wanglab/gogpt-training-data huggingface dataset:
Protein: Pre-hexon-linking protein IIIa (Capsid vertex-specific component IIIa) (CVSC) (Protein IIIa) (pIIIa) [Cleaved into: Hexon-linking protein IIIa] (P12537)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Structural component of the virion that acts as a cement protein on the capsid exterior and which mediates the interactions between the hexons, including the peripentonal hexons, and reaches all the way to the penton vertices. Two hexon linking proteins IIIa, one from each facet, stabilize the unique edge interface between a pair of facets. As the virus enters the host cell, hexon linking proteins IIIa are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in the serotype specificity of the packaging of viral DNA via its interaction with packaging protein 3.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:18786542, ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000305}. Note=Surrounds the border of each facet on the capsid exterior. Present in around 60 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04047, ECO:0000269|PubMed:25071205}.
Interaction partners:
Sequence:
MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPEGNDGFLWDDIDDSVFSPQPQTLLELQQREQAEAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNPFAHLRPRLGRMF
Protein: F-box protein ETP2 (EIN2 targeting protein 2) (Q9LJ74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negative regulator of EIN2 protein stability.
Interaction partners:
- Ethylene-insensitive protein 2
- EIN3-binding F-box protein 1
- Serine/threonine-protein kinase CTR1
- ETHYLENE INSENSITIVE 3-like 1 protein
- Protein ETHYLENE INSENSITIVE 3
- EIN3-binding F-box protein 2
- Ethylene receptor 1
- Protein EIN4
- Ethylene receptor 2
Sequence:
MKTIQEQLPNDLVEEILCRVPATSLRRLRSTCKAWNRLFKGDRILASKHFEKSAKQFRSLSLRNDYRIFPISFNLHGNSPSLELKSELIDPHSKNSAAPFEISRVIHCEGLLLCSSQLDESRVVVWNPLTGETRWIRTGDFRQKGRSFDVGYYYQKDKRSWIKSYKLLCYYRGTKYFEIYDFDSDSWRILDDIIAPRGSIGYSELSVSLKGNTYWFAKGVTEERPRTISLLKFDFYTEKSVPVLLPYQSRRLFQASSLSVVREDKLSVLLQLDQSSKTEIWVTNVIDETTKGAVSWTKVLALDLSPHLQIGNDGSFFLGEDKKVVMFCEKLIDENKVKDMVYIVGEDNVVTEVGFGVDEMDGCRAVILNYVPSLVQIERAGGNRKRGH
Protein: Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) (P70697)
Organism: Mus musculus (Mouse)
Function: Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway. Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (By similarity). In vitro also decarboxylates pentacarboxylate porphyrinogen I.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12297827}.
Interaction partners:
- Protoporphyrinogen oxidase
- Uroporphyrinogen-III synthase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Porphobilinogen deaminase
- Ferrochelatase, mitochondrial
- Delta-aminolevulinic acid dehydratase
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- 5-aminolevulinate synthase, non-specific, mitochondrial
- Mitochondrial glycine transporter
Sequence:
MEANGFGLQNFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPGKGPSFPEPLREERDLERLRDPAAAASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGSSSTMAQAKRWLYQRPQASHKLLGILTDVLVPYLIGQVAAGAQALQLFESHAGHLGTELFSKFALPYIRDVAKRVKAGLQKAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARERVGKAVTLQGNLDPCALYASEEEIGRLVQQMLDDFGPQRYIANLGHGLYPDMDPERVGAFVDAVHKHSRLLRQN
Protein: Cytochrome c oxidase subunit 6b-1 (AtCOX6b-1) (Q9S7L9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. This protein may be one of the heme-binding subunits of the oxidase.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Cytochrome c oxidase subunit 6a, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 5b-2, mitochondrial
- Cytochrome c oxidase subunit 5b-1, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
Sequence:
MADAVNAQTPSLSEQYHLEKEVKQDTSAKPVEVKEVAPEVTTQAEEVKTEQAKEESPVEEAVSVVEEKSESAPESTEVASEAPAAAEDNAEETPAAAEENNDENASEEVAEETPDEIKLETAPADFRFPTTNQTRHCFTRYVEYHRCVAAKGDDAPECDKFAKFYRSLCPSEWVDRWNEQRENGTFPGPLP
Protein: Heterogeneous nuclear ribonucleoprotein A/B (A0A8J8XXQ6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIRALLISEAKIRLLPPGDLGFRDFLRLILLFWEAGFASEAPVEPSPGAAAPATPAGSGGGTTAAPSGNQNGAEGDQINASKNEEDAGKMFVGGLSWDTSKKDLKDYFTKFGEVVDCTIKMDPNTGRSRGFGFILFKDSSSVEKVLDQKEHRLDGRVIDPKKAMAMKKDPVKKIFVGGLNPEATEEKIREYFGQFGEIEAIELPIDPKLNKRRGFVFITFKEEDPVKKVLEKKFHTVSGSKCEIKVAQPKEVYQQQQYGSGGRGNRNRGNRGSGGGQGSTNYGKSQRRGGHQNNYKPY
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9LW05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAFYVNDNVDNVIDVKRIYNDYDGELRKSQKLFFDFKVHYTRAEEEDDDVEEEEDFPDFDNLQTLTLEQTHEFDRDWLFGGDGDHSLAIVYHILDSLQVPPYSAIVNTLADEIKDLKKDGAKDVERVQVKIGVTVSRFPGEDDHVDVQVQLAVAPANDEAVEMHLETLVVENEGYCVICMDNIRVGSDVEAGRMPCSHVFHRTCGEEWLRNSGICPVCRALFPA
Protein: REL proto-oncogene, NF-kB subunit (A0A8I5XW27)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
ILSGGYNPYVEIIEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSIQIMNYYGKGKVRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGPERRPLFFQNLGIRCVKKKEVKEAIILRISAGINPFNVPEQQLLDIEDCDLNVVRLCFQVFLPDEHGNFTTALPPIVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEAKGIFSQADVHRQVAIVFRTPPYCRAIVEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDAYGNKSKKQKTTLIFQKLLHFPEKTRAVPLESIGETRFIKKESNLFSHGTVLPETPRSSGVPGQAEPYYSSSGSISNALPHHPSAMPSMVHQPASWSPVTHPTSHPGSTNTLSSFPAGQLSSNSQGVLPFLDGAGMNDLSASNACLFSTDNLARMETPSMSPTDLYSISDVNMLTNRPVSVMTSSTDGMGDTDHPRLVSVNLENPSCNSRLDPRDPRQLHQMSTASMSAAGTSSSSVFVSQSDTFNRPHFSCIDNGLTNEPGLANDAHHPNFAQSSQYSGIDALQSEQLGDSFEYSFFKI
Protein: cAMP-activated global transcriptional regulator CRP (Catabolite activator protein) (CAP) (Catabolite gene activator) (cAMP receptor protein) (CRP) (cAMP regulatory protein) (P0A2T6)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding to regulate transcription. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. Plays a major role in carbon catabolite repression (CCR) (By similarity).
Interaction partners:
- Adenylate cyclase
- RNA polymerase sigma factor RpoD
- RNA polymerase sigma factor RpoS
- DNA-binding protein Fis
- RNA-binding protein Hfq
- Leucine-responsive regulatory protein
- Translational regulator CsrA
- HTH-type transcriptional repressor CytR
- DNA-directed RNA polymerase subunit beta'
- DNA-binding dual transcriptional regulator OmpR
Sequence:
MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSSQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR
Protein: Large ribosomal subunit protein bL32m (39S ribosomal protein L32, mitochondrial) (L32mt) (MRP-L32) (Q9BYC8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL22m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS12m
- Elongation factor Tu, mitochondrial
- Large ribosomal subunit protein uL13m
Sequence:
MALAMLVLVVSPWSAARGVLRNYWERLLRKLPQSRPGFPSPPWGPALAVQGPAMFTEPANDTSGSKENSSLLDSIFWMAAPKNRRTIEVNRCRRRNPQKLIKVKNNIDVCPECGHLKQKHVLCAYCYEKVCKETAEIRRQIGKQEGGPFKAPTIETVVLYTGETPSEQDQGKRIIERDRKRPSWFTQN
Protein: Salt-mediated killer protoxin 1 [Cleaved into: Salt-mediated killer toxin 1 alpha chain (SMK toxin alpha chain); Salt-mediated killer toxin 1 gamma chain (SMK toxin gamma chain); Salt-mediated killer toxin 1 beta chain (SMK toxin beta chain)] (P19972)
Organism: Millerozyma farinosa (Yeast) (Pichia farinosa)
Function: This toxin kills sensitive strains of yeast.
Interaction partners:
Sequence:
MRKETLIGLAFITANVIAWSLRWRMQKSTTIAAIAGCSGAATFGGLAGGIVGCIAAGILAILQGFEVNWHNGGGGDRSNPVKRSSDSFSIVNHNGEKVDSYAHLVPGKVGKVIIDNIELSAIRYANNHTSLGYHFTSDGSGPAARGEATTIWGVGADEAIDKGTPSKNDLQNMSADLAKNGFKGHQGVACSTVKDGNKDVYMIKFSLAGGSNDPGGSPCSDD
Protein: Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein) (Protein E2F TARGET GENE 1) (Q501D5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and may act by promoting the disassembly of the MCM complex from chromatin. Required for sister chromatid cohesion.
Subcellular location: Nucleus {ECO:0000269|PubMed:18528439}. Note=Associates with the replisome complex.
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM2
- Probable DNA helicase MCM8
- Origin of replication complex subunit 2
- Probable DNA primase large subunit
- Proliferating cellular nuclear antigen 1
Sequence:
MGGPAYDCLTNPLGAVRFSFVNALSSGYDPASSVGKDWGVVDLFRHYFSDESAISQVPILDSSSIKWVQPKTLVRFRGMIQDMLGNEFYAGAYKDDSTWRTNKYSDVSQFPEGSSTEIQVWERRLLYCVPVPGKNQWTECSSQELKNRFLDLTGQNREKRVRVDEEMTDSMDSSTLEAGRNGSPFKKMKVGEATSSASESQVPQTSGIPPATSADSLPCLVKIYDSPESDLKLNDVVEFLGVLTFDPIVMMDTDTLDENSDALSEAESVQMPSGKVPRLHCLIHRKLETQHFLHGSSLLPEPKSPQIFKEIRESLMKYLTGLLGNDHIAAQFLLLHLLSKVHGRVDNVAVGKLSLNLIHLNKESMSIFGTQLSGALKSLLPFTQSIPLTIEYLNTASFGPKKDYGINRLMPGVLQIADGTHLILDETELQPGTLNSVGVENANLLKNLLECQKVEYDFQYYKMEMATDVQMLIFSEGKSNIMPADLVLPLQPSQVNSLEVITPETAETWRCYLATCKSLSHSIGQELQQVVENDLVAARQTDRSLGSQDLSRLLTMARMMSVSYGETTLSLEHWQMVLELERLRKERLK
Protein: CUGBP Elav-like family member 4 (M0QY66)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYIKMATLANGQADNASLSTNGLGSSPGSAGHMNGLSHSPGNPSTIPMKDHDAIKLFIGQIPRNLDEKDLKPLFEEFGKIYELTVLKDRFTGMHKGCAFLTYCERESALKAQSALHEQKTLPGMNRPIQVKPADSESRGGSSCLRQPPSHRKLFVGMLNKQQSEDDVRRLFEAFGNIEECTILRGPDGNSKGCAFVKYSSHAEAQAAINALHGSQTMPGASSSLVVKFADTDKERTMRRMQQMAGQMGMFNPMAIPFGAYGAYAQLMQQQAALMASVAQGGYLNPMAAFAAAQMQQMAALNMNGLAAAPMTPTSGGSTPPGITAPAVPSIPSPIGVNGFTGLPPQANGQPAAEAVFANGIHPYPAQSPTAADPLQQAYAGVQQYAGPAAYPAAYGQISQAFPQPPPMIPQQQREGPEGCNLFIYHLPQEFGDAELMQMFLPFGFVSFDNPASAQTAIQAMNGFQIGMKRLKVQLKRPKDANRPY
Protein: Mitochondrial thiamine diphosphate carrier 1 (Q8RXZ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial transporter that mediates uptake of thiamine diphosphate (ThDP) into mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:22426856}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nudix hydrolase 24, chloroplastic
- Hydroxyethylthiazole kinase
- Thiamine pyrophosphokinase 2
- Nudix hydrolase 20, chloroplastic
- Purine-uracil permease NCS1
- Thiamine pyrophosphokinase 1
- Lecithin-cholesterol acyltransferase-like 1
- 5-formyltetrahydrofolate cyclo-ligase-like protein COG0212
- Bifunctional TH2 protein, mitochondrial
- Bifunctional TENA-E protein
Sequence:
MSGTELDEPGKLKRAVIDASAGGVAGAISRMVTSPLDVIKIRFQVQLEPTATWALKDSQLKPKYNGLFRTTKDIFREEGLSGFWRGNVPALLMVVPYTSIQFAVLHKVKSFAAGSSKAENHAQLSPYLSYISGALAGCAATVGSYPFDLLRTVLASQGEPKVYPNMRSAFLSIVQTRGIKGLYAGLSPTLIEIIPYAGLQFGTYDTFKRWSMVYNKRYRSSSSSSTNPSDSLSSFQLFLCGLASGTVSKLVCHPLDVVKKRFQVEGLQRHPKYGARVELNAYKNMFDGLGQILRSEGWHGLYKGIVPSTIKAAPAGAVTFVAYELASDWFEANLT
Protein: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase (Cholesterol dehydrogenase) [Includes: 3-beta-hydroxy-Delta(5)-steroid dehydrogenase (3-beta-HSD) (3BHSD) (EC 1.1.1.145) (3-beta hydroxysterol dehydrogenase) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone reductase); Steroid Delta-isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)] (P9WQP7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: 3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidation and isomerization of cholesterol, pregnenolone, and dehydroepiandrosterone (DHEA) into cholest-4-en-3-one, progesterone, and androsterone, respectively.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17630785}.
Interaction partners:
- Cholesterol oxidase
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
- Exodeoxyribonuclease 7 small subunit
- Exodeoxyribonuclease 7 large subunit
- Uncharacterized protein Rv1109c
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
Sequence:
MLRRMGDASLTTELGRVLVTGGAGFVGANLVTTLLDRGHWVRSFDRAPSLLPAHPQLEVLQGDITDADVCAAAVDGIDTIFHTAAIIELMGGASVTDEYRQRSFAVNVGGTENLLHAGQRAGVQRFVYTSSNSVVMGGQNIAGGDETLPYTDRFNDLYTETKVVAERFVLAQNGVDGMLTCAIRPSGIWGNGDQTMFRKLFESVLKGHVKVLVGRKSARLDNSYVHNLIHGFILAAAHLVPDGTAPGQAYFINDAEPINMFEFARPVLEACGQRWPKMRISGPAVRWVMTGWQRLHFRFGFPAPLLEPLAVERLYLDNYFSIAKARRDLGYEPLFTTQQALTECLPYYVSLFEQMKNEARAEKTAATVKP
Protein: Leucine-rich repeats and immunoglobulin-like domains protein 2 (LIG-2) (O94898)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:15145052}; Single-pass type I membrane protein {ECO:0000269|PubMed:15145052}. Cytoplasm {ECO:0000269|PubMed:15145052}.
Interaction partners:
- Zinc finger protein 621
- Leucine-rich repeats and immunoglobulin-like domains protein 1
- Inactive heparanase-2
Sequence:
MAPAPLGVPEEQLLGCRSRVLSRLLFIAQTALLLLPAAGAGLCPAPCSCRIPLLDCSRRKLPAPSWRALSGLLPPDTAILDFSHNRLSNWNISLESQTLQEVKMNYNELTEIPYFGEPTSNITLLSLVHNIIPEINAQALQFYPALESLDLSSNIISEIKTSSFPRMQLKYLNLSNNRITTLEAGCFDNLSSSLLVVKLNRNRMSMIPPKIFKLPHLQFLELKRNRIKIVEGLTFQGLDSLRSLKMQRNGISKLKDGAFFGLNNMEELELEHNNLTRVNKGWLYGLRMLQQLYVSQNAIERISPDAWEFCQRLSELDLSYNQLTRLDESAFVGLSLLERLNLGDNRVTHIADGVFRFLSNLQTLDLRNNEISWAIEDASEAFAGLTSLTKLILQGNQIKSITKKAFIGLESLEHLDLNNNAIMSIQENAFSQTHLKELILNTSSLLCDCHLKWLLQWLVDNNFQHSVNVSCAHPEWLAGQSILNVDLKDFVCDDFLKPQIRTHPETIIALRGMNVTLTCTAVSSSDSPMSTVWRKDSEILYDVDTENFVRYWQQAGEALEYTSILHLFNVNFTDEGKYQCIVTNHFGSNYSQKAKLTVNEMPSFLKTPMDLTIRTGAMARLECAAEGHPAPQISWQKDGGTDFPAARERRMHVMPEDDVFFIANVKIEDMGIYSCMAQNTAGGLSANASLTVLETPSFIRPLEDKTVTRGETAVLQCIAGGSPAPRLNWTKDDGPLLVTERHFFAAANQLLIIVDAGLEDAGKYTCIMSNTLGTERGHIYLNVISSPNCDSSQSSIGHEDDGWTTVGIVIIVVVCCVVGTSLIWVIVIYHMRRKNEDYSITNTEELNLPADIPSYLSSQGTLSEPQEGYSNSEAGSHQQLMPPANGYIHKGTDGGTGTRVICSDCYDNANIYSRTREYCPYTYIAEEDVLDQTLSSLMVQMPKETYLVHPPQDTTALESLIPSANREPSAFPTNHERISEKKLPSTQMSGETLQRPVWNINRELGLPHPPFSQQPVHESPQLHQNEGLAGREPDCSASSMSCHRLQDHAFDFSRTRNIQDGSEGT
Protein: Na+/Ca2+ exchanger NCX1 isoform (Q8R505)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
HEGDRPASKTEIEMDGKVVNSHVDNFLDGALVLEVDERDQDDEEARREMARILKELKQKHPEKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNMEMAENDPVSKIFFEQGTYQCLENCGTVALTIMRRGGDLSTTVFVDFRTEDGTANAGSDYEFTEGTVIFKPGETQKEIR
Protein: Histamine-gated chloride channel alpha2 subunit (Histamine-gated chloride channel subunit 1 variant) (Histamine-gated chloride channel subunit 1, isoform B) (Histamine-gated chloride channel subunit B) (Q8WS32)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQSPTSKLVEFRCLIALAIYLHALEQSIQHCHCVHGYRNNTESAELVSHYESSLSLPDILPIPSKTYDKNRAPKLLGQPTVVYFHVTVLSLDSINEESMTYVTDIFLAQSWRDPRLRLPENMSEQYRILDVDWLHSIWRPDCFFKNAKKVTFHEMSIPNHYLWLYHDKTLLYMSKLTLVLSCAMKFESYPHDTQICSMMIESLSHTVEDLVFIWNMTDPLVVNTEIELPQLDISNNYTTDCTIEYSTGNFTCLAIVFNLRRRLGYHLFHTYIPSALIVVMSWISFWIKPEAIPARVTLGVTSLLTLATQNTQSQQSLPPVSYVKAIDVWMSSCSVFVFLSLMEFAVVNNFMGPVATKAMKGYSDENISDLDDLKHHRESIIEPQYDTFCHGHATAIYIDKFSRFFFPFSFFILNIVYWTTFL
Protein: RBR-type E3 ubiquitin transferase (EC 2.3.2.31) (Q9LZH2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEESTLVPSGAIYKLYFKGIVIEETSQLLAGFGVAIFDQDDKLLFQMKRPIHGSDITVLEAELTALKQGLTETMKLGLDRISICCDHDHIYELVMGRSTPEQDNIAMLMNDVQRMRQQLRYSNPILVTRDQISFAYKLAMETVVSEISICMPATCSICFNNVLEAEKMFSVAICGHQFCVECVKHYIEVKLLEGGVPRCLDYQCESKLTLTSCGNLLTPKLKAIWKQRIEEELILVAERVYCPNPRCSGLMSKTELSTSTEEDVSTRTCCVKCGEPFCINCKVPWHSNLSCDDYKRLGPNPTKNDIKLKVLANQQKWSQCAKCQHMIARIEGCNVIICRYHHRYIL
Protein: At1g14260 (RING domain protein) (RING/FYVE/PHD zinc finger superfamily protein) (Q4PS45)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSNHHTVVYVNGLVRPVLAEAEYSMRTESPADNAIDIYDGDTTENEEEDSLISSAECRICQDECDIKNLESPCACNGSLKYAHRKCVQRWCNEKGNTICEICHQPYQAGYTSPPPPPQSEETTIDIGGGWRISGLDLDDPRLLAIAEAERQILESEYDDYTASDTSGAAFFRSAALILMTLLLLRHALTIPDYSDSEDDDPSSILSLFLLRAASFLLPCYIMASAISILHRRRQRQEAADLATRFALVLSSRQPRPVINYLSMEP
Protein: Transcription factor MYB80 (MYB-related protein 103) (AtMYB103) (Myb-related protein 80) (AtMYB80) (Protein MALE STERILE 188) (Q9XHV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to the DNA sequence 5'-CCAACC-3'. Regulates directly PME5, UND and GLOX1. Essential for tapetum development in anthers and microsporogenesis. Regulates the timing of tapetal programmed cell death (PCD) which is critical for pollen development. May act through the activation of UND, encoding an A1 aspartic protease. Required for anther development by regulating tapetum development, callose dissolution and exine formation. Acts upstream of A6 and FAR2/MS2, two genes required for pollen exine formation. Negatively regulates trichome endoreduplication and trichome branching.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17727613}.
Interaction partners:
- Transcription factor DYT1
- Short-chain dehydrogenase reductase ATA1
- NAC domain-containing protein 73
- NAC domain-containing protein 12
- NAC domain-containing protein 10
- Cytochrome P450 703A2
- NAC domain-containing protein 43
- Homeobox protein knotted-1-like 7
- NAC domain-containing protein 30
- NAC domain-containing protein 66
Sequence:
MGRIPCCEKENVKRGQWTPEEDNKLASYIAQHGTRNWRLIPKNAGLQRCGKSCRLRWTNYLRPDLKHGQFSEAEEHIIVKFHSVLGNRWSLIAAQLPGRTDNDVKNYWNTKLKKKLSGMGIDPVTHKPFSHLMAEITTTLNPPQVSHLAEAALGCFKDEMLHLLTKKRVDLNQINFSNHNPNPNNFHEIADNEAGKIKMDGLDHGNGIMKLWDMGNGFSYGSSSSSFGNEERNDGSASPAVAAWRGHGGIRTAVAETAAAEEEERRKLKGEVVDQEEIGSEGGRGDGMTMMRNHHHHQHVFNVDNVLWDLQADDLINHMV
Protein: Transcription factor TGA2.1 (OsNIF2) (bZIP transcription factor 63) (OsbZIP63) (Q7X993)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plays a negative role in rice basal defense responses to the bacterial blight pathogen Xanthomomas oryzae pv. oryzae (Xoo). May function in both positive and negative regulation of rice defense genes. Binds DNA in vitro. Acts as transcriptional activator when bound to NPR1/NH1 in vitro. Binds to the promoter sequence of CRK10 in vitro.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- BTB/POZ domain and ankyrin repeat-containing protein NPR1
- Os01g0104800 protein
- Os04g0662100 protein
- Os12g0166500 protein
- U3 small nucleolar RNA-associated protein 18 homolog
- Pre-mRNA-splicing factor SLU7
- DEAD-box ATP-dependent RNA helicase 36
- Os03g0598200 protein
- Os05g0295100 protein
- BTB/POZ domain and ankyrin repeat-containing protein NPR3
Sequence:
MADASSRTDTSIVVDNDDKNHQLENGHSGAVMASNSSDRSDRSDKLMDQKTIRRLAQNREAARKSRLRKKAYVQQLESSKLKLAQLEQELQKARQQGIFISSSGDQTHAMSGNGALTFDLEYTRWLEEQNKQINELRTAVNAHASDSDLRLIVDGIMAHYDEVFKVKGVAAKADVFHILSGMWKTPAERCFLWLGGFRPSELLKLLANHLEPLTEQQLLGLNNLQESSQQAEDALSQGMEALQQSLADTLAGSLGSSGSSGNVANYMGQMAMAMGKLGTLENFLCQADNLRQQTLHQMQRILTIRQASRALLAIHDYFSRLRALSSLWLARPRE
Protein: Heparan sulfate glucosamine 3-O-sulfotransferase 5 (EC 2.8.2.23) (Heparan sulfate D-glucosaminyl 3-O-sulfotransferase 5) (3-OST-5) (Heparan sulfate 3-O-sulfotransferase 5) (h3-OST-5) (Q8IZT8)
Organism: Homo sapiens (Human)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site. Also generates GlcUA-GlcNS or IdoUA-GlcNS and IdoUA2S-GlcNH2. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes simplex virus-1 (HSV-1) and permits its entry.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Atypical chemokine receptor 1
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MLFKQQAWLRQKLLVLGSLAVGSLLYLVARVGSLDRLQPICPIEGRLGGARTQAEFPLRALQFKRGLLHEFRKGNASKEQVRLHDLVQQLPKAIIIGVRKGGTRALLEMLNLHPAVVKASQEIHFFDNDENYGKGIEWYRKKMPFSYPQQITIEKSPAYFITEEVPERIYKMNSSIKLLIIVREPTTRAISDYTQVLEGKERKNKTYYKFEKLAIDPNTCEVNTKYKAVRTSIYTKHLERWLKYFPIEQFHVVDGDRLITEPLPELQLVEKFLNLPPRISQYNLYFNATRGFYCLRFNIIFNKCLAGSKGRIHPEVDPSVITKLRKFFHPFNQKFYQITGRTLNWP
Protein: tRNA (guanine(9)-N1)-methyltransferase (EC 2.1.1.221) (tRNA methyltransferase 10) (tRNA(m1G9)-methyltransferase) (tRNA(m1G9)MTase) (O14214)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus {ECO:0000250|UniProtKB:Q12400}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- Vacuolar import and degradation protein 27
- tRNA pseudouridine synthase 4
- tRNA
- tRNA wybutosine-synthesizing protein 2
- Putative tRNA pseudouridine synthase C16C4.06c
- Putative tRNA pseudouridine synthase C25B8.05
- tRNA
Sequence:
MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN