wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger (Ran-binding) family protein (Q9C7M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase RFK1
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
Sequence:
MAASISLLLIKRISHLHINPKSHRLFQPFLTKSLSTSPQSNTESTHEPNHKPSSLSSRLSFVFDQIDAIEKRHSEKDETLERIRAWRQSKQTHQLKTPPSAPQQDPDLREVESVVSNDKLDSCVVLEPIQIDSGELSKEKGVIELVHPWPEWMELMERLVKQNYFDHRRERDDDDMVNSLGIDVSSVGLGEDENVGVALFQDFRAVQNACSNFGKDRFDILRSLSRNDIQILVGHGCPATDRKVVFSGKLLRKRVHLDEGDVCSSCSLRNSCEKAFLLTNKEDEARTIDLMRILFTYGFDPLNGTVANKSLLKKKSVKSVVRKLLHEIVKLSAVPIDPNLTPPVIKRAPPKVKQPPPTPKRRVGRDDVEMKKGDWLCPKCDFMNFAKNTICLQCDAKRPKRQLLPGEWECPECNFLNYRRNMACFHCDCKRPADAILENKPQETYRFTEAQTDRVVKRDDVSNAWNFDFDDDESDGAEVAAFEYADSSKKNENLLREGLRDPEEEFGNLPPGARESSEFGRSRRPGVGFDDFDDEDDIDSYEIDESKERDVPVEGARSSFASDEFSEDEKFPESKSGFNAHRGGSSNFHNSGKKHGNSKGGFSRDDELGFSSDDEVSANPRWKSSHVASTQRGPPSRKLTFGSDEEFGLDSDMEDDSPRSGLRRGQRNNGARGGFKGKRSSYSASESDDDMDDQEYRGSSFSGNRSRGSRGRMRGGGRGGFNDNFASDSYRGSNGSSANRSRGRGGRIGSRRSSFDSDDEDYRGSSSSASRSRGNREDSGGVGGRMGSRRGGFDDEFDRKSSRGRGSGSFRGSNRGGRGGGGGGNRHGHSDGKDTDVGDFRNSRRVIER
Protein: Centrin, putative (Q382E7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-repair protein, putative
Sequence:
MEGPKLKGAARCAAVEKVESKTQLSIAISEKHKAQLREAFDFFDSDGTGRINAQDVKVAFCALGYEVGKEELTHLLRQVGASTTGVIDFNDFYSVIIAKIMQRENRSEAIRAFKLIDTGEKGYINVDDLRPIAASLQMNLTDDELAEMVLFAHPSATYSKADTEMKDPLTVSEEEFLKLMNRAHVY
Protein: Tegument protein VP16 (Alpha trans-inducing protein) (Alpha-TIF) (ICP25) (Vmw65) (P68336)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F 1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection (By similarity).
Subcellular location: Virion tegument {ECO:0000250|UniProtKB:P04486}. Host nucleus {ECO:0000250|UniProtKB:P04486}.
Interaction partners:
Sequence:
MDLLVDDLFADADGVSPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSGFPTNADMYRECKFLSTLPSDVIDWGDAHVPERSPIDIRAHGDVAFPTLPATRDELPSYYEAMAQFFRGELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRNRDLREMLRTTIADRYYRETARLARVLFLHLYLFLSREILWAAYAEQMMRPDLFDGLCCDLESWRQLACLFQPLMFINGSLTVRGVPVEARRLRELNHIREHLNLPLVRSAAAEEPGAPLTTPPVLQGNQARSSGYFMLLIRAKLDSYSSVATSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLVAPRMSFLSAGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit P (A0A2R8Q1D2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q isoform X1
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol glycan anchor biosynthesis, class L.
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GPI alpha-1,2-mannosyltransferase 3
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- Glycosylphosphatidylinositol anchor attachment 1.
- Phosphatidylinositol glycan anchor biosynthesis, class T.
Sequence:
MVMVENSPSPLPERAIYGFVLFLGAQLGFLLYVVWAFVPDSWLHAAGLTYWPQKYWALAGPIYLLVALSTCFVLLFGVNMMNTAPLASVDNITDAYGRSQRVDEDQPGAIPRLRDVSVSEMSRLFYL
Protein: Haptoglobin (Zonulin) [Cleaved into: Haptoglobin alpha chain; Haptoglobin beta chain] (P00738)
Organism: Homo sapiens (Human)
Function: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway.
Subcellular location: Secreted.
Interaction partners:
- Scavenger receptor cysteine-rich type 1 protein M130
- Apolipoprotein A-I
- Alpha-2-macroglobulin
- Hemoglobin subunit alpha
- Albumin
- Hemoglobin subunit beta
- Hemopexin
- Alpha-1-acid glycoprotein 1
- Myoglobin
- Haptoglobin-related protein
Sequence:
MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN
Protein: NAD(P) transhydrogenase subunit beta (EC 7.1.1.1) (Nicotinamide nucleotide transhydrogenase subunit beta) (Proton-translocating transhydrogenase NADP(H)-binding component) (Pyridine nucleotide transhydrogenase subunit beta) (dIII) (Q2RSB4)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
Subcellular location: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- NAD
- NAD
- Glutamine-dependent NAD
- Alanine dehydrogenase
- NAD kinase
- Probable nicotinate-nucleotide adenylyltransferase
- Nucleoside triphosphate pyrophosphohydrolase
- NAD-dependent protein deacylase
- NAD
Sequence:
MTHSLTMAAYIVAGVLFILALRGLSNPESARNGNRMGMVGMAIAILTTLLSPSVQAYAWIVLAIAIGGAIGTVIAKKVLMTALPQLVAAFHSLVGMAAVLVATGALLNPEAYGIGSAGAIHAGSLVEMSLGLAVGAITFSGSVIAFGKLQGLIAGKPVTFPMQHPLNAVLGILLVVLLVVFAATESHTAYFALMILAFALGFLLIIPIGGADMPVVISMLNSYSGWAAAGIGFTLGNPLLIIAGALVGSSGAILSYIMCKGMNRSIFNVILGGFGSEGGVAAAGGAAGDRSVKAGSAEDAAFIMKNASKVIIVPGYGMAVAQAQHALREMADVLKKEGVEVSYAIHPVAGRMPGHMNVLLAEANVPYDEVFELEEINSSFQTADVAFVIGANDVTNPAAKTDPSSPIYGMPILDVEKAGTVLFIKRSMASGYAGVENELFFRNNTMMLFGDAKKMTEQIVQAMN
Protein: Forkhead box protein O4 (Afxh) (Fork head domain transcription factor AFX1) (Q9WVH3)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity (By similarity). Represses smooth muscle cell differentiation by inhibiting the transcriptional coactivator activity of myocardin.
Subcellular location: Cytoplasm. Nucleus. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm (By similarity). {ECO:0000250|UniProtKB:P98177}.
Interaction partners:
- Cellular tumor antigen p53
- Histone lysine acetyltransferase CREBBP
- RAC-alpha serine/threonine-protein kinase
- Ataxin-3
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
- Ubiquitin carboxyl-terminal hydrolase 7
- Serine/threonine-protein kinase Sgk1
- Mitogen-activated protein kinase 14
- Cyclin-dependent kinase 2
Sequence:
MDPENKKSATGAAAILDLDPDFEPQSRPRSCTWPLPRPDLATEPHEPSEVEPSLGQKVPTEGHSEPILLPSRLPEPAGGPQPGILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPDGGKGGKAPRRRAASMDSSSKLLRGRSKGPKKKPSVLPAPPEGATPRSPLGHFAKWSSSPCPRNREEADVWTTFRPRSSSNASTVSTRLSPMRPESEVLAEEEMPASASSYAGGVPPTLSEDLELLDGLNLASPHSLLSRSGLSGFSLQHPGLAGPLHSYGASLFGPIDGSLSAGEGCFSSSQSLEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGMPSSSKLGTGVSLCPTPLEGPGPSNLVPNLSVMAPPPVMAGAPIPKVLGTPVLASPTEDSSHDRMPQDLDLDMYMENLECDMDNIISDLMDGEGLDFNFEPDP
Protein: Transcription factor srbB (Sterol regulatory element-binding protein B) (Q4W9W8)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Patched sphingolipid transporter
- Importin-95
Sequence:
MAYNNRPDASTAFTFDNDDRFVNQQPKGPDPLSANWSYDSAIDLFSLNTMLPETFPLDIPNDMLLDPKDFPTDLFAPPADISGFAISHSGEDSLSSDQESEDQPWSPAYRVSSLDSTTPDAPTVSPRSTEKPATRRRTTTQKREQATRWSSSPEMTPQEYPVTSQATTSPAPAPVSPPAASTSRKNSRSLSTDSQTATGRNAAKRAAHNIIEKRYRTNMNAKFVALEKAMSGSGVQKPTKGGSGPASLKKSEILTNAIAYMQELQDQNAALQKELALLKQNLLPGGLWRHNKENDKFRT
Protein: LP10490p (Q9VRR4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPRVTFVDSAPMVLKETNINKMHTPSEGMLHINPKDFVNFNSKNAEATMTIKSIATSAVTYKIQTTSPEKFRVRPRCGIIQPNQEATINIWLKSEHKLSDDSKDKFLVMAMVAPGGECGGADVTELWRSKSPTSADVEQHRLVCRFDENKSKAQLDCASKSSKASVDCSKKSGAGVDPATAMERQLAFTQNLQYVTLALLFLLFAGFGFLMYQQLGQHAATCPKATAYSCAKRK
Protein: ATPase 1, plasma membrane-type (PM H(+)-ATPase 1) (Plasma membrane-type ATPase 1) (EC 7.1.2.1) (Proton pump 1) (P20649)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26071421, ECO:0000305|PubMed:15308754}; Multi-pass membrane protein {ECO:0000305|PubMed:15308754}.
Interaction partners:
- Phytosulfokine receptor 1
- Cyclic nucleotide-gated ion channel 17
- Phytosulfokine receptor 2
- RPM1-interacting protein 4
- Protein unc-13 homolog
- Proton pump-interactor 1
- Proton pump-interactor 3B
- Proton pump-interactor 4
- Tyrosine-sulfated glycopeptide receptor 1
- Soluble inorganic pyrophosphatase 5
Sequence:
MSGLEDIKNETVDLEKIPIEEVFQQLKCTREGLTTQEGEDRIVIFGPNKLEEKKESKILKFLGFMWNPLSWVMEAAALMAIALANGDNRPPDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTSIGNFCICSIAIGIAIEIVVMYPIQHRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDSDGNWHRVSKGAPEQILDLANARPDLRKKVLSCIDKYAERGLRSLAVARQVVPEKTKESPGGPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSAALLGTDKDSNIASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEFDFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGIVLGGYQAIMSVIFFWAAHKTDFFSDKFGVRSIRDNNDELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFVIAQLVATLIAVYADWTFAKVKGIGWGWAGVIWIYSIVTYFPQDILKFAIRYILSGKAWASLFDNRTAFTTKKDYGIGEREAQWAQAQRTLHGLQPKEDVNIFPEKGSYRELSEIAEQAKRRAEIARLRELHTLKGHVESVAKLKGLDIDTAGHHYTV
Protein: Putative glutathione hydrolase 3 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 3) (Putative gamma-glutamyltranspeptidase 3) (GGT 3) (EC 2.3.2.2) [Cleaved into: Putative glutathione hydrolase 3 heavy chain; Putative glutathione hydrolase 3 light chain] (A6NGU5)
Organism: Homo sapiens (Human)
Function: Hydrolyzes and transfers gamma-glutamyl moieties from glutathione and other gamma-glutamyl compounds to acceptors.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
Interaction partners:
Sequence:
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCLEIGRDTLRDGGSAVDAAIAALLCVGLMNAHSMGIGVGLFLTIYNSTTRKAEVINAREVAPRLAFASMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAVLENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPRLADTYEMLAIEGAQAFYNGSLMAQIVKDIQAAGGIVTAEDLNNYCAELIEHPLNISLGDAVLYMPSARLSGPVLALILNILKGYNFSRESVETPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRSQISDHTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVCSPVSGILFNNMDDFSSPSITNEFGAPPSPANFIQPGKQPLLSMCPTIMVGQDGQVRMVVGAAGGTQITTDTALAIIYNLWFGYDVKRAVEEPRLHNKLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
Protein: Myoglobin (Nitrite reductase MB) (EC 1.7.-.-) (Pseudoperoxidase MB) (EC 1.11.1.-) (Q6VN46)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Subcellular location: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}.
Interaction partners:
- Neuroglobin
- Cytoglobin-1
- Cytoglobin-2
- Cytochrome c
- Thyroglobulin.
- Androglobin
- Myosin, light chain 1, alkali; skeletal, fast
- Alpha-1,4 glucan phosphorylase
- Alpha-1,4 glucan phosphorylase
- Mediator of RNA polymerase II transcription subunit 12
Sequence:
MADHDLVLKCWGAVEADYAANGGEVLNRLFKEYPDTLKLFPKFSGISQGDLAGSPAVAAHGATVLKKLGELLKAKGDHAALLKPLANTHANIHKVALNNFRLITEVLVKVMAEKAGLDAAGQGALRRVMDAVIGDIDGYYKEIGFAG
Protein: Protoporphyrinogen oxidase (PPO) (EC 1.3.3.4) (P51175)
Organism: Mus musculus (Mouse)
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:3346226}; Peripheral membrane protein {ECO:0000269|PubMed:3346226}; Intermembrane side {ECO:0000269|PubMed:3346226}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Ferrochelatase, mitochondrial
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Uroporphyrinogen-III synthase
- Delta-aminolevulinic acid dehydratase
- Porphobilinogen deaminase
- Endonuclease V
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Mitochondrial glycine transporter
Sequence:
MGRTVIVLGGGISGLAASYHLIRGPSPPKVILVEGSKRLGGWIRSIRGSDGAIFELGPRGIRPAGALGARTLLLVSELGLESEVLPVRGDHPAAQNRFLYVGGTLHPLPSGLRGLLRPSPPFSKPLFWAGLRELLKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGQSPQPDSSLIRQARAERWSQWSLRGGLEVLPQALHNHLASKGVTVLSGQPVCGLSLQPEGRWKVSLGDSSLEADHIISAIPASELSKLLPAEAAPLARILSTIKAVSVAVVNLQYRGACLPVQGFGHLVPSSEDPTVLGIVYDSVAFPEQDGNPPSLRVTVMLGGYWLQKLKAAGHQLSPELFQQQAQEAAATQLGLKEPPSHCLVHLHKNCIPQYTIGHWQKLDSAMQFLTAQRLPLTLAGASYEGVAVNDCIESGRQAAVAVLGTESNS
Protein: TATA element modulatory factor (TMF) (Androgen receptor coactivator 160 kDa protein) (Androgen receptor-associated protein of 160 kDa) (P82094)
Organism: Homo sapiens (Human)
Function: Potential coactivator of the androgen receptor. Mediates STAT3 degradation. May play critical roles in two RAB6-dependent retrograde transport processes: one from endosomes to the Golgi and the other from the Golgi to the ER. This protein binds the HIV-1 TATA element and inhibits transcriptional activation by the TATA-binding protein (TBP).
Subcellular location: Cytoplasm. Nucleus. Golgi apparatus membrane. Note=Concentrated at the budding structures localized at the tips of cisternae.
Interaction partners:
- Ras-related protein Rab-6A
- Ras-related protein Rab-6B
- Ankyrin and armadillo repeat-containing protein
- Golgin subfamily A member 4
- GRIP and coiled-coil domain-containing protein 2
- GRIP and coiled-coil domain-containing protein 1
- Vacuolar protein sorting-associated protein 54
- Golgin subfamily A member 1
Sequence:
MSWFNASQLSSFAKQALSQAQKSIDRVLDIQEEEPSIWAETIPYGEPGISSPVSGGWDTSTWGLKSNTEPQSPPIASPKAITKPVRRTVVDESENFFSAFLSPTDVQTIQKSPVVSKPPAKSQRPEEEVKSSLHESLHIGQSRTPETTESQVKDSSLCVSGETLAAGTSSPKTEGKHEETVNKESDMKVPTVSLKVSESVIDVKTTMESISNTSTQSLTAETKDIALEPKEQKHEDRQSNTPSPPVSTFSSGTSTTSDIEVLDHESVISESSASSRQETTDSKSSLHLMQTSFQLLSASACPEYNRLDDFQKLTESCCSSDAFERIDSFSVQSLDSRSVSEINSDDELSGKGYALVPIIVNSSTPKSKTVESAEGKSEEVNETLVIPTEEAEMEESGRSATPVNCEQPDILVSSTPINEGQTVLDKVAEQCEPAESQPEALSEKEDVCKTVEFLNEKLEKREAQLLSLSKEKALLEEAFDNLKDEMFRVKEESSSISSLKDEFTQRIAEAEKKVQLACKERDAAKKEIKNIKEELATRLNSSETADLLKEKDEQIRGLMEEGEKLSKQQLHNSNIIKKLRAKDKENENMVAKLNKKVKELEEELQHLKQVLDGKEEVEKQHRENIKKLNSMVERQEKDLGRLQVDMDELEEKNRSIQAALDSAYKELTDLHKANAAKDSEAQEAALSREMKAKEELSAALEKAQEEARQQQETLAIQVGDLRLALQRTEQAAARKEDYLRHEIGELQQRLQEAENRNQELSQSVSSTTRPLLRQIENLQATLGSQTSSWEKLEKNLSDRLGESQTLLAAAVERERAATEELLANKIQMSSMESQNSLLRQENSRFQAQLESEKNRLCKLEDENNRYQVELENLKDEYVRTLEETRKEKTLLNSQLEMERMKVEQERKKAIFTQETIKEKERKPFSVSSTPTMSRSSSISGVDMAGLQTSFLSQDESHDHSFGPMPISANGSNLYDAVRMGAGSSIIENLQSQLKLREGEITHLQLEIGNLEKTRSIMAEELVKLTNQNDELEEKVKEIPKLRTQLRDLDQRYNTILQMYGEKAEEAEELRLDLEDVKNMYKTQIDELLRQSLS
Protein: choline-phosphate cytidylyltransferase (EC 2.7.7.15) (Q9W0D9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RE24176p
- choline-phosphate cytidylyltransferase
- GH11618p
- diacylglycerol cholinephosphotransferase
- FI05338p
- Glyoxylate reductase/hydroxypyruvate reductase
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MDRMPKEDDESPVSTAPATPTSPMEFKMLPLFMDFEDFSICQPAPFSYDDKAMLELERCDYTQRITYHMARAGKTTRRVRVYADGIYDLFHQGHARQLMQAKNVFPNVYLIVGVCNDELTLRMKGRTVMNGFERYEAVRHCRYVDEIVPNAPWTLNEEFIEEHKIDFVAHDDIPYGAGGVNDIYAPLKAKGMFVATERTEGVSTSDIVARIVKDYDVYVRRNLARGYSAKELNVSFLSEKKFRLQNKMDELKTRGKRELTKVKVDIITKWEEKSREFIDAFLLLFGRERLNTFWNESKGRIIQALSPPGSPNGSVNGDDPDATDDLDSEDEYMELPPDYGSGSCVSLSRKQKRPDKVNASANLNYSEQPEHKDVVDERRSD
Protein: Uncharacterized protein YjcZ (P39267)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Clamp-binding protein CrfC
- Cyclic di-GMP phosphodiesterase PdeH
- Uncharacterized protein YnjH
- Uncharacterized protein YkfB
- Motility protein A
- Methyl-accepting chemotaxis protein IV
- Flagellar protein FliT
- Methyl-accepting chemotaxis protein II
Sequence:
MTKTLLDGPGRVLESVYPRFLVDLAQGDDARLPQAHQQQFRERLMQELLSRVQLQTWTNGGMLNAPLSLRLTLVEKLASMLDPGHLALTQIAQHLALLQKMDHRQHSAFPELPQQIAALYEWFSARCRWKEKALTQRGLLVQAGDQSEQIFTRWRAGAYNAWSLPGRCFIVLEELRWGAFGDACRLGSPQAVALLLGDLLEKATQHLAESINAAPTTRHYYHQWFASSTVPTGGEHADFLSWLGKWTTADKQPVCWSVTQRWQTVALGMPRLCSAQRLAGAMLEEIFSVNLA
Protein: Uncharacterized protein (Q585S6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKHMPFREIAQLCCRLQSSQGNDTRIQSAVIDSIRSQVLDGSTLPLVMQRLVKDGNWKLALCVIKSHHLDKAGIRRDHNIWPIMERAAPCDESRSAMRKALITLFASTCCFHRRS
Protein: Aldehyde oxidase GLOX (EC 1.2.3.1) (Glyoxal oxidase) (VpGLOX) (Q3HRQ2)
Organism: Vitis pseudoreticulata (Chinese wild grapevine)
Function: Catalyzes the oxidation of aldehydes to the corresponding carboxylate by coupling the reaction to the reduction of dioxygen to hydrogen peroxide. Substrates include glyoxal and other aldehydes (By similarity). Involved in disease resistance against the grapevine powdery mildew E.necator. Is sufficient to confer disease resistance to E.necator. Can produce hydrogen peroxide in response to E.necator infection, and this may directly play a role in the defense mechanism during plant-pathogen interactions.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:23090239}.
Interaction partners:
Sequence:
MILDAAIVALADLPGTWELIVPNAGIASMHTAVTRYGTVVLLDRTNIGPSRKMLPKGHCRYDPKDEVLKRDCYAHSVILDLNTNKIRPLKILTDTWCSSGQFLPDGSLLQTGGDLDGVKKIRKFVPCGPHGFCDWEELKDVELETGRWYATNQILPDGSVIIVGGRAANSVEYYPPRKGGAVQLPFLSDVEDKQMDNLYPYVHLLPNGHLFIFANNKAVMYDYTSNKVMLEYPPLDGGPRNYPSAGSSVMLALEGDYSMAIIVVCGGAQFGAFIQKSTDTPAHGSCGRIVATSPHPVWEMEDMPFGRIMGDMVMLPTGDVLIINGAQAGSQGFELASSPCFFPLLYRPNQPLGLRFMTLTPGTVPRMYHSTANLLPDGRVLIAGSNPHYFYKFAAEFPTELRIEAFSPEYLFADKANIRPVIDESPEMVRFGEQFDVFVSVSLPVVGSMEVNLASAPFATHSFSQGQRLVKLTVSPTVPDADERYRIVCTAPPGGKIAPPGYYMMFAVNLGVPSVARWVQLVP
Protein: EG:80H7.4 protein (LP12150p) (Rab27, isoform B) (O76901)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Rab proteins geranylgeranyltransferase component A
- Bitesize, isoform I
- Rab GDP dissociation inhibitor
- MAP kinase-activating death domain protein
- Rabphilin, isoform A
Sequence:
MRAAPPEPEPLQLAGSGEQFLVLGDSGVGKTCLLYQYTDGRFHTQFISTVGIDFREKRLLYNSRGRRHRIHLQIWDTAGQERFRSLTTAFYRDAMGFLLIFDLTSEKSFLETANWLSQLRTHAYSEDPDVVLCGNKCDLLQLRVVSRDQVAALCRRYRLPYIETSACTGANVKEAVELLVGRVMERIENAACNREFSLLLTQSRCLPNIAYGQPEDLVRLHDRREEPCSRRNCRNC
Protein: Kinesin-like protein KIF1B (EC 5.6.1.3) (Q60575)
Organism: Mus musculus (Mouse)
Function: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:11389829, ECO:0000305|PubMed:7528108}. Note=Has a plus-end-directed microtubule motor activity and therefore associates with microtubules. {ECO:0000269|PubMed:11389829, ECO:0000269|PubMed:7528108}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:11389829}. Note=Associates with synaptic vesicles and mediates their anterograde transport along axonal microtubules. {ECO:0000269|PubMed:11389829}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion {ECO:0000305|PubMed:7528108}. Note=Associates with mitochondria and mediates their movement along microtubules. {ECO:0000269|PubMed:7528108}.
Interaction partners:
- Disks large homolog 4
- Kinesin heavy chain isoform 5A
- Disks large homolog 1
- Kinesin light chain 2
- KIF-binding protein
- Transmembrane protein 127
- Kinesin light chain 1
- Kinesin-associated protein 3
- Kinesin-like protein KIF21A
Sequence:
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQNRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEEMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLIDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQVGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCLFRSERSNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKKEKEEADLLLEQQRLDYESKLQALQRQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPSEMEKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVASSAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFSSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQDLNSPPQPSRRFFPPPMPLSKPVPATKLNTMNKTTLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAVLSLNIISAKSLKAAHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSVPKSLSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADVESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIVPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMVKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY
Protein: Cellular tumor antigen p53 (H2EHT1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD