLINLALIDTEFANFELKDICSFAVTKSSLNDLDYDLIADTITNSSSSSDIIVPDLIELKSDLLVAPPLENENSNCLLSIPKSTKGKILTIKQQQQQQQQQNGQQPPTTSNLIIFLYKFNGWSLVGRILQNLLHSYMEKGTQLDDLQHELMISIIKLVTNVVDPKTSIEKSSEILSYLSNSLDTSASTINGASIIQVIFEIFEISLQRKDYTSIVQCCEFMTMLTPNYLHLVSSYLNKSDLLDKYGKTGLSNMILGSVELSTGDYTFTIQLLKLTKVFIRESLSLKNIHISKRSKIDIINKLILHAIHIFESYYNWKYNNFLQKFEIAFHLTLIFYDVLHDVFTINPHQKDQLIISSSANKLLQLFLTPMDSIDLAPNTLTNILISPLNTTTKILGDKILGNLYSKVMNNSFKLCTLLIAIRGSNRDLKPSNLEKLLFINSSKLVDVYTLPSYVHFKVQIIELLSYLVEAPWNDDYPFLLSFLGEAKSMAFLKEVLSDLSSPVQDWNLLRSLYIFFTTLLESKQDGLSILFLTGQFASNKKINDESSIDKKSSILTVLQKNSLLLDSTPEEVSCKLLETITYVLNTWTNSKIFIKDPKFVNSLLAKLKDSKKLFQKKENLTRDETVSLIKKYKLISRIVEIFALCIYNSTDSNSEILNFLNQEDLFELVHHFFQIDGFNKTFHDELNLKFKEKWPSLELQSFQKIPLSRINENENFGYDIPLLDIVLKADRSWNEPSKSQTNFKEEITDASLNLQYVNYEISTAKAWGALITTFVKRSTVPLNDGFVDLVEHFLKLNIDFGSDKQMFTQIYLERIELSFYILYSFKLSGKLLKEEKIIELMNKIFTIFKSGEIDFIKNIGKSLKNNFYRPLLRSVLVLLELVSSGDRFIELISDQLLEFFELVFSKGVYLILSEILCQINKCSTRGLSTDHTTQIVNLEDNTQDLLLLLSLFKKITNVNPSKNFNVILASSLNEVGTLKVILNLYSSAHLIRINDEPILGQITLTFISELCSIEPIAAKLINSGLYSVLLESPLSVAIQQGDIKPEFSPRLHNIWSNGLLSIVLLLLSQFGIKVLPETCLFVSYFGKQIKSTIYNWGDNKLAVSSSLIKETNQLVLLQKMLNLLNYQELFIQPKNSDDQQEAVELVIGLDSEHDKKRLSAALSKFLTHPKYLNSRIIPTTLEEQQQLEDESSRLEFVKGISRDIKALQDSLFKDV
Protein: Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial (4-hydroxy-3-methoxy-5-polyprenylbenzoate decarboxylase) (EC 4.1.1.-) (Coenzyme Q biosynthesis protein 4 homolog) (Q54CZ2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the coenzyme Q biosynthetic pathway. May play a role in organizing a multi-subunit COQ enzyme complex required for coenzyme Q biosynthesis. Required for steady-state levels of other COQ polypeptides.
Subcellular location: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03111}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03111}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03111}.
Interaction partners:
- Sugar phosphate transporter domain-containing protein
- Probable ubiquinone biosynthesis protein coq9
- Putative UDP-sugar transporter DDB_G0278631
- Mitochondrial DNA repair protein recA homolog
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- Probable serine/threonine-protein kinase abkA
Sequence:
MNSSSNIIYKSFKNSKIFLNKQCIINNGLKLNKKYFTTTSTKENNNNNNNKNPKFIENNLFQKGLLTIGSAFVAFINPGRGDMVATLGEMTGGCAIKSMKQKMMLDPIGRQLLKEKPRIKESTYPLNIHLLPSTTFGGAYYRWMKEHGYSPDERTEVTLIQDEDDAYVMQRYREVHDFWHVLAGVRPDFQGEVAIKWFEFLQTGLPMNAIGSIIGPLRCSWNERNELINHMIPWAIKSSKSCVYLMNVKYEDHWEDDLNEFRAKLNFIPYKYLSDINQNKTTTINM
Protein: Protein E7 (P04020)
Organism: Human papillomavirus 11
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MHGRLVTLKDIVLDLQPPDPVGLHCYEQLEDSSEDEVDKVDKQDAQPLTQHYQILTCCCGCDSNVRLVVECTDGDIRQLQDLLLGTLNIVCPICAPKP
Protein: Lipoamide dehydrogenase, putative, expressed (Os03g0797600 protein) (cDNA clone:006-203-H10, full insert sequence) (Q7Y1H4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGQQPQQQGPPEDDFFDQFFSLTSSFPGAAPGGRAAGDQPFSLALSLDAAAAAEASGSGKRLGVGDDAEGGGSKADRETVQLTGLFPPVFGGGGVQPPNLRPTPPTQVFHPQQSKQGGAAVGPQPPAPRPKVRARRGQATDPHSIAERLRRERIAERMRALQELVPNTNKTDRAAMLDEILDYVKFLRLQVKVLSMSRLGGAGAVAQLVADIPLSVKGEASDSGGNQQIWEKWSTDGTERQVAKLMEEDIGAAMQFLQSKALCMMPISLAMAIYDTQQTQDGQPVKHEPNTPS
Protein: Auxin response factor 12 (Q9XID4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxin response factors (ARFs) are transcriptional factors that bind specifically to the DNA sequence 5'-TGTCTC-3' found in the auxin-responsive promoter elements (AuxREs). Could act as transcriptional activator or repressor. Formation of heterodimers with Aux/IAA proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus.
Interaction partners:
- Auxin-responsive protein IAA28
- Auxin-responsive protein IAA34
- Auxin-responsive protein IAA26
- B3 domain-containing protein REM7
- Auxin-responsive protein IAA8
- Auxin-responsive protein IAA5
- Auxin-responsive protein IAA2
- Auxin-responsive protein IAA30
- Auxin-responsive protein IAA32
- Auxin-responsive protein IAA29
Sequence:
MESGNVVNAQPELSGIIDGSKSYVYEQLWKLCAGPLCDIPKLGEKVYYFPQGHIELVETSTREELNELQPICDLPSKLQCRVIAIHLKVENNSDETYAEITLMPDTTQVVIPTQNENQFRPLVNSFTKVLTASDTSAHGGFFVPKKHAIECLPSLDMSQPLPAQELLAIDLHGNQWRFNHNYRGTPQRHLLTTGWNAFTTSKKLVAGDVIVFVRGETGELRVGIRRARHQQGNIPSSIVSIDCMRHGVVASAKHAFDNQCMFTVVYKPRSSKFIVSYDKFLDAVNNKFNVGSRFTMRLEGDDFSERRCFGTIIGVSDFSPHWKCSEWRSLEVQWDEFTSFPGPKKVSPWDIEHLMPAINVPRSFLLKNKRLREVNEIGSSSSHLLPPILTQGQENEQLSVASPMNISLRYRDATEDAMNPSKLLMSYPVQPMPKLNYNNQMVTEMEENITTKTGTNFRLFGVTLDTPPVIKDPIEEIGSEISKLTEGKKFGLSQTLRSPTEIQNKQFSSSRTCTKVQMQGVTIGRAVDLSVLNGYDQLILELEKLFDIKGQLQTRNQWEIAFTDSDEDKMLVGDDPWPEFCNMVKKIFIQKRR