wanglab/gogpt-training-data huggingface dataset:
Protein: LIM zinc-binding domain-containing protein (Q586W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSSRGSFPESLEGAPDTNAEEDEVNLHDISSPPDLANTRKGIDASDCVTLNDERNFETASPPMDPKENETIEAIKSSDTTETHQVPGSICGTNTENHIGEIKKKSYGTDNVTTDAAETVEIMEVSEIVEADDATETVEAMEVAETVEADDATETVEATEVAEAAEALNATETVEATEVAEAVEALNATETVEATEVAEAAEALNATETVEATEVAEAVEALNATETVEATEVAETAEALNATETVEATEVAEAAEALNATETVEATEVAEAAEALNATETVEATEVAETAEALNATETVEATEVAEAAEALNATETVEATEVAEAAEALNATETVEATEVAETAEALNATETVEATEVAETAEALNATETVEATEVAEAAEALNATETVEATEVAEAVEALNATETVEATEVAETAEALNATETVEATEAAEAAEALNATETVEATEVAEAVEALNATETVEATEVAEAVEALNATETVEATEVAEAVEALNATETVEATEVAEAVEALNATETVEATEVAETAEALNATETVEATEVAEAAEALNATETVEATEVAEAAEALNATETVEATEVAEAAEALNATETVEATEVAETAEALNATETVEATEVAETAGALNATETVEATEVAETAEALNATETVEATEVAETAGALNATETVEATEVAETAEALNATETVEATEVAEAAEALNATETVEAMEVAEAVEALNATETVEATEVAEAAEALNATETVEATEVAEAVEALNATETVEATEVIEGAEVTISVDGTESAVVVEESEIVYQADTTRDDSVVDGAITSGGIEVDNDAKAVDKNKATHEAVEVLKDLESERAANNTEAPLAEVTGVETDAIASAGAVDDIKTLEAPSGENPPVVEYDEVVNTVGSAGVSGGARGEQDIAVVSSREDDVKNTEGSGFPERKETETSATTPTPLHSDAGVRAQTAGPGGMAKELALPKDASADGPKRVESAAVNPSEKKDLTPNVGKEPQRTLEKSKGDKPAKQEVLASAQHQPAAGTVGKHVRRKRKGLLYENYYGPHVIQRVRNPLNLTPAEEYSVFRARNGVSLNYTGPIHVVEEIHVGCAYCGCPVDAVTRVEAGKLHFHPQCIRCKLCGANSISDAYFQVTNNSVICSECSVRGLSENVAKEEAADDTMFTSNFRHKFERAIRRFDVNSERRPRLNVNAEGIIPPTLTLNIDHERGSSTNSKRLALIHRQQYYSQNDNNIICLSPPESPSISPKKN
Protein: Solute carrier family 22 member 19 (Organic anion transporter 5) (Q8VCA0)
Organism: Mus musculus (Mouse)
Function: Sodium-independent organic anion transporter which shows high specificity for estrone sulfate, dehydroepiandrosterone sulfate, and the mycotoxin ochratoxin A (OTA). Transport of OTA is strongly inhibited by estrone sulfate and probenecid, and to a lesser extent by 2,4-dichlorophenoxyacetic acid (2,4-D) and salicylate. Transport of estrone sulfate is inhibited by various steroid sulfate conjugates including dehydroepiandrosterone sulfate, alpha-naphthyl sulfate, beta-estradiol sulfate, 4-methylumbelliferyl sulfate and p-nitrophenyl sulfate (but not minoxidil sulfate).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15068970, ECO:0000269|PubMed:16150593}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAFQDLIIQIGSLGRFQILHMIFVLICHALSAPHTLLENFTAAIPSHRCWVPILDNDTASDNGSRILSQDDLLRISIPLDSNLRPDKCRRYIQPQWHLLHLNGTFPTVTEPDTEPCVDGWVYDQSTFLSTTVTQWDLVCGSQALNSVAKFIYMTGIFIGYIMGGHLSDKFGRKLIFTCSLLKMAITETCVAFAPSFLIYCSLRFLSGIFSSTLRTNSALLILEWTSPKFQALVMALIFIASGVGQTLLGGLAFAFRNWHHLQLALSVPMFLLLIPTRWLSESARWLIMANKPQKSLKELKKAACVNRIKNSGDALTLEVVKTIMKEELEAAQTKPSPLDLFRTPNLRKRICLLSFVRFVSVMSLLGLLINIQYLSNNVFLLQCLYGVVCIPANVLGNFSMNYMGRRMTQLIFMSVLGISILAVVFLPQEMQILRVFLSTLGGAISSASITSTLVHANELVPTIIRATALGVVGIAGSAGGALSPLLMILTTYSASLPWIIYGILPFLGGLVALLLPETKNQPLPDSIQDIENKRKSSKEAKKDVVAKVTPL
Protein: Cinnamoyl-CoA reductase-like SNL6 (EC 1.2.-.-) (Protein SUPPRESSOR OF NH1-MEDIATED LESION 6) (Q0JKZ0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in defense response. Required for NPR1/NH1-mediated resistance to the bacterial blight pathogen Xanthomomas oryzae pv. oryzae (Xoo). Required for pathogenesis-related (PR) genes expression. May be involved in lignin biosynthesis.
Interaction partners:
- 40S ribosomal protein S29, putative, expressed
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS9
- Os10g0411700 protein
- 40S ribosomal protein S15, putative, expressed
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS21
- 40S ribosomal protein S21
- 40S ribosomal protein S12
- 40S ribosomal protein S12
Sequence:
MGVLRSTQSMQAEVEEMRAALLHGHGGGAAAAAAAGWRPSAGDADVKRTAGGDGGAAGPRTVCVTGGISFVGFAVVDRLLRHGYTVRLALETQEDLDKLREMEMFGEDGRDGVWTVMANVTDPESLHRAFDGCAGVFHTSAFVDPGGMSGYTKHMASLEAKAAEQVIEACVRTESVRKCVFTSSLLACVWRQNYPHDRRFPTIIDENCWSDESFCRDNKLWFALGKTAAEKTAWRAARGRDLKLVTVCPALVTGPGFRRRNSTASIAYLKGARAMLADGLLATASVETVAEAHVRVYEAMGDNTAGGRYICYDHVVKRPEEFAELERQLGIPRRAAAAAAAQDSGDRPARFDLCRQKLARLMSTRRRCTYDDYYSVAFD
Protein: GH11341p (Hypothetical 55kDa protein) (Regulatory particle non-ATPase 5) (Q9V3Z4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 1
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome regulatory complex subunit p50
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 11
- Ubiquitin carboxyl-terminal hydrolase
- Proteasome subunit alpha type-5
- Proteasomal ubiquitin receptor ADRM1 homolog
- 26S proteasome regulatory subunit 4
Sequence:
MDTYLFDGGRITKMEVDYEPACNEKIPLAKELAKKNPDAFHEAIEMMLQLEKQTRLGADMVSCSRVLVAICQICFDASNWNALNEYVSLLVRRRSQLKQAVVKMIQECVTYVDKTPDKETKLKLIDTLRSVTEGKIYVEIERARLTKILADIKEADGDVAGAATVMEELQVETYGSMDKREKVELILEQMRLCLLKEDYVSTQIIAKKISIKFFDDPAQHDLKLKFYYLMIQLNRDTSFLNTSRHYQAIAEPPRKKTGLTPVDSAASTDEQKKKDDDKKKKEEDDKDKKPEVATEAEVEIELTEEQKKELTEKLVCAVLYCVLAPFDNEQSDMMAHLSKNKKLEEVPAYKEILRLFMSKELINFDTFNADFGLVLAENEMFKDSTKHGKKCITELKDRLIEHNIRIIAMYYSRLHLARMSELLNLPTSRCEEYLSKLANTDTIRVKIDRPAGIIYFTQKKSASDILNNWATDVNQLMSLVNKTCHLINKEECVYSVMCAVED
Protein: Uncharacterized protein (Q584S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- G domain-containing protein
- rRNA processing protein, putative
- NLE domain-containing protein
- Ribosome biogenesis protein NSA2 homolog
- 60S ribosomal protein L24, putative
Sequence:
MLCSGRIILKKKWIPPLGYRPKDFERKLRSPRSSKPWRDRRAASGGQIEVSPSTAATNIPRGDLVFRPPLGIRDVRPGSPSALLPTFGFSEEHLAAHALPAAGSQVEGGDVLAVADPRSASHLTLPFGRALNVNVEEIKTYEEGPVPIHLQQFRRSRREAADSIILPRHINRLFHKIMGWSEDLVKVEMDEAPTPNTGGVPSDTAAVRAKEAQESEVPLLRMKYDNVVDKMKYGVLLDNYEKDKFAIEHQLEIAGEKFERKFLDWEGMHVLDQDPSAAVREVLENKASIVMEQPSSFAIPVVNRDCCRGCGALLQDQDENSFGYVRKGDVERYIIEKQQKMRARAEYADRMSELQAHWRKHGRRVGEEWLDFMTQEEFDAFYRDRNAPFVCHRCHALENLGVEGRRRIWSAPDFTDKLRALREKKCVVVLVVDVTDFPGTMVYDLPGLISMNNDVIIAVNKMDCVRNRSFNYRGKDRAVAACLVTERYVRRWVTGIAVQFGLPRHQIKDVIPLSAKRGWNVEALIAAVEEASNLNLRRPTKPIPTYFVGVANVGKSSVINAIAHKLYVPLPPHPESRKVYYTKKAPDGSESVFWRWYTPPNVNQAEMIDIPSRHDKKASKLVTTSSLPGTTVDAVAVRVSLSKGAEKGRAHLFDTPGLLPHWHRHSPLTLLQMRRTLIRKFRNPQCFILVPGNTLFLGGLCAVDVVKGTSRGMLFMVYTSQKVRNAIINTDRSDEFWREQLGRALDPPGSVEQVGDLRLTESRSYLFECYQRNRKRPKADIYFCGLGWVAFCVNEPADVVLRVRTLPGVVHGVREPLRYKDLLAFKGWPKLRRRFTSAGVPNDEEDDDNSIATVVRLTAGGGACGLSAAPVCGSPEEDVDGPAVRVVRKSVLPKPIPASSTPFDGVVEELSLSGQAGGGTGAGM
Protein: Coiled-coil domain-containing protein 146 (Q8IYE0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:25074808, ECO:0000269|PubMed:30094225, ECO:0000269|PubMed:38441556}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:38441556}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:38441556}. Midbody {ECO:0000269|PubMed:38441556}. Note=In sperm cells, was seen localized to only one centriole identified as the mother centriole by co-staining with CEP164 (PubMed:25074808). In other experiments, localization to centrioles in sperm cells was not observed (PubMed:38441556). Localizes to the sperm connecting piece and flagellum during spermiogenesis and to the flagellum in spermatozoa from cauda of the epididymis (By similarity). In sperm cell flagellum, may be associated with tubulin doublets (PubMed:38441556). {ECO:0000250|UniProtKB:E9Q9F7, ECO:0000269|PubMed:25074808, ECO:0000269|PubMed:38441556}.; SUBCELLULAR LOCATION: Note=(Microbial infection) In cells infected with C.trachomatis incM, recruited to the periphery of the pathogen-containing vacuole but recruitment is not dependent on incM. {ECO:0000269|PubMed:30094225}.
Interaction partners:
- Geminin
Sequence:
MEDSSTDTEKEEEEEKDEKDQEPIYAIVPTINIQDERFVDLSETPAFIFLHELHAMGKLPGTRMAALKAKYTLLHDAVMSTQESEVQLLQNAKRFTEQIQQQQFHLQQADNFPEAFSTEVSKMREQLLKYQNEYNAVKEREFHNQYRLNSLKEEKIIIVKEFEKITKPGEMEKKMKILRESTEELRKEIMQKKLEIKNLREDLASKQKQLLKEQKELEELLGHQVVLKDEVAHHQTIPVQIGKEIEKITRKKVEMEKKKIVLEQEVKTLNDSLKKVENKVSAIVDEKENVIKEVEGKRALLEIKEREHNQLVKLLELARENEATSLTERGILDLNLRNSLIDKQNYHDELSRKQREKERDFRNLRKMELLLKVSWDALRQTQALHQRLLLEMEAIPKDDSTLSERRRELHKEVEVAKRNLAQQKIISEMESKLVEQQLAEENKLLKEQENMKELVVNLLRMTQIKIDEKEQKSKDFLKAQQKYTNIVKEMKAKDLEIRIHKKKKCEIYRRLREFAKLYDTIRNERNKFVNLLHKAHQKVNEIKERHKMSLNELEILRNSAVSQERKLQNSMLKHANNVTIRESMQNDVRKIVSKLQEMKEKKEAQLNNIDRLANTITMIEEEMVQLRKRYEKAVQHRNESGVQLIEREEEICIFYEKINIQEKMKLNGEIEIHLLEEKIQFLKMKIAEKQRQICVTQKLLPAKRSLDADLAVLQIQFSQCTDRIKDLEKQFVKPDGENRARFLPGKDLTEKEMIQKLDKLELQLAKKEEKLLEKDFIYEQVSRLTDRLCSKTQGCKQDTLLLAKKMNGYQRRIKNATEKMMALVAELSMKQALTIELQKEVREKEDFIFTCNSRIEKGLPLNKEIEKEWLKVLRDEEMHALAIAEKSQEFLEADNRQLPNGVYTTAEQRPNAYIPEADATLPLPKPYGALAPFKPSEPGANMRHIRKPVIKPVEI
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC1 (RNA polymerases I, II, and III subunit ABC1) (DNA-directed RNA polymerase II 23 kDa polypeptide) (DNA-directed RNA polymerase II subunit E) (RPB5 homolog) (XAP4) (P19388)
Organism: Homo sapiens (Human)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:9852112}. Nucleus, nucleolus {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerase II subunit RPB11-a
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase III subunit RPC5
- General transcription factor IIF subunit 2
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MDDEEETYRLWKIRKTIMQLCHDRGYLVTQDELDQTLEEFKAQSGDKPSEGRPRRTDLTVLVAHNDDPTDQMFVFFPEEPKVGIKTIKVYCQRMQEENITRALIVVQQGMTPSAKQSLVDMAPKYILEQFLQQELLINITEHELVPEHVVMTKEEVTELLARYKLRENQLPRIQAGDPVARYFGIKRGQVVKIIRPSETAGRYITYRLVQ
Protein: Golgi reassembly-stacking protein 1 (Golgi peripheral membrane protein p65) (Golgi phosphoprotein 5) (GOLPH5) (Golgi reassembly-stacking protein of 65 kDa) (GRASP65) (Q9BQQ3)
Organism: Homo sapiens (Human)
Function: Key structural protein of the Golgi apparatus. The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon. Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks. However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (By similarity). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes. Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane.
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11781572}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:11781572}.
Interaction partners:
- Golgin subfamily A member 2
- General vesicular transport factor p115
- Golgin-45
- Serine/threonine-protein kinase PLK1
- Golgin subfamily B member 1
- Protein transport protein Sec24B
- Syntaxin-5
- Golgin subfamily A member 3
- WD40 repeat-containing protein SMU1
- Serine/threonine-protein kinase 25
Sequence:
MGLGVSAEQPAGGAEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEQVWHVLDVEPSSPAALAGLRPYTDYVVGSDQILQESEDFFTLIESHEGKPLKLMVYNSKSDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAPPPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLPHFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPEDICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSAELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE
Protein: Ribonuclease kappa (RNase K) (RNase kappa) (EC 3.1.-.-) (V-type proton ATPase subunit f) (V-ATPase subunit f) (Q3ZC23)
Organism: Bos taurus (Bovine)
Function: Endoribonuclease which preferentially cleaves ApU and ApG phosphodiester bonds. Hydrolyzes UpU bonds at a lower rate (By similarity). Regulates the activity of vacuolar (H+)-ATPase (V-ATPase) which is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). Required at an early stage of receptor-mediated endocytosis (By similarity).
Subcellular location: Endomembrane system {ECO:0000250|UniProtKB:Q6P5S7}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32764564}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit E 1
- Renin receptor
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit C 1
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit e 2
- V-type proton ATPase subunit H
Sequence:
MASLLCCGPKLAACGIVLSAWGVIMLIMLGIFFNVHSAVLIEDVPFTEKDFENGPQNIYNLYEQVSYNCFIAASLYLLLGGFSFCQVRLNKRKEYMVR
Protein: Neuromusculin, isoform H (M9NGD9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGNMALRQSAKDVAKSNCVAVRSSISLSLVLVLCLALVDSSTAQVDTTISQQESQSVVLPCPVDAEKCGKLHSLNWFKGDDRIAAMLLGDSNVTSVNKEFDERVTVEQNPYRLVIKDLKIADEDIYLCDTTFFIPEETCDNFNGYRIELRVLVPPTEVVILDAKGDRIKNGSVVGPMQERQSLKATCTVRNTRPQPEVSWFRGTKRLTTYSPTHDLVDGLYTSTLELDWTLSREDLAQDIECRVKSAAIQNVTVTKFSVDLQVRPTSIDINGVKHHTVQGSKVVLTCDIHGARPAVNLTWYNTTTIISSGENEITEVRSKSLEKSDGTFHTQSELIFNATRFENDRVFRCEAENIVLQINREKPISSALTLEVLYPPVVKVSPSAITANTSEIVLLNCEYFANPASLTQVEWYRNDILVNVNDTTHYKGGNSENVALVIKSTEKEDIGNYSCQLSNNIGKGTSDQKINLDVQYAPTVEILMIPEGPVKESDESNVTLFCNVLDANPSVLTKVRWYANSTLLKELPDCEETREDLCHIDPSKLLLESIGRGFFYNYSCEGFNAAGWGPRSEDKELLVHYEPGPAALSHFPLVAVKKKSVTFSCSVDDPGFPESNRFVAQKANQNHKMKNPQHAPLMDFHTVQAMQPQEVDIAFEAMLLHKHQNPLPFIDSIQTSTRTPQESASHPAHKIKETHALIDLHLNHSLCTLITLTTYMPQSPILTLYTGVQQKKDASATSYALYRKMGKFSFVAQIVSKPNRFRWLRGGRGPLQDIVTKDWTVEPVGLDSRTNYSCYAYNEGGKGVMATVNLEVHAPPFFIKNLPPYTGILHSSPNATLTCRIECVPRCDISWQKDGVPIERNDSRYFIKEKYMDASPATGDFESMLSVLHFNMPNWPDSKFNIEADNANYSCVSTGNIVGGSIRSRTYFGIEYAPENTTVSENIVYVQEDTIPGRVICKSRANPEPSYKWIFKNETIANGNALIINTAMNRNDDGTYTCLAYNKHGSSIAKTVIKVQFKPRCEIERQEIDDQDTLICTAYGNPIEADFSWSIKTENETDENLGSGKKENSVEKSFYILQTDYAISRTYRCVANNTVGYGPFCEIEVAAASSLLVWWQEQLAWWQLWEKNTLIILVAAILGLLLTVIVICCIIICICRRRRRQDKLHDKSSSLREPLTEPGEYENLPFHGLQTAPNKHLSDFEDPYKSSNTYIF
Protein: Solute carrier family 66 member 1 (A2A2E6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
PLQTYTAVYYVLADLVMLTLYFYYKFRTRPSLLSAPINSVLLFLMGMACATPLLSAAGPVAAPREAFRGRALLSVESGSKPFTRQEVIGFVIGSISSVLYLLSRLPQIRTNSCTPPVCQAPSWTLEP
Protein: Adenosine kinase 1 (AK 1) (EC 2.7.1.20) (Adenosine 5'-phosphotransferase 1) (Q9SF85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives. Essential to sustain methyl recycling.
Interaction partners:
- Adenylate kinase 1, chloroplastic
- Adenine phosphoribosyltransferase 1, chloroplastic
- Adenine phosphoribosyltransferase 2
- Adenine phosphoribosyltransferase 4
- Adenine phosphoribosyltransferase 5
- AMP deaminase
- N6-mAMP deaminase
- Adenine phosphoribosyltransferase 3
- Adenylosuccinate lyase
- Adenylosuccinate lyase
Sequence:
MASSDFDGILLGMGNPLLDVSAVVDQQFLDKYDIKLNNAILAEDKHLPMYDEMSQKFNVEYIAGGATQNSIKVAQWMLQVPGATSYMGSIGKDKYGEAMKKDATAAGVYVHYYEDEATPTGTCGVCVLGGERSLIANLSAANCYKVEHLKKPENWALVEKAKFYYIAGFFLTVSPESIQLVREHAAANNKVFTMNLSAPFICEFFKDVQEKCLPYMDYIFGNETEARTFSRVHGWETDDVEQIAIKMSQLPKASGTYKRTTVITQGADPVVVAEDGKVKKYPVIPLPKEKLVDTNGAGDAFVGGFLSQLVHGKGIEECVRAGCYASNVVIQRSGCTYPEKPDFN
Protein: Cytochrome b (Q2F912)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MTIRNQRFSLLKQPIYSTLNQHLIDYPTPSNLSYWWGFGSLAGICLVIQIVTGVFLAMHHTPHVDLAFNSVEHIMRDVEGGWLLRYMHANGASMFLIVVHLHIFRGLYHASYSSPREFVWCLGVVIFLLMIVTAFIGYVPPWGQMSFWGATVITSLASAIPVVGDTIVTWLWGGFSVDNATLNRFFSLHHLLPLILVGASLLHLAALHQYGSNNPLGVHSEMDKIASYPYFYVKDLVGRVASAIFFSIWIFFAPNVLGHPDNYIPANPMPTPPHIVPEWYFLPIHAILRSIPDKAGGVAAIAPVFISLLALPFFKEMYVRSSSFRPIHQGIFWLLLADCLLLGWIGCQPVEAPFVTIGQIPSFFFFLFFAITPIPGRVGRGIPKYYTDETHRTGSVS
Protein: Ras-related protein RABB1c (AtRABB1c) (Ras-related protein Rab2A) (AtRab2A) (P92963)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta 1
- Rab escort protein 1
- Kinesin-like protein KIN-14E
- Rho GDP-dissociation inhibitor 1
- Geranylgeranyl transferase type-2 subunit beta 2
- At1g12070
- Immunoglobulin E-set superfamily protein
Sequence:
MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDNKPIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRETFNHLASWLEDARQHANANMTIMLIGNKCDLAHRRAVSTEEGEQFAKEHGLIFMEASAKTAQNVEEAFIKTAATIYKKIQDGVFDVSNESYGIKVGYGGIPGPSGGRDGSTSQGGGCCG
Protein: Nucleoporin nup132 (Nuclear pore protein nup132) (Q9UTH0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15226438, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleoporin nup107
- Nucleoporin nup85
- Nucleoporin nup189
- Nucleoporin nup120
- Nucleoporin seh1
- Protein transport protein sec13
- Nucleoporin nup131
- Uncharacterized protein ely5
- Nucleoporin nup146
- Nucleoporin nsp1
Sequence:
MSSILGKRKNEEVVSFSPLKRISVEKSLLDSTAYNNSLDWLRSKNFKVSCLLKHFNSKIINDHPLSGSCYTDIGYALINSRKACFILSYRQSLGTAEPPTITFPLPEEDSNGFSGQNALTAFVPSDASDKEPGLLIVMPISGRIAYWTSIGNALAQSYICPQGMESLIKLLPKEKCEHLCCSNPMKFIISTNFGRLFSVQLRDPAGQPDVSVQLFASDISTFSTILQKMKIFNYPSIHIIALKSPPLFSPYQHLLYVAEASGLLEIYDLKLENKLVSGMNLSPIFKQVLREGCPDASGLEVLDLTICPTNGNLVSFLVCWKNSINYRYMIISLDFSDISSPSVMNIHPLYSFSSKSLESSKLHYSSSGNSLFVVLTDAVIIVHVQEDDKDIVSRTSWEEVIRMNTNVSGGIFMSTCYKYVLGKYSIPTESCFIATPYSGIAEIEVHSLEHPANNESLVKSKLEEAVFYSFLPGNPIDFSCNYLRSIKKPELERIIVDLGMDILNSRSTHLPPLFASLMQHLSCRLNSLNNLVRYIRSMSLDVDRQVLYKLRVMGEKCNSVRYLWNTIDTEFSTVSHSLIFQRIIYRLTQSASSDNALREWFLHNIESIDQLIAQAHEFCIDSGSRVQELPLEVLDVIMEANEVILAIQSSALAYRRESQKIYKLSIDTFGEEVPWTSTPETLVLLCRQFELTRSALVQSHQGTSDVENTFKIKDKGVLRNVVSNLEVQLVALTEVCFDAYSERIRWIEQRCGKDASEIQDVKEAFAVNRRFWVQTLSDIGKGSSAIRIAEKYSDYRSLVELCYQLYEDNELTDALNNYLDLFGIKFAFILYDYFVENGMALELLNSDRFNKSYLKQFFKSRDYNQISWMHDMRLGDYDAASHRLLQLATKQEKLVDKKESELSLSKLFLYAVPSNSGNIRDLVLVEQKLEQLHIQKMVSKSVMPVVERLRSQGKKYQLVEAVVDDLIGAKVAPVIARQVMQRVVKKFIAGQVVEATELLEYLSFSLYRREDLVEGEVTDYYLALRLLLTTRLTDDAKRFYENTIWRRAVLHDNWIQVLDTQGKNDAIIETQFRMSALYRTLEAVTINGLFHEGLIRPGSLSSCKFEGYDPQNLISIYPPARFGDVTEVTKVLNRESVKLDHYLTKTNLNTCYISMCLSCDTI
Protein: Protein ORF28 (F5HI25)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Subcellular location: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSMTSPSPVTGGMVDGSVLVRMATKPPVIGLITVLFLLVIGACVYCCIRVFLAARLWRATPLGRATVAYQVLRTLGPQAGSHAPPTVGIATQEPYRTIYMPD
Protein: GPN-loop GTPase QQT1 (EC 3.6.5.-) (Protein EMBRYO DEFECTIVE 1705) (Protein QUATRE QUART 1) (Q56XY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Small GTPase that is essential for the correct formation of the tangential divisions in early embryos. Associates with microtubule during mitosis and may function in the positioning of the division plane. May participate in the patterning of the early embryo at the octant-dermatogen transition. Is crucial for normal development of the plant.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17419841}. Nucleus {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17419841}. Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:17419841}. Note=During interphase, mainly expressed in the cytoplasm and weakly in the nucleus. Associated with microtubules during cell division. {ECO:0000269|PubMed:17419841}.
Interaction partners:
- Transcriptional elongation regulator MINIYO
- GPN-loop GTPase QQT2
- DNA-directed RNA polymerases II, IV and V subunit 3
- Protein DEHYDRATION-INDUCED 19 homolog 2
- U11/U12 small nuclear ribonucleoprotein 31 kDa protein
- Pathogenic type III effector avirulence factor Avr AvrRpt-cleavage: cleavage site protein
- AT5G18310 protein
- Leucine carboxyl methyltransferase
- U11/U12 small nuclear ribonucleoprotein 65 kDa protein
- DNA-directed RNA polymerases II, IV and V subunit 11
Sequence:
MVFGQVVIGPPGSGKTTYCNGMSQFLSLMGRKVAIVNLDPANDALPYECGVNIEELIKLEDVMSEHSLGPNGGLVYCMEYLEKNIDWLESKLKPLLKDHYILFDFPGQVELFFIHDSTKNVLTKLIKSLNLRLTAVQLIDSHLCCDPGNYVSSLLLSLSTMLHMELPHVNVLSKIDLIGSYGKLAFNLDFYTDVQDLSYLEHHLSQDPRSAKYRKLTKELCSVIEDYSLVNFTTLDIQDKESVGDLVKLIDKSNGYIFAGIDASVVEYSKIAIGQTDWDYNRVAAVQEKYMEDEEIQD
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B (Q381V0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Serine/threonine-protein kinase, putative
- separase
- Uncharacterized protein
- Protein phosphatase 2A regulatory subunit, putative
- Serine/threonine protein phosphatase 2a regulatory subunit, putative
- Protein phosphatase methylesterase 1
- Serine/threonine-protein phosphatase
- Serine/threonine specific protein phosphatases domain-containing protein
- Serine/threonine-protein phosphatase
- EF-hand domain-containing protein
Sequence:
MSDQDGNHSPSPSPSPCCSMESSAETLSCRGSRAESEVPHRSHLPKSDRQSRVRDEQLQRKRGGKCLESCSLYKSQVQENEVTGLNEPKGVETKLRKDRPRHHNNRGKRGARRDGGSNREGKLPTKGTAAVTATASGSSGRNVESPEWSKDVADSDNNSSYLSRGGGNGFKLFQKLCHPFSTHDVMPRWGPCSHKPEATDSAELEAIGDFMVTNSGDAGGMRSVLRKVANTIPSRVNSMALSVLPNFATGSSLIAIGVGDANGRVNYCEIPVGDAKLSRPSLSSQRKSESVVTTASQCRTDMDVSSISTSIPSVSPRQQLDTFGFQQQSVRKHTHQAYVEELDCLTSVPISQSVNCFQFLRPHLSPSTVSYLTSNDRVIKLFRVQREGLSMFHAFPEMESIVGPELSKTKYFPCATLPSLILPARVYSGNHINRIHGLSVCADDQSFLSVDDLEVFWWNFECADGSNGSRIADMRPPSGNMDDVVELVTTAGFHPTHNSLFFVGRNSGFLGIGDLREAATGAQRRYSTYVRGRAGAGWNSRLQDYGEILCSVSAAGFIGTDHIVTRDYFSLKLWDLRRTSEPCDMVRLMPYVEPYLRSLYESDAIFDRFSAAVDHVSGTIITGLYDGAVAAWQPFHSGRPGGEEILTFYRADPLALLCEVENGGRVTVETLQASFSRRLGVYCSTHSECGQFHQTHLPEPIANRVTCVSISEGGDRFAMSLRDGRGVFLFER