wanglab/gogpt-training-data huggingface dataset:
Protein: Adhesin (O32641)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MIKKNRTLFLSLALCASISYAEDDGGFFTVGYQLGQVMQDVQNPGGAKSDELARELNADVTNNILNNNTGGNIAGALSNAFSQYLYSLLGAYPTKLNGSDVSANALLSGAVGSGTCAAAGTAGGTSLNTQSTCTVAGYYWLPSLTDRILSTIGSQTNYGTNTNFPNMQQQLTYLNAGNVFFNAMNKALENKNGTSSASGTSGATGSDGQTYSTQAIQYLQGQQNILNNAANLLKQDELLLEAFNSAVAANIGNKEFNSAAFTGLVQGIIDQSQAVYNELTKNTISGSAVISAGINSNQANAVQGRASQLPNALYNAQVTLDKINALNNQVRSMPYLPQFRAGNSRSTNILNGFYTKIGYKQFFGKKRNIGLRYYGFFSYNGASVGFRSTQNNVGLYTYGVGTDVLYNIFSRSYQNRSVDMGFFSGIQLAGETFQSTLRDDPNVKLHGKINNTHFQFLFDFGMRMNFGKLDGKSNRHNQHTVEFGVVVPTIYNTYYKSAGTTVKYFRPYSVYWSYGYSF
Protein: Protein PELOTA 2 (AtPelota2) (Q9M2H7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal chromosome segregation during cell division and genomic stability (By similarity). May function in recognizing stalled ribosomes and triggering endonucleolytic cleavage of the mRNA, a mechanism to release non-functional ribosomes and degrade damaged mRNAs. May have ribonuclease activity (Potential).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P48612}. Nucleus {ECO:0000250|UniProtKB:P48612}.
Interaction partners:
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Protein PELOTA 1
- Large ribosomal subunit protein eL38z/eL38y
- DExH-box ATP-dependent RNA helicase DExH11
- Large ribosomal subunit protein uL18y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Tetratricopeptide repeat protein SKI3
- Large ribosomal subunit protein eL42z/eL42y
- Small ribosomal subunit protein uS12z
- Small ribosomal subunit protein uS12y
Sequence:
MKIIRKDFVRNGPGSVKMMAEDSDDLWYTYNLIGPEDSVMAITFRKVGGEGRDSTPSLSRIESKYLGKKRSFTRTERVKLKLEVQVEEVDYDKDGDVMRIRGKNIMENEHVRIGAFHTLEIELKRPFLLRKENWDSLALDTLKQASDLAASADLAVVLMQEGLAQIFLAGKSVKSCGARIKTSIPWKHGAGTAGYESVLKKFFENVVQAFLKHVDFSVVRCAVIASPGFTKDQFHRHLLLEAERRQLRPILENKSRFILVHTNSGYKHSLSEVLHDPNVMNMIKDTKAAKEVKALNDFFTMFSNDPNRACYGPKHVEVAHERMAIQTLLIIDGLFRNSDVKTRKKYVDFVESVKDSGGEVFIFSSMHASGEQLAQHTGIAAILRFPLPDLEDIEM
Protein: Brevinin-2Rj (C0HL02)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000269|PubMed:28012108}.
Interaction partners:
Sequence:
GIFLDKLKNFGKDVAGILLKKASCALSGQC
Protein: RNA-binding protein NOB1 (Q383J3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PNO1 second type I KH domain-containing protein
- Bystin, putative
- Protein LTV1 homolog
- Serine/threonine-protein kinase RIO2
- Bms1-type G domain-containing protein
- 40S ribosomal protein S17, putative
- Serine/threonine-protein kinase RIO1
- 40S ribosomal protein S14
- 40S ribosomal protein S15, putative
- Small ribosomal subunit protein uS4
Sequence:
MSWAALVEKAKDVTPAVTEPKRVAFAVEPGEGRKKESNSAEGKDGNDVVGDVVGVEVPSFSKGLLVLDANAFIKGMNLLDGTADALVTTSQVISEVRDRAARQMLERLPTHLHVLEPSKESVTAIVNIAQKTGDLGTLSRTDIRVCALALDCCKATNTLLEPIAPRAAVINPECSDGTKIVTELKDESEEAQSEDDQNDEGVADHKNDTERGDDDDEGWITPENIHLCKANEGSSAGAAAGERFECGVACVTSDYAMQNTLLHVGVPIVGPHGMRIREVRQWLLRCTACFTINADTTRQFCSECGSGNTLRRVQYVVTTDGERQLFINFRKRISTRGTVYNLPKPRGGRRGTNRCLVLREDQLAHLIRGTTSMKMKEKLATRSGNGGLDDDLAAFGEAPKQRKRDPDQPRVTSSYHKYNVNERKKLRAARRK
Protein: Nucleoporin 98-96 (Q867W7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SKYGLGDSDEEDELPTDPKKAKISTLEAQQRANAEKMTLNSLRQAQKISEDAARNLDPKALVAGVASGFRPMDDTAEFLLMDKTQFFQAGGNSDFSMFDPPRQRPTITSPTAVLAQEMVGNEAHKMQLMKSSFFVEDNAPEDEPMETTGRLLRHRKFFNVEPLVWKDGASESSSQYDFEHPSPALPISSSVSEASLMCDAHYEETSSMATGSIVAAVKETKFEMPVTKAFKFVCKPKVAPIKLRATTVPLPRSIAYEMRDNWIADLGFYKGRSFKLSFGPQNSLVLPSTYNNMQNLKEFTGPSLPVSMVFAPRSATDLSPSVMQLVEFNMVKGNEGFRESIIPHLEVQLNDCLSVNVEGSECPCIHPDSGTKLISKHFSESLKQRNAGLKEDYSVSVWSLLFALWGDHDELVDLEKNSHYMVMCRRNLLSEWLENTLLGKDLLSKKVSTHSYLEHMLDLLSCHRVNEACELAFSYDDANLALVLSQLSSGAVFRLLMEEQLFAWQQSKSDKYIDLERLKMYMLAAGAPMMQSSHGAINLLENKNWLTALALQLWYFTAPTSSITDALNAYNDAFQAEECYAEPPKPSYRDAPTDTKKPVYDLRYHLLQLHSKRMHSLEETLNPITHTADAMDFRLSWLLLQTLRALGYRHCSPLTEARLSVDFASQLENEGLWQWGIFVLLHIKQQTQRERAVQQMLQRNVSVSAKVALYAEERFIVEELGIPMSWVDYAKAVKAGASGKHHLQAKYLLKAKHFATAHDVIFQHIAPDAIINGKMKYLHSLLIQFEDTEGSSIRVPNWANQGQIFLDFIDISAKFKQIRSVTNIADINARWENLKPQLSELCSRISLLPCPTSKHRLCQSEISQSLSCLVHGMCIVCPEMESSTVLKVALERLPLPQEFASKELRIWLEELLDKIQNEPPFSERQQPTMMEI
Protein: GH14208p (Rhodopsin 7) (Q9VTU7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
Sequence:
MEAIIMTTLPNLTTDAGDSSFWLTGALSLSEMLANSSHSHSTGSTTSTAGSSATESSAVNVGKDHDKHVNDSVSTGLSNYSNYPSYIHYRDKYDLSYIAKVNPFWLQFEPPKSSTFLIMAALYCLISVVGCVGNAFVIFMFANRKSLRTPANILVMNLAICDFLMLIKCPIAIYNNIKEGPALGDIACRLYGFVGGLSGTCAIGTLTAIALDRYNVVVHPLQPLRRCSRLRSYLIILLIWCYSFLFAVMPALDIGLSVYVPEGFLTTCSFDYLNKEMPARIFMALFFVAAYCIPLTSIVYSYFYILKVVFTASRIQSNKDKAKTEQKLAFIVAAIIGLWFLAWSPYAIVAMMGVFGLERHITPLGSMIPALFCKTAACVDPYLYAATHPRFRVEVRMLFYGRGVLRRVSTTRSSYMTRSRSSFTHRLRTSTTGEGGMGDHRMENYLMNNNLMMVPEETEENEEIVVVAEINNSISSVMEQSKF
Protein: KLF transcription factor 4 (A0A8I5ZW83)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEDWWETSEQWPGCPLTPGLCAPRPARRQPPGESDMAVSDALLPSFSTFASGPAGREKTLRPAGAPTNRWREELSHMKRLPPLPGRPYDLAATVATDLESGGAGAACSSNNPALPRRETEEFNDLLDLDFILSNSLSHQESVAATVTTSASASSSSSPASSGPASAPSTCSFSYPIRAGGDPGVAAGNTGGGLLYSRESAPPPTAPFNLADINDVSPSGGFVAELLRPELDPVYIPPQQPQPPGGGLMGKFVLKASLSTPGSEYTSPSVISVSKGSPDGSHPVVVAPYSGGPPRMCPKIKQEAVPSCTVSRSLEAHLSAGPQLSNGHRPNTHDFPLGRQLPTRTTPTLSPEELLNSRDCHPGLPLPPGFHPHPGPSYPPFLPDQMQSQVPSLHYQELMPPGSCLPEEPKPKRGRRSWPRKRTATHTCDYAGCGKTYTKSSHLKAHLRTHTGEKPYHCDWDGCGWKFARSDELTRHYRKHTGHRPFQCQKCDRAFSRSDHLALHMKRHF
Protein: Putative beta-D-xylosidase (EC 3.2.1.-) (PpAz152) (P83344)
Organism: Prunus persica (Peach) (Amygdalus persica)
Function: May be involved in cell wall metabolism, related to senescence.
Interaction partners:
Sequence:
ADAIKAGLDLDCGPFLAIHTEAAVRRGLVSQLEINWALANTMTVQMRLGMFDGEPSAHQYGNLGPRDVCTPAHQQLALEAARQGIVLLENRGRSLPLSTRRHRTVAVIGPNSDVTVTMIGNYAGVACGYTTPLQGIGRYTRTIHQAGCTDVHCNGNQLFGAAEAAARQADATVLVMGLDQSIEAEFVDRAGLLLPGHQQELVSRVARASRGPTILVLMSGGPIDVTFAKNDPRISAIIWVGYPGQAGGTAIANVLFGTANPGGKLPMTWYPQNYVTHLPMTDMAMRADPARGYPGRTYRFYIGPVVFPFGLGLSYTTFAHNLAHGPTLVSVPLTSLKATANSTMLSKTVRVSHPDCNALSPLDVHVDVKNTGSMDGTHTLLVFTSPPDGKWASSKQLMGFHKIHIATGSEKRVRIAVHVCKHLSVVDRFGIRRIPLGEHKLQIGDLSHHVSLQTNLGEIKV
Protein: V-type proton ATPase subunit D 2 (V-ATPase subunit D 2) (Vacuolar H+ ATPase subunit 36-3) (Vacuolar proton pump subunit D 2) (Q9NEF6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d 1
- Probable V-type proton ATPase subunit d 2
- V-type proton ATPase subunit G
- H
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit H
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MAAKDRLPIFPSRGAQTLMKSRLAGATKGHGLLKKKADALQMRFRLILGKIIETKTLMGQVMKEAAFSLAEVKFTTGDINQIVLQNVTKAQIKIRTKKDNVAGVTLPIFEPYTDGVDTYELAGLARGGQQLAKLKKNYQSAVRLLVQLASLQTSFVTLDDVIKVTNRRVNAIEHVIIPRINRTIEYIISELDELEREEFYRLKKIQDKKREARKASDKLRAEQRLLGQMAEAQEVQNILDEDGDEDLLF
Protein: Butyrophilin subfamily 2 member A2 (A4QPC6)
Organism: Mus musculus (Mouse)
Function: Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Perilipin-2
- CD209 antigen-like protein E
- Xanthine dehydrogenase/oxidase
Sequence:
MEPTTSLRSCPIASLLFFLVLSLFVLVSAQFTVIGPAEPILAMVGENTTLHCHLSPERNAEEMEVRWFRWRFFPAVLVYRGHQERPEEQMVAYRGRTTFMRTDISKGRVALIIHNVTAYDNGIYCCYFQEGRSYDQATMKLMVASLGSEPLIKMKTLEDGSILLECTSEGWYPEPRAVWRDPYDEVVPALEEEYTADREGLFTVTMTIIIRDCSVRNMTCSVNNTLLSQEVESVILIPESFVPSLPLWMVAVAVTLPVVMLILLTSGSICLVKKHRRKKSILSAEKEAEYEEKEAARQLQEELRWRRTLLHAADVVLDPDTAHPELFLSDDQRSVIRGSSRQSVPDNPERFDCRPCVLGRESFSSGKHYWEVEVENVMVWAIGVCRDSVERKGEALLVPQNGFWTLEMFGSQYRALSSPEKIIPLKERLHRIAVFLDCEGGDISFYNMRDRSHIYTCPPVTFTGPLRPFFRLGSDDSPLFICPAFTGAQGVTIPEGGLFLYKTRPISQSLVRKP
Protein: Eukaryotic peptide chain release factor subunit 1-3 (Eukaryotic release factor 1-3) (eRF1-3) (Omnipotent suppressor protein 1 homolog 3) (SUP1 homolog 3) (P35614)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. Modulates plant growth and development.
Subcellular location: Cytoplasm.
Interaction partners:
- T10F20.8 protein
- Eukaryotic peptide chain release factor subunit 1-2
- Eukaryotic peptide chain release factor subunit 1-1
- ABC transporter E family member 1
- AT5g45350/MFC19_1
- ABC transporter E family member 3
- ABC transporter E family member 2
- At3g16040
- F9L1.21 protein
- Large ribosomal subunit protein uL14x/uL14z/uL14y
Sequence:
MADQESDKNIEIWKIKKLIKGLETARGNGTSMISLIMPPRDQVARVTKMLADEYGTASNIKSRVNRQSVLSAITSAQQRLKLYNKVPPNGLVLYTGTIVTDDGKEKKVTIDFEPFKPINASLYLCDNKFHTEPLNELLESDDKFGFIVMDGNGTLFGTLSGNTREVLHKFTVDLPKKHGRGGQSALRFARLRMEKRHNYVRKTAELATQFYINPATSQPNVSGLILAGSADFKTELSQSELFDPRLQAKILNVVDVSYGGENGFNQAIELSAEILSNVKFIQEKKLIGKYFEEISQDTGKYVFGVEDTLKALEMGAVETLIVWENLDINRYELKNNTTGEIVIKHLGKDQENNQSNFHDAETNAELEVQEKMPLLEWFANEYKRFGCTLEFVTNKSQEGSQFCRGFGGIGGLLRYQLDMRTFDELSDGEVYEDSD
Protein: Protein SDA1 homolog (Nucleolar protein 130) (SDA1 domain-containing protein 1) (hSDA) (Q9NVU7)
Organism: Homo sapiens (Human)
Function: Required for 60S pre-ribosomal subunits export to the cytoplasm.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11790298, ECO:0000269|PubMed:14976432}.
Interaction partners:
- GTP-binding protein 4
- Ribosome biogenesis protein NOP53
- Nucleolar GTP-binding protein 2
- Notchless protein homolog 1
- Ribosome biogenesis protein NSA2 homolog
- Proliferation-associated protein 2G4
- Guanine nucleotide-binding protein-like 3-like protein
- mRNA turnover protein 4 homolog
- WD repeat-containing protein 18
- Guanine nucleotide-binding protein-like 3
Sequence:
MSNRNNNKLPSNLPQLQNLIKRDPPAYIEEFLQQYNHYKSNVEIFKLQPNKPSKELAELVMFMAQISHCYPEYLSNFPQEVKDLLSCNHTVLDPDLRMTFCKALILLRNKNLINPSSLLELFFELFRCHDKLLRKTLYTHIVTDIKNINAKHKNNKVNVVLQNFMYTMLRDSNATAAKMSLDVMIELYRRNIWNDAKTVNVITTACFSKVTKILVAALTFFLGKDEDEKQDSDSESEDDGPTARDLLVQYATGKKSSKNKKKLEKAMKVLKKQKKKKKPEVFNFSAIHLIHDPQDFAEKLLKQLECCKERFEVKMMLMNLISRLVGIHELFLFNFYPFLQRFLQPHQREVTKILLFAAQASHHLVPPEIIQSLLMTVANNFVTDKNSGEVMTVGINAIKEITARCPLAMTEELLQDLAQYKTHKDKNVMMSARTLIHLFRTLNPQMLQKKFRGKPTEASIEARVQEYGELDAKDYIPGAEVLEVEKEENAENDEDGWESTSLSEEEDADGEWIDVQHSSDEEQQEISKKLNSMPMEERKAKAAAISTSRVLTQEDFQKIRMAQMRKELDAAPGKSQKRKYIEIDSDEEPRGELLSLRDIERLHKKPKSDKETRLATAMAGKTDRKEFVRKKTKTNPFSSSTNKEKKKQKNFMMMRYSQNVRSKNKRSFREKQLALRDALLKKRKRMK
Protein: tRNA sulfurtransferase (EC 2.8.1.4) (Sulfur carrier protein ThiS sulfurtransferase) (Thiamine biosynthesis protein ThiI) (tRNA 4-thiouridine synthase) (P77718)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Subcellular location: Cytoplasm.
Interaction partners:
- Cysteine desulfurase IscS
- Sulfur carrier protein ThiS adenylyltransferase
- Thiazole synthase
- Sulfur carrier protein TusA
- tRNA-specific 2-thiouridylase MnmA
- tRNA-cytidine
- Sulfurtransferase TusE
- Molybdopterin synthase sulfur carrier subunit
- 2-iminoacetate synthase
- Iron-sulfur cluster assembly scaffold protein IscU
Sequence:
MKFIIKLFPEITIKSQSVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHHILEVEDVPFTDMHDIFEKALVQYRDQLEGKTFCVRVKRRGKHDFSSIDVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLLIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEILEKIDDGQMGVILKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTEDFARTMPEYCGVISKSPTVKAVKSKIEAEEEKFDFSILDKVVEEANNVDIREIAQQTEQEVVEVETVNGFGPNDVILDIRSIDEQEDKPLKVEGIDVVSLPFYKLSTKFGDLDQNKTWLLWCERGVMSRLQALYLREQGFNNVKVYRP
Protein: Lysozyme D (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase D) (Q556Y7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Has antibacterial activity.
Subcellular location: Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:Q554H2}.
Interaction partners:
Sequence:
MRLLVTLILLIFVLTVSGQYSCSNPCYGNMCCSIPSNNEYYLTTFCDESTACGTPCSAQTYFTADSQRFGCGVTLTICSTSGGSTTTGGTGSAGTSTSSGSGSGSGSGSGSGSGSGSGTSGSSSSGSSSGSGSGSSSGSGGSSGSGSGSTMETGGFYGVCVKAITIDAGPNISVEEEAGMAIIDASSQICQDLFGSSSCGWSDKRSITAVQSSVEDGFPVNKPFNVTFEDYNKIISNSLILDQQCSNKNNCKYNKLELMK
Protein: Anthranilate synthase component 2 (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase, GATase component) (Anthranilate synthase, glutamine amidotransferase component) (P20576)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Interaction partners:
- Anthranilate synthase component 1
- Anthranilate synthase component 1, pyocyanine specific
- Anthranilate phosphoribosyltransferase
- aminodeoxychorismate synthase
- Indole-3-glycerol phosphate synthase
- N-
- anthranilate synthase
- Tryptophan synthase beta chain
- Chorismate synthase
- Bifunctional chorismate mutase/prephenate dehydratase
Sequence:
MLLMIDNYDSFTYNLVQYFGELKAEVKVVRNDELSVEQIEALAPERIVLSPGPCTPNEAGVSLAVIERFAGKLPLLGVCLGHQSIGQAFGGEVVRARQVMHGKTSPIHHKDLGVFAGLANPLTVTRYHSLVVKRESLPECLEVTAWTQHADGSLDEIMGVRHKTLNVEGVQFHPESILTEQGHELLANFLRQQGGVRGEGN
Protein: UBX domain protein 7 (C9JAT7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
Protein: DNA repair protein Rad9 (Q38EW7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLLKFTATGDFLRPFINLLQATTKQGVVLFFQPLDNVLVLRTVGPNSTLYLVASVGTEHFHEYRYDKGDATADSFAVDGILEAGKDSSAEVNNMEHHVPVLSRALLATVLRQPQGLHLISVQYSSRDGDGISKDVMQWECVCGDGIVKVFMLPLVREKLERAYVNPERYVFDACASAKTWGHFLRHLPGSQFIVVQPHDTHLELLVMNCSEAAGHEVDSKVLVRQGDLLFMRRIHRATEGNDDGYSLLPGKYAELKPLKHICLLADQLGMMIRLRSAMGGVPLFVETLTMQEAQSLKAGGAPTVSMDTVIDTTAPDLYNRGMAPISSSLRIRYAVYIPAIDIWPSSADSFDAPTDGGRRSVASTATSHRDSRDLTNIASPRGSVGLPQADPCLGCAETPVASATTAVNGVTSAPLPTGLHFGTNQVGTGGGLNPQTLASPTPAPLTSGYSVGSPVISAQSAPSYDPPPSGVVIDGNMMMVRSTFQVGNSVGSEHTNYKRSRDNVTSERSSALPFSLSERVPCTDNFGPQPIEQRGHESTTWSTLTPERRSSFQLNHDEQSKLPPMGSRQLPLDARYPLDFNAYVLELDEGRCEDDLDEDDEDLQRFLDSCASVLVVPQTQSY
Protein: Beta-galactosidase-1-like protein 2 (EC 3.2.1.-) (Q8IW92)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MTTWSLRRRPARTLGLLLLVVLGFLVLRRLDWSTLVPLRLRHRQLGLQAKGWNFMLEDSTFWIFGGSIHYFRVPREYWRDRLLKMKACGLNTLTTYVPWNLHEPERGKFDFSGNLDLEAFVLMAAEIGLWVILRPGPYICSEMDLGGLPSWLLQDPGMRLRTTYKGFTEAVDLYFDHLMSRVVPLQYKRGGPIIAVQVENEYGSYNKDPAYMPYVKKALEDRGIVELLLTSDNKDGLSKGIVQGVLATINLQSTHELQLLTTFLFNVQGTQPKMVMEYWTGWFDSWGGPHNILDSSEVLKTVSAIVDAGSSINLYMFHGGTNFGFMNGAMHFHDYKSDVTSYDYDAVLTEAGDYTAKYMKLRDFFGSISGIPLPPPPDLLPKMPYEPLTPVLYLSLWDALKYLGEPIKSEKPINMENLPVNGGNGQSFGYILYETSITSSGILSGHVHDRGQVFVNTVSIGFLDYKTTKIAVPLIQGYTVLRILVENRGRVNYGENIDDQRKGLIGNLYLNDSPLKNFRIYSLDMKKSFFQRFGLDKWSSLPETPTLPAFFLGSLSISSTPCDTFLKLEGWEKGVVFINGQNLGRYWNIGPQKTLYLPGPWLSSGINQVIVFEETMAGPALQFTETPHLGRNQYIK
Protein: Cytochrome c biogenesis protein CcsA (Q6ENA8)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01391}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01391}.
Interaction partners:
- Uncharacterized protein
- ResB-like domain-containing protein
- Cytochrome C biogenesis protein transmembrane domain-containing protein
- Uncharacterized protein
- uroporphyrinogen-III C-methyltransferase
Sequence:
MLFATLEHILTHISFSTISIVITIHLITLLVRELGGLRDSSEKGMIATFFCITGFLVSRWASSGHFPLSNLYESLIFLSWALYILHMIPKIQNSKNDLSTITTPSTILTQGFATSGLLTEMHQSTILVPALQSQWLMMHVSMMLLSYATLLCGSLLSAALLMIRFRKNLDFFSKKKKNVLLKTFFFNEIEYFYAKRSALKSTFFPLFPNYYKYQLIERLDSWSYRVISLGFTLLTIGILCGAVWANEAWGSYWNWDPKETWAFITWTIFAIYLHSRTNPNWKGTKSAFVASIGFLIIWICYFGINLLGIGLHSYGSFTLPI
Protein: Importin subunit beta (Karyopherin subunit beta) (Protein ketel) (O18388)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. In Drosophila, may not function as a snRNP import receptor as it does not interact with components of the snRNP complex such as snRNP U1, U2, U4/U6 and Snup.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11102382}. Note=In cleavage embryos.
Interaction partners:
- Snurportin-1
- Importin subunit alpha
- GTP-binding nuclear protein Ran
- D-Importin 7/RanBP7
- Nuclear pore complex protein Nup153
- Importin subunit alpha
- Importin subunit alpha
- H/ACA ribonucleoprotein complex subunit 4
- E3 SUMO-protein ligase RanBP2
- Ribosomal RNA-processing protein 8
Sequence:
MTSDIAMQLIAILEKTVSPDKNELLSAKNFLEQAAASNLPEFLKALSEILVNTANSAVARMAAGLQLKNHLTSKDEKVSQQYQDRWHQFPSEIRELIKNNILAALGTENTRPSCAAQCVAYVAVIELPINRWPMLIQTLVNKVVSEGSSEMHRESALEAIGYICQDIRFGVMENQSNDVLTAIIHGMRKVEPSNHVRLAATTALHNSLEFTKSNFEKDMERNFIMEVVCEATQCQDSQICVAALQCLVKIMTLYYQYMEPYMAQALFPITLAAMKSDNDAVALQGIEFWSNVCDEEIDLAIESQEATDQGRAPQRVSKHYARGALQFLTPVLVEKLTKQDECDDEDTWSPAKAASVCLMVLATCCEDEIVPHVLPFIKENIESPNWRFRDAAVMTFGSVLNGLETNTLKPLVEQAMPTLIRLMYDSSVIVRDTIAWTFGRICDIIPEAAINETYLQTLLECFVKSLKSEPRVAANVCWAFIGLSDAAWEAAVTNDGETPETYALSPYFEYIITQLLETTDRSDGAQANLRCAAYQALMDMIKNSPLDCYLVVQRTTLVILERLNQVMQMETQINNHSDRHQFNDLQSLLCATLQSVLRKVHEQDAPQISDAIMTALLTMFNSSAGKSGVVQEEAFLAVSTLVELLGAQFAKYMPAFKDFLVMGLKNFQEYQVCCAAVGLTGDIFRALKDLMVPYSNEIMTVLINNLTEPTIHRTVKPQVLSAFGDIALSIGNHFLPYLSMVLDMLRVASNLQTDANNFDMNEYINELRESILEAYTGIIQGLKGVDQTAHTDVMHMEPHLMHIISFIKRIAQEGDVSDSMLASAAGFIGDLCTSFGPRLYPLLDDAIITQFLAEGKRSKAQRTKMLCTWAVKEIKKINTQVITQ
Protein: Polyubiquitin [Cleaved into: Ubiquitin] (P0CG69)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase parkin
- Ubiquitin carboxyl-terminal hydrolase
- Ubiquitin carboxyl-terminal hydrolase
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 14
- Ubiquitin-conjugating enzyme E2-17 kDa
- E1 ubiquitin-activating enzyme
- ubiquitinyl hydrolase 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIQA
Protein: Cyclin-dependent kinase inhibitor 1C (Cyclin-dependent kinase inhibitor p57) (p57Kip2) (P49919)
Organism: Mus musculus (Mouse)
Function: Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life.
Subcellular location: Nucleus.
Interaction partners:
- Cyclin-dependent kinase 2
- Cyclin-A2
- G1/S-specific cyclin-E1
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 4
- Cyclin-A1
- G1/S-specific cyclin-D1
- S-phase kinase-associated protein 2
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-D3
Sequence:
MGMSDVYLRSRTAMERLASSDTFPVIARSSACRSLFGPVDHEELGRELRMRLAELNAEDQNRWDFNFQQDVPLRGPGRLQWMEVDSESVPAFYRETVQVGRCRLQLGPRPPPVAVAVIPRSGPPAGEAPDGLEEAPEQPPSAPASAVVAEPTPPATPAPASDLTSDPIPEVTLVATSDPTPDPIPDANPDVATRDGEEQVPEQVSEQGEESGAEPGDELGTEPVSEQGEEQGAEPVEEKDEEPEEEQGAEPVEEQGAEPVEEQNGEPVEEQDENQEQRGQELKDQPLSGIPGRPAPGTAAANANDFFAKRKRTAQENKASNDVPPGCPSPNVAPGVGAVEQTPRKRLR
Protein: Rop guanine nucleotide exchange factor 4 (AtRopGEF4) (Rho of plants guanine nucleotide exchange factor 4) (Q0WNP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. In association with ROPGEF1, acts as specific regulator of ARAC10/ROP11 function in ABA-mediated stomatal closure.
Subcellular location: Cytoplasm. Cell membrane. Note=Interacts with ARAC10/ROP11 on plasma membrane in guard cells.
Interaction partners:
- Rac-like GTP-binding protein ARAC10
- Rho GTPase-activating protein 3
- Interactor of constitutive active ROPs 5
- Kinesin-like protein KIN-13A
- Rac-like GTP-binding protein ARAC4
- Rac-like GTP-binding protein ARAC2
- Pollen receptor-like kinase 2
- Protein IQ-DOMAIN 13
- Brefeldin A-inhibited guanine nucleotide-exchange protein 5
- Protein ACTIVITY OF BC1 COMPLEX KINASE 1, chloroplastic
Sequence:
MESSSNSDQNEGTPTSSVSSPYRRTYSDISGLSHRFDVQSFYNRPSNTNAVVLSGHEEDVSEDAEEPKDDVVNDVHGDGDEEDSDIDSAEDAELEMMRERFAKLLLGEDMSGSGKGVCTAVTVSNSITNLYATVFGQSLRLQPLSTEKKDLWKREMNCFMSICDYIVEVIPRSLGTNVEITETKLRSDILMSLPALRKLDNMLMEILDSFTENEFWYVERGSSSMNSGGGGRDSGTFRKVVVQRKDEKWWLPVPCVPAEGLSEEERKHLRHKRDCASQIHKAALAINDSTLNDMDIPDSYLTTLPKSGKASVGDVIYKQLCTAEKFYPDQLLDILKITSEHEALELADKVEASLVTWRRKTGGLTHSKSSWDMMKDISGDADRGNDKNHILAARARSLLFCLKQRYPELSQTSLDICKIQFNRDVGKAVLESYSRVLEGLAYNVVSWIDDVLYVDRTVRNRDD