wanglab/gogpt-training-data huggingface dataset:
Protein: Pectinesterase inhibitor 7 (Pectin methylesterase inhibitor 7) (AtPMEI7) (Q9SB37)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pectin methylesterase (PME) inhibitor that can target the PME3 and may regulate homogalacturonan methylesterification during plant development.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:Q9STY5}. Secreted, cell wall {ECO:0000269|PubMed:26183897}. Note=Present in hypocotyl cell walls. {ECO:0000269|PubMed:26183897}.
Interaction partners:
- Berberine bridge enzyme-like 11
- Probable pectinesterase/pectinesterase inhibitor 17
- Pectinesterase inhibitor 2
- Pectinesterase inhibitor 1
- Pectinesterase inhibitor 5
- Nucleic acid-binding, OB-fold-like protein
- Cell wall / vacuolar inhibitor of fructosidase 2
- Berberine bridge enzyme-like 8
- Berberine bridge enzyme-like 10
- glucan endo-1,3-beta-D-glucosidase
Sequence:
MARNFELSLILFVLYLSTAAIVMARNLEEESSGDTEFIKASCETTSYPDRCFQSLSSYASEIKKQPRKLAETALAVSIARAKSAKTYVSEMTDYKGITKRQHEAVADCLEEMGDTVDRLSNSLKELKHLEEGDSGEDFWFCLSNVRTWTSAALTDETACMDGFGGKAMAGELKSLIRTHIVSVAEETSNALALINDFASKH
Protein: Aryl hydrocarbon receptor nuclear translocator (ARNT protein) (Class E basic helix-loop-helix protein 2) (bHLHe2) (Dioxin receptor, nuclear translocator) (Hypoxia-inducible factor 1-beta) (HIF-1-beta) (HIF1-beta) (P27540)
Organism: Homo sapiens (Human)
Function: Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (Probable). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription.
Subcellular location: Nucleus {ECO:0000305|PubMed:34521881}.
Interaction partners:
- Hypoxia-inducible factor 3-alpha
- Histone acetyltransferase p300
- Hypoxia-inducible factor 1-alpha
- Aryl hydrocarbon receptor
- Endothelial PAS domain-containing protein 1
- Neuronal PAS domain-containing protein 4
- Aryl hydrocarbon receptor
- Aryl hydrocarbon receptor nuclear translocator 2
- CREB-binding protein
- Single-minded homolog 2
Sequence:
MAATTANPEMTSDVPSLGPAIASGNSGPGIQGGGAIVQRAIKRRPGLDFDDDGEGNSKFLRCDDDQMSNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGSSSVDPVSVNRLSFVRNRCRNGLGSVKDGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNVCQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKNQEWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIQRPQLGPTANLPLEMGSGQLAPRQQQQQTELDMVPGRDGLASYNHSQVVQPVTTTGPEHSKPLEKSDGLFAQDRDPRFSEIYHNINADQSKGISSSTVPATQQLFSQGNTFPPTPRPAENFRNSGLAPPVTIVQPSASAGQMLAQISRHSNPTQGATPTWTPTTRSGFSAQQVATQATAKTRTSQFGVGSFQTPSSFSSMSLPGAPTASPGAAAYPSLTNRGSNFAPETGQTAGQFQTRTAEGVGVWPQWQGQQPHHRSSSSEQHVQQPPAQQPGQPEVFQEMLSMLGDQSNSYNNEEFPDLTMFPPFSE
Protein: Nuclear pore complex protein Nup85 (85 kDa nucleoporin) (Nucleoporin Nup85) (Q68FJ0)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (By similarity). Involved in nephrogenesis (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9BW27}. Nucleus membrane {ECO:0000250|UniProtKB:Q9BW27}.
Interaction partners:
Sequence:
MEELDVDPAETPIPGLGQQNRHIGFSWGPGDLLLYETLYQKQGNSETAARCPFMYLVRSDEDIYSPVLRKLFNESHSIFVGLQKSAEEASGKSRKAQLVQVSRNYRSVLRACMEEMHTLSESTRETAQKYISQISILSAMELSWNLCEILFIESAPAGPLLILLLEWVRLHVCEVDNIVQDVLRSEKPTEHEKFWDGVTGYVLQGRMNEARQLLAKEASTSASARSMCRVLDDLLKKMPMLHTGGTQTLTEFELKWQHWREECERHLQNGTFSSNVHMEAVCRVLLGDEEVLLEKRDLMTTWYHFLVSRLLFKHPTVKPTELHFYAQSSLDMFLAGDSCPEPLDNILLAAFEFDIHQVIKEFSIVSSNWWFVAHLTDLLDHCQLFQAHNLYFGANMREFLLLDYASGLFSHHSLWQLGVDYFDYCPNLGREYLKLHMERIPLSTEKKALKALRICEQRQMTEQVRSICKTMAMQSLCNRRLGSALSWSIRAKDAAFATLISDRFLKEYCERGNFTDLDLIDNLGSAMLLSDRLTFLGKYREFHRMYSQEQFSEAASLLLSLMTARIAPCSFWLTLLLDALPLLEQKQVIFSAEQTYELMRCLEDRMAAKLESTSPDEIQKQDSSIDNTKVEMLRLALARNLARAIVTEGALQE
Protein: Mediator complex subunit 8 (D3ZM37)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 15
Sequence:
MAHVTYLSFLEVHSRENAKWNKNQHQVSFNASLPAVSVDGSLHSQVICAELSNEIIFCSRLI
Protein: Rho GTPase activating protein at 19D, isoform D (X2JEI9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLQNSNGAAAAHSAASAVATPAAAASAAAAAAAAAVAAAANNAALAASSIQPKLIVIRRRPNQGFGFTLRHFIAYPPEDDQASSSASGLVSGSATAATAASVSTNWPQEASSAAGSNSGSSSSVGVAGITGLEPTSPTSLPPYQVKAMETIFIKEVQANGPAHYANLQTGDRVLMVNNQPIAGIAYSTIVSMIKQTPAVLTLHVVPKECDVLQMHYTSIAHTPESNRLTMSTHSPSLLANGSHKTTFPAAAAVAAPPHQHQQQQQQLISYPAVAAVTTSTPAGSPQSQSQSQSHSHPNTHHAPSLHGGSRSGSITSTASGGITVLSQPFYPQQQQQQQQQQQHRHPALTGGSSSIDFGDMAHGLRQHQQQQQHLYQQQQQHHQFMRANQPPNLTVLSASSATNTPTPTARQPKSATSHNQALYAVGAGPSSAAGSGSGSLSGGSENSDLMIRLRESIKQKEEFLKSPVPASMSSASSINGNQAQSSSPAQQQHLQQHQQHFFPSHTPPGGVQVVVPPPRSRHQVMLKQQQQQQQQHQQHHVLGYDMYHSGGKLVQRSSTAPGSVCHQHQQQQQHHLYHQQQHQQLQQTQHRQVMINNNAKYAKDLDYFETLQETGVTNKVFERKLVSHMSKGFDPFKPLSINTSALESSASTSSTSATTTVKKQSVLYESLQQHPLAKYHQTQQQTTTTTTVDGQTSSRMELHKATLANATIDPVPVGSSKFVTLPDKPDKGSSVATLADIAESSAAAIVDSASGSGNVVRRYKPLSSSSFDEGKPMRRISYLRATNNETDFNAEAAAGGDAAATGASGPASASAASSAPGPTPSSAPAPAPAPAPLPISIPIPVAAVVEPQKTKSLVEEHPDPTYDVIGGTGGGHEFIETPNGLEDVRLSAHGSRRASMSSDMRSSIHIDAELNGKYVPNELEAFETEIEIKSSCINGKRMSEYRSWRQVKLEIKGDLLRIYSGRHAKSEHNVIELDIRNFKFFDESMDKKKYLIRMQSKPSPSGAHLASLGNELNLDEGHDKLLTSSGSSSANEPAANAASALTASTSSSTCSSGPYTEILFKTKSSNEMKRLFGLLQWKDSLNYDDNEHQPQGKQLAEPQKTVASASYLDDVQGGASAADSSPLSSHSGGIADASGSHHVSALPAAAAIVAATSDSISPVMKARKSSSHKHIPDKDLGSPKSKNWKDLLFRRGGSGSGGVSHHDLASPSACAAKQIGSIGVPLRSCPMSKVNAYVPHLVEVCTNIVETKGLGVVGIYRIPGNKAAISELSELVNTKDFQFESCASDDRWEDVNVVSSLLKLFIRSLPDALMPASYYINFIEADKKFGLERIVLLREIVESLPRHPYETMKHLIRHLCRVSGNCDVNRMEPKNLAIIFGPSIIRTPNDTLETAVKDMKHQCRIVELLVTQYDYFFEGGSLPDIAEVSGGTAAVSAAQPQQQTQEDQTSMLLHNLSKIERITERETTRTSRFMPQLRRKTHGKRSAVNSDTYSGESVLVSGSSSNTTTTTTTTTHTTSSTSSSNTITTTISTTTIQQRRAQRKAVQSICDQALILLLPTPVSSVSLPFQSLDYAKASASASASASSTASTSSSSTLHSGGKASASSSSSSTTKFSSSSSSACSTTAVAISSSISATSSKLLSANFKKRSTGGFLGSRSSHQTRKASLDEKDSGQSSGSLGHSLGVGINLAKEQQRSSVDISILLTDDDSSSRLSDTGSMSLTTITDTLDSKLRNLRSGSESNDENGSPEFPKNRRHTLGQPLHMHSENIPYADESPERLFHQFCNPLETAPLSLHLSRSCTATNTIGGDEKPSKQSGGVAPLPPSLLKAAHKLQHSATVPIHQGSSTAPTSGAATPVGTPTGSGGAGAIPSRSSSSSVTTLTKSIQPRFSNYLSYERGNAAAGGAERVVGSAGGAASDDDSEGSTTSDPKEKLLLGERPSPSFFIERYNKKRRDHRLFRSASFNCRNYSTRHITAQTSGGVAAGVSGGVAGAVAVGVACCQALSTTGLTKDEKTDMNLTKKRQIQNKQNRSIKRRHTVGGPHDYSASNGGCSNHSHGHDLAAINYNHHNRHHQQQLLKLGSATSGGGGSGAAAAETTTTTTTTTTVLRRLGTGQAGAEASVALPASSSGSSSNNNNSPQSDGSNGNGGGVAGVASNAPPTGVGVGGNNSSGSSSNSSSTSTTPAGNGDQVLEVGIRIKNISRGRF
Protein: Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9) (EC 3.4.24.-) (Cellular disintegrin-related protein) (Meltrin-gamma) (Metalloprotease/disintegrin/cysteine-rich protein 9) (Myeloma cell metalloproteinase) (Q13443)
Organism: Homo sapiens (Human)
Function: Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:8647900}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:12054541}.
Interaction partners:
- Sorting nexin-9
- Mitotic spindle assembly checkpoint protein MAD2B
- Protein kinase C and casein kinase substrate in neurons protein 3
- Endophilin-A1
- Mitotic spindle assembly checkpoint protein MAD2A
- Amyloid-beta precursor protein
Sequence:
MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT
Protein: Histidine protein methyltransferase 1 homolog (EC 2.1.1.85) (Arsenic-transactivated protein 2) (AsTP2) (Methyltransferase-like protein 18) (O95568)
Organism: Homo sapiens (Human)
Function: Protein-L-histidine N-tele-methyltransferase that specifically monomethylates RPL3, thereby regulating translation elongation. Histidine methylation of RPL3 regulates translation elongation by slowing ribosome traversal on tyrosine codons: slower elongation provides enough time for proper folding of synthesized proteins and prevents cellular aggregation of tyrosine-rich proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:33693809}. Nucleus {ECO:0000269|PubMed:33693809}. Nucleus, nucleolus {ECO:0000269|PubMed:33693809}.
Interaction partners:
- Large ribosomal subunit protein uL3
- Protein N-lysine methyltransferase METTL21A
- Protein N-lysine methyltransferase METTL21D
- Methyltransferase-like protein 22
Sequence:
MTFQFNFTIEDHLENELTPIRDGALTLDSSKELSVSESQKGEERDRKCSAEQFDLPQDHLWEHKSMENAAPSQDTDSPLSAASSSRNLEPHGKQPSLRAAKEHAMPKDLKKMLENKVIETLPGFQHVKLSVVKTILLKENFPGENIVSKSFSSHSDLITGVYEGGLKIWECTFDLLAYFTKAKVKFAGKKVLDLGCGSGLLGITAFKGGSKEIHFQDYNSMVIDEVTLPNVVANSTLEDEENDVNEPDVKRCRKPKVTQLYKCRFFSGEWSEFCKLVLSSEKLFVKYDLILTSETIYNPDYYSNLHQTFLRLLSKNGRVLLASKAHYFGVGGGVHLFQKFVEERDVFKTRILKIIDEGLKRFIIEITFKFPG
Protein: Beta-1,4-galactosyltransferase 7 (EC 2.4.1.133) (Proteoglycan UDP-galactose:beta-xylose beta1,4-galactosyltransferase I) (Xylosylprotein beta 4-galactosyltransferase) (Q9VBZ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:12244071}; Single-pass type II membrane protein {ECO:0000255|RuleBase:RU368121}.
Interaction partners:
- Hexosyltransferase
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase I
- Xylosyltransferase oxt
- Hexosyltransferase
- UDP-glucuronic acid decarboxylase 1
Sequence:
MVNISTINWVFVCGLSFCLGGIAVLSLMPLGSDCVCPLSNPLAKLAGGGEGVSVIKKEPADEKQPQPHDHGASVHKMALLVPFRDRFEELLQFVPHMTAFLKRQGVAHHIFVLNQVDRFRFNRASLINVGFQFASDVYDYIAMHDVDLLPLNDNLLYEYPSSLGPLHIAGPKLHPKYHYDNFVGGILLVRREHFKQMNGMSNQYWGWGLEDDEFFVRIRDAGLQVTRPQNIKTGTNDTFSHIHNRYHRKRDTQKCFNQKEMTRKRDHKTGLDNVKYKILKVHEMLIDQVPVTILNILLDCDVNKTPWCDCSGTAAAASAVQT
Protein: At1g16290 (Transglycosylase) (A1L4W6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MANSFTFWNDCVEPEDLEEMWMDPAVSAEWIDVGETKGQKVHLSRDPDGQPYLTQTEMRAVSDITVRRHFDSILDSEMICAIAELESDRKPLIMRYSKKTKETGLGILQVFEKTAAWLAGGQGYQAYNVDDNPDLLHKPFINVYFGAAYLKWLTDYQNNQRSEEFVVRAYNGGTKKATHKSTLPYWKRYLAVKESLPSRKHGDAGPSSFRPTNPASPGSNTDFTYWDSRASPEDMEDMWNQSEICKEWTKSKEERGKVRFSQDGEKRPYLSRGELKAVAEIIVSKYFSTKGIRVPLVCAIADTVCMRFVNGIKKHVGILGVDYSTASWLYSELGYRAYRVDSADDLTKPFISMYFGVAYLVWLSEYEGSQRSNQFIVQAYMKGPDHVDLEESCPLWLKFEQALSYYEESKRDSGSCVIL
Protein: T. brucei spp.-specific protein (Q38BV2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGNCLCCRDKHKHEPEPEVVMDVMDVKEKQEIGHHNKTQVSTPPTCQSDYPPPSGLPTSPPDDTQSSVSPRDNVQFATAPPDDSSNAASPRYDEQPVTTLSHDVVSSTPPRVETPPTSSPREEVTDVVPAIEEFTPAVSLGEEVVVSEASPAENPFTASPHDDTTATGSRGDNPFTASRDNAEYDFSPREDVNHPPQDKPEVVLAYDFSAPVASVYKNAAVWTFTAPKEEKSGNRVVGFASAERGPRGDVPPSTERVSEKPSGRADEDFDTDETTTGRSSKPVDAADDRAPKLRAPLLAPPVDDTVMESEEAAEEREAQVFTEAAKEGNESVGKEPPGGEGDTYQVSDAVELGDAMESTNEPEVKEIGQADVEKLKGAGTPEKADDEEESPRTSGRRDNNVLSPLLEDKAPAVLAVAGENNDETNAFVHSAERALEQSKVGKDSEENSELEGEHPSEEGLGDVSYANTAGDLPESVAYTTHSSAELQTRKTEGSHAITDGETVRKSDSNDNALAGIIRRQRDMERRSSTGVLLPTQSDALGFLETHSSGVAEHDLVNTGVEGEDNTDGKMQYLQGELSLDFGGLETFNADNMSENRVHSWSSVESNGGAEDRGERGASGLNNEGNDRTVGGCVDSGSSDGGSERRRLADIVQPKDWGREIHEEEEVTEKYSVEEVVADKEKSAEDRVSYNEDFGVNRSNELFNGREAFFQDEKTESKSRSTSVPYRTIPIISPPLATPQNREDGDESLM
Protein: Non-specific lipid-transfer protein (Q9M6B7)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASSMSLKLTCVVVFCMVVGAPLAQGAISCGQITSALAPCIAYLKGNGAGSAPPACCNGIRSLNSAAKTTPDRQAACSCIKSAATGISGINYSTAAGLPGKCGINIPYKISPSTDCKSIK
Protein: Glycine cleavage system P protein (EC 1.4.4.2) (A0A8I6AWV3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU364056}.
Interaction partners:
Sequence:
MLQALGLASIDELIEKTVPASIRLKRPLKLEDPVCENEILETLHAIASKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWVTQYTPYQPEVSQGRLESLLNYQTMVSDITGLDMANASLLDEATAAAEAMQLCHRHNKRKRFFIDPRCHPQTIAVVQTRAKYRGVIVELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQTGSLTCCATDLLALCILRPPGEFGVDIALGNSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLQHIAKRVHNATLILSEGLKRAGHQLQHDLFFDTLKVQCGCSLKEVLGRAAQRQINFRLFDDGTLGISLDETVTEKDLDDLLWIFGCESSTELVAEGMGEEWRGLLGSSFKRTSPFLTHQVFNSYHSETNLVRYMKKLENKDISLVHSMIPLVAPITWREFANIHPFVPLDQAQGYQQLFQELEKDLCELTGYDRVSFQPNSGAQGEYAGLATIRAYLDQKGERHRTVCLIPKSAHGTNPASAYMAGMKIQPVEVDRYGNIDVAHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCALIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLVPFLPSHPIVCLKPNEDTWPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKEATEIAILNANYMAKRLERYYRVLFRGARGYVAHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVAGTLMIEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSRWDRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
Protein: Protein CHUP1, chloroplastic (Protein CHLOROPLAST UNUSUAL POSITIONING 1) (Q9LI74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.
Subcellular location: Plastid, chloroplast outer membrane {ECO:0000269|PubMed:14615600, ECO:0000269|PubMed:18193273, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18715957}; Peripheral membrane protein {ECO:0000269|PubMed:14615600, ECO:0000269|PubMed:18193273, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18715957}; Cytoplasmic side {ECO:0000269|PubMed:14615600, ECO:0000269|PubMed:18193273, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:18715957}.
Interaction partners:
- Kinesin-like protein KIN-14A
- Kinesin-like protein KIN-14B
- Phototropin-2
- Phototropin-1
- Protein WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1
- J domain-containing protein required for chloroplast accumulation response 1
- Outer envelope membrane protein 7
- Protein PLASTID MOVEMENT IMPAIRED 1
- Uncharacterized protein At1g66480
- Protein PLASTID MOVEMENT IMPAIRED 1-RELATED 1
Sequence:
MFVRIGFVVAASIAAVTVKRLNVKPSKPSKPSDNGEGGDKEQSVDPDYNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDYLDDDILPEFEDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEVNNLKHNNEDLLKQVEGLQMNRFSEVEELVYLRWVNACLRYELRNYQTPAGKISARDLSKNLSPKSQAKAKRLMLEYAGSERGQGDTDLESNYSQPSSPGSDDFDNASMDSSTSRFSSFSKKPGLIQKLKKWGKSKDDSSVQSSPSRSFYGGSPGRLSSSMNKQRGPLESLMIRNAGESVAITTFGQVDQESPGTPETPNLPRIRTQQQASSPGEGLNSVAASFHVMSKSVDNVLDEKYPAYKDRHKLAVEREKHIKHKADQARAERFGGNVALPPKLAQLKEKRVVVPSVITATGDQSNESNESNEGKASENAATVTKMKLVDIEKRPPRVPRPPPRSAGGGKSTNLPSARPPLPGGGPPPPPPPPGGGPPPPPGGGPPPPPPPPGALGRGAGGGNKVHRAPELVEFYQSLMKRESKKEGAPSLISSGTGNSSAARNNMIGEIENRSTFLLAVKADVETQGDFVQSLATEVRASSFTDIEDLLAFVSWLDEELSFLVDERAVLKHFDWPEGKADALREAAFEYQDLMKLEKQVTSFVDDPNLSCEPALKKMYKLLEKVEQSVYALLRTRDMAISRYKEFGIPVDWLSDTGVVGKIKLSSVQLAKKYMKRVAYELDSVSGSDKDPNREFLLLQGVRFAFRVHQFAGGFDAESMKAFEELRSRAKTESGDNNNNNNNNSNEEESVN
Protein: Phosphopantothenoylcysteine decarboxylase subunit SIS2 (Halotolerance protein HAL3) (Sit4 suppressor 2) (P36024)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance. Also modulates the expression of the ENA1 ATPase.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphopantothenoylcysteine decarboxylase subunit VHS3
- Serine/threonine-protein phosphatase PP-Z1
- Coenzyme A biosynthesis protein 3
- Dephospho-CoA kinase CAB5
- Phosphopantothenate--cysteine ligase CAB2
- Phosphopantetheine adenylyltransferase
- Serine/threonine-protein phosphatase PP-Z2
- Serine/threonine-protein phosphatase PP1-1
- Sodium/potassium exporting P-type ATPase 1
- Na
Sequence:
MTAVASTSGKQDADHNQSIECPRFSRGQKEILLDHEDAKGKDSIINSPVSGRQSISPTLSNATTTTTKSIMNATGTSGAVVSNTPEPGLKRVPAVTFSDLKQQQKQDSLTQLKNDSERTKSPNSNPAPVSNSIPGNHAVIPNHTNTSRTTQLSGSPLVNEMKDYDPKKKDSALKIVDTMKPDKIMATSTPISRENNKVTAKAPTSITLRKEDAQDQANNVSGQINVRSTPEETPVKQSVIPSIIPKRENSKNLDPRLPQDDGKLHVLFGATGSLSVFKIKPMIKKLEEIYGRDRISIQVILTQSATQFFEQRYTKKIIKSSEKLNKMSQYESTPATPVTPTPGQCNMAQVVELPPHIQLWTDQDEWDAWKQRTDPVLHIELRRWADILVVAPLTANTLSKIALGLCDNLLTSVIRAWNPSYPILLAPSMVSSTFNSMMTKKQLQTIKEEMSWVTVFKPSEKVMDINGDIGLGGMMDWNEIVNKIVMKLGGYPKNNEEEDDDEDEEEDDDEEEDTEDKNENNNDDDDDDDDDDDDDDDDDDDDDDDDEDEDEAETPGIIDKHQ
Protein: Multiple antibiotic resistance protein MarA (P0ACH5)
Organism: Escherichia coli (strain K12)
Function: May be a transcriptional activator of genes involved in the multiple antibiotic resistance (Mar) phenotype. It can also activate genes such as sodA, zwf and micF.
Interaction partners:
- Multiple antibiotic resistance protein MarR
- Multiple antibiotic resistance protein MarB
- Arabinose operon regulatory protein
- HTH-type transcriptional regulator AcrR
- Outer membrane protein TolC
- Multidrug efflux pump subunit AcrA
- Small ribosomal subunit protein uS4
- Outer membrane porin F
- Redox-sensitive transcriptional activator SoxR
- DNA gyrase subunit A
Sequence:
MSRRNTDAITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTFKNYFDVPPHKYRMTNMQGESRFLHPLNHYNS
Protein: Macro domain-containing protein (Q57ZT5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- E2 ubiquitin-conjugating enzyme
- ATP-dependent RNA helicase
Sequence:
MKRERGGRADPFEFVTYSGEEIKESSSEERVKEGANKSSPTRTRILSVALSPAERAIFDVPIENWLSIDRSSLSGWKCAVPRPVTIEQLRPVDPSDAILRHIALYRGPVTDLQLDAIVNAANTRCLGGGGVDGAIHRVAGPLLLRECATFNGCQTGECRLTKGYQLPARYVLHTVGPVGEKPDMLRKCYRSILSLALKNGLRSIGFCCVSTGVYGYPLLPATRIALGETRKFLEEHGGALDMCCFACFQEDEYKTYEKCVGRSSL
Protein: Geminin coiled-coil domain-containing protein 1 (xGEMC1) (D3YN49)
Organism: Xenopus laevis (African clawed frog)
Function: Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating topbp1- and cdk2-dependent recruitment of cdc45l onto replication origins.
Subcellular location: Nucleus {ECO:0000269|PubMed:20383140}. Note=Associates with chromatin during pre-replication complex (pre-RC) formation following interaction with topbp1.
Interaction partners:
Sequence:
MNTILTCQDEYFAGGLGYDCPYFSSTSASTVDVSKETWVSLWASGLLDNRSSNHGPHTQGQLYNMGNSLQEDYLFGDQLSSQISANKQLQDTLLQKEEELSRLHEENNKLKEFLNSAFVKTLAEKTKKLLHQNGQSSFCTNPNSRVPFSSNSTPGSKAKRARRNLYGELTACEAQSSPVVEKWVLQTLGLKDVDTIDDSALANYSAMSLQPKQDSPSSGYSSAHLTPGHSQAATSCSLSPSQCSSASLPESETASPLSSPTYHTPDVAPNKTEVAFSTSLHPHCNVKTHSFPQGQAFVRRDTQGGWKFTWVPKQSE
Protein: RELA proto-oncogene, NF-kB subunit (A0A8I6A5H5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LSDLFPLIFPSEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLTPVLSHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFNGPTEPRPPPRRIAVPSRGPTSVPKPAPQPYAFSTSLSTINFDEFSPMVLPPGQISNQALALAPSSAPVLAQTMVPSSAMVPSLAQPPAPVPVLAPGPPQSLSAPVPKSTQAGEGTLSEALLHLQFDADEDLGALLGNNTDPGVFTDLASVDNSEFQQLLNQGVAMSHSTAEPMLMEYPEAITRLVTGSQRPPDPAPATLGTSGLPNGLSGDEDFSSIADMDFSALLSQISS
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) [Cleaved into: Ghrelin; Obestatin] (Q9GKY5)
Organism: Sus scrofa (Pig)
Function: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Growth hormone secretagogue receptor type 1
- Leptin
- Pro-glucagon
- Membrane bound O-acyltransferase domain containing 4
- Cholecystokinin
- Insulin
- Somatotropin
- Peptide YY
- Pro-neuropeptide Y
- Agouti-related protein
Sequence:
MPSTGTICSLLLLSVLLMADLAMAGSSFLSPEHQKVQQRKESKKPAAKLKPRALEGWLGPEDSGEVEGTEDKLEIRFNAPCDVGIKLSGAQSDQHGQPLGKFLQDILWEEVTEAPADK
Protein: Pulmonary surfactant-associated protein A2 (PSP-A) (PSPA) (SP-A) (SP-A2) (35 kDa pulmonary surfactant-associated protein) (Alveolar proteinosis protein) (Collectin-5) (Q8IWL1)
Organism: Homo sapiens (Human)
Function: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.
Subcellular location: Secreted {ECO:0000269|PubMed:26792177, ECO:0000269|PubMed:32855221}. Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Interaction partners:
Sequence:
MWLCPLALTLILMAASGAACEVKDVCVGSPGIPGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF