wanglab/gogpt-training-data huggingface dataset:
Protein: DUF2779 domain-containing protein (Q384Y7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRKKAHSTLVSSVVDAVKKVNDADEPLRHVLRSYREASEPMSDLDECLEGRDGSDNKEKSSEGTTQRATSSAARSPAILTYKGFAASLTCPKKFHLLQNHTDLTSDISIADAVHLDDGAAFNELARRWDRLQFGSRAVVVQEQNFEDAVRRSEEILLKYFQTVYAQLGDQAPALTIHRPAFATPFGGQSRGSQEQQKVQQGGKKGAADIILRARPAVLRFRPKDNQWVILETASALDPAGNPVRLAQYLQRLHFTTVAFRYWITQPHIPIGIRKRFLDIDLDTVTEKNLKGHRLETAAEVAVPLDLKRSGLLHIRQFFPGPVTLMDCDPTRLVKYVQRLSLEDMIDADINNSQRSGSAFGTGEFPSSDEQDITKLQAEVEAMQERGHGRQQWAGSTSNRTAKKREVELRKLFAKQQKLVEALISTRTLRLVEMGREPANAQKWRAFASDTDAVLKATFVDEGESGMLVDDQEDKGKKGKAAKAKQGPTATGKGGGRHCATQIPCVPTYSEFIGAHCSRGDVCPFFAEGLCLPNKFDEPIRQRDNHLFTVPSTAVSRKTTWWLQGLRTVQDVLYQYKKGAVNLTAPQLRYVKAITAGKVFVNPKEIEDFFSRIRYPAFLIDFEATQFALPPFEKVVAFQPLPFQFSLDVFQEDVLNETPTHYDFLHFGKGYSPNEDPRRACIAELMHIVRKERAKKRDAMTASGELARLERLKKQLEEEEFAAVTNARRGRRATKARGPNITKNNPLHEPVNFYDGCFIAHFASFEKSCLEKLGQLVDEYKEEIKQFYFLDTLDLFKRGFVHPNAHGSNSLKKVLPGLCPDFKYGVFGGDAAGDVVDAGEGEGSGGGGRQDEQKGENAMGVYRLWYHHEGGGSLRDLQQTVMQDERRRGIYEGKNKLDTMVQAARPDVRDKAWAMLRIQLLEYCSLDTKALYEIMRQVWLEKESAKGLKPDKGGWVMTDPLPREYRL
Protein: Assimilatory ferredoxin-dependent nitrite reductase (NiR) (EC 1.7.7.1) (Ferredoxin:nitrite reductase) (I3R637)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
Interaction partners:
- Probable nitrate transporter
- Assimilatory nitrate reductase
- Copper-containing nitrite reductase
- Glutamate dehydrogenase
- Glutamate dehydrogenase
- Glutamate dehydrogenase
- Gamma-glutamylputrescine synthetase
- Glutamate--ammonia ligase
- uroporphyrinogen-III C-methyltransferase
- Glutamine synthetase 3
Sequence:
MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSAGKSDHVGVHEQSDGRYYVGLSVAVGRLTAADALELADLADKYGSGKIRLTRRQNPIVMDVPAGALDDLLAEPLLSKHTPEPNPFQRGTVACTGTEFCSLALTETKARTARMLRWLRDNVEVPDDVHQLKIHYSGCTADCGQANTADIGLFGMRAQKDGEMVEAMDIGVGGGIGDEPSFVEWIHQRVPADEVPGAIASLVEAFAAHRTAGQTFRQWVEAEGPDAVAEYCEPIETDFEAPYMHDAKQSWYPFADEDEPPKTEQPMTSD
Protein: Endoplasmin homolog (Glucose-regulated protein 94 homolog) (GRP-94 homolog) (Heat shock protein 90-7) (AtHSP90.7) (AtHsp90-7) (Protein SHEPHERD) (Q9STX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a molecular chaperone role in the processing of secreted materials. Required for shoot apical meristem (SAM), root apical meristem (RAM) and floral meristem (FM) formation, probably by regulating the folding of CLAVATA proteins (CLVs). Also involved in pollen tube elongation. Involved in resistance to tunicamycin- or high calcium-induced ER stresses. Possesses ATPase activity.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250}.
Interaction partners:
- Protein SGT1 homolog A
- Protein SGT1 homolog B
- Calreticulin-2
- Calreticulin-1
- Heat shock 70 kDa protein 17
- Calreticulin-3
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein BIP3
- Cysteine and histidine-rich domain-containing protein RAR1
- Heat shock 70 kDa protein BIP1
Sequence:
MRKRTLVSVLFLFSLLFLLPDQGRKLHANAEESSDDVTDPPKVEEKIGGHGGLSTDSDVVHRESESMSKKTLRSNAEKFEFQAEVSRLMDIIINSLYSNKDIFLRELISNASDALDKIRFLALTDKDVLGEGDTAKLEIQIKLDKAKKILSIRDRGIGMTKEDLIKNLGTIAKSGTSAFVEKMQSSGDLNLIGQFGVGFYSAYLVADYIEVISKHNDDSQYVWESKANGKFAVSEDTWNEPLGRGTEIRLHLRDEAGEYLEESKLKELVKRYSEFINFPISLWASKEVETEVPVEEDESADEETETTSTEEEKEEDAEEEDGEKKQKTKKVKETVYEWELLNDVKAIWLRSPKEVTEEEYTKFYHSLSKDFTDEKPMAWSHFNAEGDVEFKAVLYVPPKAPHDLYESYYNSNKANLKLYVRRVFISDEFDELLPKYLSFLKGLVDSDTLPLNVSREMLQQHSSLKTIKKKLIRKALDMIRKLAEEDPDEIHDDEKKDVEKSGENDEKKGQYTKFWNEFGKSVKLGIIEDAANRNRLAKLLRFETTKSDGKLTSLDQYIKRMKKSQKDIFYITGSSKEQLEKSPFLERLIKKGYEVIFFTDPVDEYLMQYLMDYEDKKFQNVSKEGLKVGKDSKDKELKEAFKELTKWWKGNLASENVDDVKISNRLADTPCVVVTSKFGWSANMERIMQSQTLSDANKQAYMRGKRVLEINPRHPIIKELKDRIASDPEDESVKETAQLMYQTALIESGFILTDPKDFAARIYNSVKSGLNISPDAVADEEIEAAEEPETSEATETKSDDLAGGLNIEAEPVEQQEENTKDEL
Protein: Mucolipin-2 (Transient receptor potential channel mucolipin 2) (TRPML2) (Q8IZK6)
Organism: Homo sapiens (Human)
Function: Nonselective cation channel probably playing a role in the regulation of membrane trafficking events. Acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. May activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway. May play a role in immune processes. In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (By similarity). In the innate immune response, may play a role in the regulation of chemokine secretion and macrophage migration (By similarity). Through a possible and probably tissue-specific heteromerization with MCOLN1 may be at least in part involved in many lysosome-dependent cellular events.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Late endosome membrane {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Lysosome membrane {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Recycling endosome membrane {ECO:0000269|PubMed:17662026}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F6RG56}. Note=Localizes to recycling endosomes in activated macrophages and microglia. {ECO:0000250|UniProtKB:Q8K595}.
Interaction partners:
- Mucolipin-1
- Mucolipin-3
Sequence:
MARQPYRFPQARIPERGSGVFRLTVRNAMAHRDSEMKEECLREDLKFYFMSPCEKYRARRQIPWKLGLQILKIVMVTTQLVRFGLSNQLVVAFKEDNTVAFKHLFLKGYSGTDEDDYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDCVQLDLQDLSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAKIEECKDLNIFGSTQKNAQYVLVFDAFVIVICLASLILCTRSIVLALRLRKRFLNFFLEKYKRPVCDTDQWEFINGWYVLVIISDLMTIIGSILKMEIKAKNLTNYDLCSIFLGTSTLLVWVGVIRYLGYFQAYNVLILTMQASLPKVLRFCACAGMIYLGYTFCGWIVLGPYHDKFENLNTVAECLFSLVNGDDMFATFAQIQQKSILVWLFSRLYLYSFISLFIYMILSLFIALITDSYDTIKKFQQNGFPETDLQEFLKECSSKEEYQKESSAFLSCICCRRRKRSDDHLIPIS
Protein: Protein phosphatase 1 regulatory subunit 1A (Protein phosphatase inhibitor 1) (I-1) (IPP-1) (P01099)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Inhibitor of protein-phosphatase 1. This protein may be important in hormonal control of glycogen metabolism. Hormones that elevate intracellular cAMP increase I-1 activity in many tissues. I-1 activation may impose cAMP control over proteins that are not directly phosphorylated by PKA. Following a rise in intracellular calcium, I-1 is inactivated by calcineurin (or PP2B). Does not inhibit type-2 phosphatases.
Interaction partners:
Sequence:
MEQDNSPRKIQFTVPLLEPHLDPEAAEQIRRRRPTPATLVLTSDQSSPEVDEDRIPNPLLKPSLAMSPRQRKKMTRTTPTMKELQMMVEHHLGQQEQGEEPEGAAEGTGAQESQPPGTPGTGAESRLGPSATAQKPAQPSPRAQERRGEEPSTAKTSQDSQGASAV
Protein: Phospholipid scramblase (Q21318)
Organism: Caenorhabditis elegans
Interaction partners:
- Cell death abnormality protein 8
Sequence:
MNKQPGQQPLRSLSLTSAAKSPEEVEPEQDSKKGEPRAKAAGFGGGGGGGKRLPEARSTPMVIPNQVAAMPVQMTGFVQLVANNILSAIAHTNSVMVVQCIKPLEIFTGFETPNRYVVHDMYCRPLLYCMERSNIFARQYEGNDRNFGMQIMDTHGAQVMTCFRGRPCCSTDDFLSTQFLDQQIGMMKKECCNPNFELVGSGCNQPLLIQSPGCAGCGGTQKFPVMTFNGVLVGEIVRLYPGFMQEMFTDADTYIVHFPMDMPPILKLLLVTSVFLIDFTYFEDRNQDQHRNGGMHSGMHSSF
Protein: Cytochrome b6-f complex subunit 6 (Cytochrome b6-f complex subunit PetL) (Cytochrome b6-f complex subunit VI) (P0C394)
Organism: Oryza sativa subsp. indica (Rice)
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex (By similarity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MLTITSYFGFLLAALTLTLALFIGLNKIRLI
Protein: Prolactin (R9WQI9)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MDSKGSAQKGSRLLLLLVVSNLLLCQGVVSTPVCPNGPGNCQVSLRDLFDRAVMVSHYIHNLSSEMFNEFDKRYAQGKGFITMALNSCHTSSLPTPEDKEQAQQTHHEVLMSLILGLLRSWNDPLYHLVTEVRGMKGVPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARHSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
Protein: Microfibril-associated glycoprotein-1 (Microfibrillar-associated protein 2 precursor) (Q2VW43)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MRLCYLLLLSLPGLLAQVQNYDEDYTDIFGNSNNYDNPFFYQQQILQTQTSGPGQNALDGQTEPTEPGPLDCREEQYPCTRLYSVHQPCKQCLNSICFYSLRRMYVINKEVCVRTVCAHEELLRADLCRDQFPRCGVMAHIGQCGAMGSNCARSCGSY
Protein: Putative regulator AbrB (AidB regulator) (P75747)
Organism: Escherichia coli (strain K12)
Function: Seems to be involved in the regulation of AidB.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Antitoxin MazE
- Antitoxin YefM
- mRNA interferase toxin RelE
- Endoribonuclease toxin MazF
Sequence:
MPVLQWGMLCVLSLLLSIGFLAVHLPAALLLGPMIAGIIFSMRGITLQLPRSAFLAAQAILGCMIAQNLTGSILTTLAVNWPIVLAILLVTLLSSAIVGWLLVRYSSLPGNTGAWGSSPGGAAAMVAMAQDYGADIRLVAFMQYLRVLFVAGAAVLVTRMMLGDNAEAVNQHIVWFPPVSINLLLTILLAVVAGTVGCLLRLPSGTMLIPMLAGAVLQSGQLITIELPEWLLAMAYMAIGWRIGLGFDKQILLRALRPLPQILLSIFALLAICAGMAWGLTRFMHIDFMTAYLATSPGGLDTVAVIAAGSNADMALIMAMQTLRLFSILLTGPAIARFISTYAPKRSA
Protein: Small ribosomal subunit protein eS6B (40S ribosomal protein S6-B) (Q9C0Z7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS21
- Elongation factor 3
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS12B
Sequence:
MKLNISYPANGTQKLIEIDDDRRLRVFMEKRMGQEVPGDSVGPEFAGYVFKITGGNDKQGFPMFQGVLLPHRVRLLLRAGHPCYRPRRDGERKRKSVRGCIVGQDLAVLALAIVKQGEQDIPGLTDVTVPKRLGPKRASKIRRFFNLSKEDDVRQFVIRREVVPKKEGKKPYTKAPKIQRLVTPRTLQHKRHRFALKRRQAEKNREEAAEFAQLMAKRVAEAKQKKEVVKARRASSMKK
Protein: Putative mRNA export protein (G0SET4)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nucleoporin NUP49
- Nucleoporin NUP152
- mRNA export factor GLE2
- Putative RNA annealing protein
- NTF2 domain-containing protein
- Putative RNA binding protein
- Nuclear cap-binding protein subunit 2
- Putative SAC3 family protein
- Nucleoporin NUP145
- Nucleoporin NUP159
Sequence:
MAPPTGPRRGGSAQKTALRPTRGGGISKHRPAPKTDIDGDIAMGGPPADTSKRGSGSSGRGARAGRGGRATSRMAQNIRNYATELAVGSNGAKTQPNKTVIKILGLKNSKAASNPDGGLRSLLDFLERKSKEKITLGRGIIDGDYVWLKVNKDDAQHLLRLNGFTYAGATLTIEETNEPMPALSSQSKLSQAAQETKQKLTSCLARRYNAEQKLLDLSALGTDETLSSLGSFNNQSLAEKSFKALMHLVSNEYKDPEQKNEAIQAVSLARNDILDVGQVYSLAVTLPRLRRLDLSGNNLENLSKISKWQQEFRFLEELHLTGNPVTTLPNYATEIKKWFPSLQILDGQQIRTPQEAAESLKSSFPTPLPQLPSNVRDGENNVASTFLQAFFQLWDHDRLTLIPQFYDSETTFSVVFATDSPQDPASSSCSKFSRNLNILSPRHPSTLQRLFVGSNLIADLWKVLPATRHPSLDQTSQWLIDCHTFPHLADPTGMAPYAMGLMINVNGQCEEADISQNLYGTRTFSRCFILGPSKPGAPHPYRVLSDQLTLHTWKPQPAPQVGTVPPPAVAAPMPGAVPIPTATPAVAPVPPVMGDEPDDATKAQLIAEVSRRTGMNVEYSQMCLTGAANWNLELALQSFEQQKANVPPEAFISQPQV
Protein: SPT4 homolog, DSIF elongation factor subunit (Suppressor of Ty 4 homolog 1 (S. cerevisiae), isoform CRA_b) (D3DTZ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGNREMVYDCTSSSFDGIIAMMSPEDSWVSKWQRVSNFKPGVYAVSVTGRLPQGIVRELKSRGVAYKSRDTAIKT
Protein: Bifunctional albaflavenone monooxygenase/terpene synthase (Cytochrome P450 170A1) (CYP170A1) [Includes: Epi-isozizaene 5-monooxygenase (EC 1.14.15.39); Beta-farnesene synthase (EC 4.2.3.47)] (Q9K498)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Involved in the biosynthesis of the sesquiterpenoid antibiotic albaflavenone. Catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone. First carries out a non-stereo-specific oxidation of epi-isozizaene to give a mixture of the albaflavenol epimers ((5R)-albaflavenol and (5S)-albaflavenol), each of which can serve as substrate for the second oxidation to yield albaflavenone. This is quite different from most other P450s which catalyze regio- and stereospecific oxidation. In addition, displays a farnesene synthase activity with farnesyl diphosphate (FPP) as substrate.
Interaction partners:
- Epi-isozizaene synthase
- Germacradienol/geosmin synthase
- Biflaviolin synthase CYP158A2
- CDA peptide synthetase III
- Biflaviolin synthase CYP158A1
- Peptide synthase
- Phenyloxazoline synthase MbtB
- biflaviolin synthase
- Peptide synthase
- CDA peptide synthetase I
Sequence:
MTVESVNPETRAPAAPGAPELREPPVAGGGVPLLGHGWRLARDPLAFMSQLRDHGDVVRIKLGPKTVYAVTNPELTGALALNPDYHIAGPLWESLEGLLGKEGVATANGPLHRRQRRTIQPAFRLDAIPAYGPIMEEEAHALTERWQPGKTVDATSESFRVAVRVAARCLLRGQYMDERAERLCVALATVFRGMYRRMVVPLGPLYRLPLPANRRFNDALADLHLLVDEIIAERRASGQKPDDLLTALLEAKDDNGDPIGEQEIHDQVVAILTPGSETIASTIMWLLQALADHPEHADRIRDEVEAVTGGRPVAFEDVRKLRHTGNVIVEAMRLRPAVWVLTRRAVAESELGGYRIPAGADIIYSPYAIQRDPKSYDDNLEFDPDRWLPERAANVPKYAMKPFSAGKRKCPSDHFSMAQLTLITAALATKYRFEQVAGSNDAVRVGITLRPHDLLVRPVAR
Protein: Interferon alpha-2 (IFN-alpha-2) (Interferon alpha-A) (LeIF A) (P01563)
Organism: Homo sapiens (Human)
Function: Produced by macrophages, IFN-alpha have antiviral activities.
Subcellular location: Secreted {ECO:0000269|PubMed:6159538}.
Interaction partners:
- Interferon alpha/beta receptor 2
- Interferon alpha/beta receptor 1
- Interferon gamma
- Interferon regulatory factor 7
- Ubiquitin-like protein ISG15
- Tyrosine-protein kinase JAK1
- Interferon alpha-5
- Interleukin-1 beta
- Signal transducer and activator of transcription 1-alpha/beta
- Interferon lambda-1
Sequence:
MALTFALLVALLVLSCKSSCSVGCDLPQTHSLGSRRTLMLLAQMRRISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMIQQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVRKYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE
Protein: Transmembrane protein 199 (Q8N511)
Organism: Homo sapiens (Human)
Function: Accessory component of the proton-transporting vacuolar (V)-ATPase protein pump involved in intracellular iron homeostasis. In aerobic conditions, required for intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. Necessary for endolysosomal acidification and lysosomal degradation. May be involved in Golgi homeostasis.
Subcellular location: Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:26833330}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:26833330}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:28296633}; Multi-pass membrane protein {ECO:0000255}. Note=Partial colocalization with GOLGB1. {ECO:0000269|PubMed:26833330}.
Interaction partners:
- Vacuolar ATPase assembly protein VMA22
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit F
- Renin receptor
- V-type proton ATPase 116 kDa subunit a 2
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase catalytic subunit A
Sequence:
MASSLLAGERLVRALGPGGELEPERLPRKLRAELEAALGKKHKGGDSSSGPQRLVSFRLIRDLHQHLRERDSKLYLHELLEGSEIYLPEVVKPPRNPELVARLEKIKIQLANEEYKRITRNVTCQDTRHGGTLSDLGKQVRSLKALVITIFNFIVTVVAAFVCTYLGSQYIFTEMASRVLAALIVASVVGLAELYVMVRAMEGELGEL
Protein: Porin (E2IFU4)
Organism: endosymbiont of Crithidia deanei
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571}.
Interaction partners:
Sequence:
MKKTLLAAALVTSFAGVAQAETAVNLYGLIDTGVNVNTVEVRDFRRVKHKISRVGPVSGAQSGSRWGLKGTEEIGNGLRAEFVLEGGFNSGNGDAAQTQRIFGRQVTVGVANDAWGRLDIGRQTNVASKYFADIDPFKGGFEQSAIGMSIGSSNVRYDNMIMYQTPSFRGIDIGVGYSFSVDTKSSKSEHVTVNNAFSAEEAANWRTNENDRAFTTGIRYSNGPVVATASFDYVKGSKRRVERDAYFDVSPCSYAVGGAYDFDVAKVSVAYAKTMDGWIGALNVDGYRDLIGLSRLITEYADGFRSSSYVVGVSAPINETSNVFGSWQRVSVNAKPKGARLTGDNDSMNVYSVGYTQDLSKRTNLYAYGSYASDYAFLYSAKSKVVGFGMRHRF
Protein: Probable G-protein coupled receptor 150 (Q8NGU9)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MEDLFSPSILPPAPNISVPILLGWGLNLTLGQGAPASGPPSRRVRLVFLGVILVVAVAGNTTVLCRLCGGGGPWAGPKRRKMDFLLVQLALADLYACGGTALSQLAWELLGEPRAATGDLACRFLQLLQASGRGASAHLVVLIALERRRAVRLPHGRPLPARALAALGWLLALLLALPPAFVVRGDSPSPLPPPPPPTSLQPGAPPAARAWPGERRCHGIFAPLPRWHLQVYAFYEAVAGFVAPVTVLGVACGHLLSVWWRHRPQAPAAAAPWSASPGRAPAPSALPRAKVQSLKMSLLLALLFVGCELPYFAARLAAAWSSGPAGDWEGEGLSAALRVVAMANSALNPFVYLFFQAGDCRLRRQLRKRLGSLCCAPQGGAEDEEGPRGHQALYRQRWPHPHYHHARREPLDEGGLRPPPPRPRPLPCSCESAF
Protein: Transcription factor IIIB 50 kDa subunit (TFIIIB50) (hTFIIIB50) (B-related factor 2) (BRF-2) (hBRFU) (Q9HAW0)
Organism: Homo sapiens (Human)
Function: General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites. Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress. Down-regulates expression of target genes in response to oxidative stress. Overexpression protects cells against apoptosis in response to oxidative stress.
Subcellular location: Nucleus {ECO:0000269|PubMed:17505538}.
Interaction partners:
- TATA-box-binding protein
- Transcription factor TFIIIB component B'' homolog
- General transcription factor 3C polypeptide 3
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase III subunit RPC3
Sequence:
MPGRGRCPDCGSTELVEDSHYSQSQLVCSDCGCVVTEGVLTTTFSDEGNLREVTYSRSTGENEQVSRSQQRGLRRVRDLCRVLQLPPTFEDTAVAYYQQAYRHSGIRAARLQKKEVLVGCCVLITCRQHNWPLTMGAICTLLYADLDVFSSTYMQIVKLLGLDVPSLCLAELVKTYCSSFKLFQASPSVPAKYVEDKEKMLSRTMQLVELANETWLVTGRHPLPVITAATFLAWQSLQPADRLSCSLARFCKLANVDLPYPASSRLQELLAVLLRMAEQLAWLRVLRLDKRSVVKHIGDLLQHRQSLVRSAFRDGTAEVETREKEPPGWGQGQGEGEVGNNSLGLPQGKRPASPALLLPPCMLKSPKRICPVPPVSTVTGDENISDSEIEQYLRTPQEVRDFQRAQAARQAATSVPNPP
Protein: Inner kinetochore subunit mhf1 (CENP-S homolog) (Constitutive centromere-associated network protein mhf1) (MHF histone-fold complex subunit 1) (O74807)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of a FANCM-MHF complex that promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork (Probable). FANCM-MHF promotes non-crossover recombination.
Subcellular location: Nucleus {ECO:0000305|PubMed:22723423}.
Interaction partners:
- Inner kinetochore subunit mhf2
- ATP-dependent DNA helicase fml1
- Inner kinetochore subunit cnp20
- Histone H3-like centromeric protein cnp1
- Inner kinetochore subunit wip1
- Replication factor A protein 3
Sequence:
MMEEERFKAEIFHVTQEVCNRTASELTESESRNVIVDELFCVGVTEMVWEQIRVLAKDIEAFAEHAGRKTVQPQDVLLCCRRNEGLYEIINNFHKESIKSKKKKKENSTT
Protein: Transcriptional regulator ICP22 homolog (Q89582)
Organism: bovine alphaherpesvirus 1
Interaction partners:
Sequence:
MSHGQPCPTCDGSCRLCRSPDRVVSGPAPADEHARRGPGAFCPEDWRPEALRLAIDVNTLFRCIATGSAFVTADTRALRRALVGFFLLGYTGATPTDACWEALLQLSPEQAGPLRRLLRAAAAAGPRARPLSPPARLPGPLFGAECDVSGSDSSSEDYEEDEEADEEGEENGGEGAAAESPPRCRPRAAVLSSASPAASAVSFVSSPTASSSTSSSSLSSFSASDGDDDVFFPGPGDPRPAGAGPGAGGPPARAGRRRPAPCWRWSSGSSPGSSPYPSPGGSPSGRARARPAPAKRRQRV
Protein: Protein Tax-1 (Protein X-LOR) (Trans-activating transcriptional regulatory protein of HTLV-1) (P0C213)
Organism: Human T-cell leukemia virus 1 (isolate Zaire EL subtype B) (HTLV-1)
Function: Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interaction with CREB1 and CREBBP. Also induces chromatin remodeling of proviral LTR-mediated gene expression by recruiting the histone acetyl transferases CREBBP and EP300 to the chromatin, which results in histone acetylation. Via its interaction with IKK regulatory subunit IKBKG, Tax-1 persistently stimulates I-kappa-B kinase (IKK), resulting in constitutive activation of the transcription factor NF-kappa-B. Induction of the nuclear expression of members of the NFkB family of transcription factors, which leads to up-regulated expression of many gene promoters containing NFkB motifs. These genes include those encoding IL2, IL15, IL2RA and IL15RA, leading to autocrine IL2/IL2RA and IL15/IL15RA loops. The resulting T-cell proliferation leads to malignant transformation and to the development of adult T-cell leukemia (ATL). IL13, known to be linked to leukemogenesis, is also up-regulated by Tax-1. Interaction with PDZ domain-containing proteins induce IL2-independent growth, which may be a factor in multi-step leukemogenesis. Inhibits the action of at least three cellular tumor suppressors p53/TP53, RB1 and DLG1, and suppresses their abilities to dictate apoptosis in primary cells. Required for viral replication (By similarity).
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:P03409}. Host cytoplasm {ECO:0000250|UniProtKB:P03409}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed between the nucleoplasm and the nuclear matrix. {ECO:0000250|UniProtKB:P03409}.
Interaction partners:
Sequence:
MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPTTHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFDHPDQLGAFLTNVPYKRMEELLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQSGLLPFHSTLTTPGLIWAFTDGTPMISGPCPKDGRPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHNLHLLFEEYTNIPISLLFNEKEADDTDHEPQVSPGGLEPPSEKHFRETEV
Protein: Maturase K (Intron maturase) (P0C381)
Organism: Oryza sativa (Rice)
Function: Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns.
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MEKFEGYSEKLKFPRQYFVYPLLFQEYIYVFAHDYGLNGSELVEIIGSNNKKFSSLLVKRLMIRMYQQNFWINLVNHPNQDRLLDYNNFFYSEFYSQILSEGFAIVVEIPFSLREQSCPEEKEIPKFQNLRSIHSIFPFLEDKFLHLHYLAHIEIPYPIHLDILLQLLQYRIQDVPSLHLLRFFLNYYSNWNSFITSMKSIFILKKENKRLFRFLYNSYVSEYEFFLLFLRKQSSCLRLTSSGTFLERIIFSRKMEHFGLMYPAFFRKTIWFVMDPLMHYVRYQGKAILASKGTLLLKKKWKCYLVRLWQYSFSFWTQPQRIHLNQLENSCFDFLGYFSSVPINSLLVRNQMLENSFLIDTQMKKFDTKVPVTPLIGSLAKAQFCTGSGHPISKPIWTDLSDWDILDRFGRICRNLFHYYSGSSKKKTLYRLKYILRLSCARTLARKHKSTVRAFMQWLGSVFLEEFFTEEEQVFSLMFAKTTYFSFRGSHSERIWYLDILRINDLVNPLN