wanglab/gogpt-training-data huggingface dataset:
Protein: 69 kDa paraflagellar rod protein (Q57UH2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGKEVEGVVSPADQQQPAVPEVTDITLEAARKQKIHNLKLKTACLSNEEYVQDLHVSEWSETQKQKLQAAHEKAHELLASVEGGTKWSLTEAYDIKKLMRVCGLEMSVRELYKPEDKPQFMEIVALKKTMNELKQHHNKTRTVSFTGMIDNAIAKLEKIEDELRRSQLDASEMAQVPVAALKNIEDTMNVAVVQTALLGNEEQIKAQLAAVEKANEIRNVAIADGEMAIAEEQYYIKAQLLEHLVELVADKFRIIGQTEDENKSFSKIHEVQKKSFQESASIKDAKRRLKQHCEDDLRNLHDAIQKADLEDAEAMKRFATQKEKSERFIHENLDKQDEAWRRIQELERVLQRLGTERFEEVKRRIEENDREEKRKVEYQQFLDVCGQHKKLLELSVYNCDLALRCMGMLEEIVAEGCSAVKSRHDKTNDELSDLRLQVHQEYLEAFRRLYKTLGQLVYKKEKRLEEIDRNIRTTHIQLEFAIETFDPNAKLHSDKKKDLYKLRAQVEEELEMLKDKMAQALEMFGPTEDALNQAGIDFVHPAEEVESGNMDRRSKMVEYRAHLAKQEEVKIAAEREELKRSKMLQSQQYRGRTMPQITQ
Protein: V-type proton ATPase catalytic subunit A (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (D4A133)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000256|ARBA:ARBA00029434}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029434}.
Interaction partners:
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit F
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase subunit
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit E 1
Sequence:
MCFKFKSDRASGSGLGTDSALRARAGKFSTMDFSKLPKIRDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWEFIPSKNLRVGSHITGGDIYGIVNENSLIKHKIMLPPRSRGSVTYIAPPGNYDASDVVLELEFEGVKEKLSMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMISFYDMARRAVETTAQSDNKITWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAFRSLED
Protein: G protein signaling modulator 1 (A0A0A0MRC4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPSPAGEGPPLALSLAEKAVCKVVYGAPRPRPLLLPVGLELWLYVQKMRNLQRKRMEASCLELALEGERLCKAGDFKTGVAFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLKEHGRALEYHKHDLLLARTIGDRMGEAKASGNLGNTLKVLGRFDEAAVCCQRHLSIAQEQGDKVGEARALYNIGNVYHAKGKQLSWNAANATQDPGHLPPDVRETLCKASEFYERNLSLVKELGDRAAQGRAYGNLGNTHYLLGNFTEATTFHKERLAIAKEFGDKAAERRAYSNLGNAHVFLGRFDVAAEYYKKTLQLSRQLRDQAVEAQACYSLGNTYTLLQDYERAAEYHLRHLLIAQELADRVGEGRACWSLGNAYVSMGRPAQALTFAKKHLQISQEIGDRHGELTARMNVAQLQLVLGRLTSPAASEKPDLAGYEAQGARPKRTQRLSAETWDLLRLPLEREQNGDSHHSGDWRGPSRDSLPLPVRSRKYQEGPDAERRPREGSHSPLDSADVRVHVPRTSIPRAPSSDEECFFDLLTKFQSSRMDDQRCPLDDGQAGAAEATAAPTLEDRIAQPSMTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRITHSNAGHLRGHGEPQEPGDDFFNMLIKYQSSRIDDQRCPPPDVLPRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGGPEQGAGGPPEPQQQCQPGAS
Protein: Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase (EC 3.2.1.113) (ER alpha-1,2-mannosidase) (ER mannosidase 1) (ERMan1) (Man9GlcNAc2-specific-processing alpha-mannosidase) (Mannosidase alpha class 1B member 1) (A2AJ15)
Organism: Mus musculus (Mouse)
Function: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity).
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Interaction partners:
- Neutral alpha-glucosidase AB
- alpha-1,2-Mannosidase
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
- Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
- Protein OS-9
- Mannosyl-oligosaccharide glucosidase
Sequence:
MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLSLDSCVFNTEAHPLPIWAPA
Protein: Na(+)/H(+) antiporter subunit D (Mrp complex subunit D) (Multiple resistance and pH homeostasis protein D) (O05229)
Organism: Bacillus subtilis (strain 168)
Function: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Na
- Na
- Na
- Na
- Na
- Na
- Probable inorganic carbon transporter subunit DabB
- Iron-sulfur cluster carrier protein
- Ca
Sequence:
MNNFVILPILIPLLSAILLIFMTKNLMLMRIFSTAASAIGIVISGILVQTVFTKGIQTLSLGGWKAPYGIVLAADQFASLLVLTTAIIGLLVGLYSFRSVGEKRERSFYYSGVQFLLAGVSGAFLTGDLFNMYVFFELLLIASYMLIVLGGTKIQLRESLKYIVFNIVSSALFVIGVGFLYAVTGTLNMADLSVKISESGQTGLITVIGVLLLLVFGMKGGIFPLYFWLPGSYYAPPAAISALFGALLTKVGLYAITRVFTLIFIHDTAFTHQLMIWLAALTVIFGVIGSLAYSNVMKIVIYNIITAVGVILFGVAVHTPASIQGAIYYLIHDMLIKGALFMLAGTLIALTGTASLHKMGGLIKRYPVLGWMFFISAISLAGIPPLSGFVGKFKIAEGGFAEGEFTISMLILLSSLLVLYSVLRIFIHAFWGEEKETPKPNHRTAKGLLYPAAIFLLLSLLFGLGTEWVSPYVDQAAETLLNPEKYIEAVLKE
Protein: methionine--tRNA ligase (EC 6.1.1.10) (A0A1D8PP08)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- methionine--tRNA ligase
- arginine--tRNA ligase
- leucine--tRNA ligase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- Arc1p
- methionyl-tRNA formyltransferase
- cystathionine gamma-lyase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- glutamine--tRNA ligase
Sequence:
MRFKIRGPLIQLRYKSTKPFYITTPIFYVNAAPHIGHLYSMLIADTRNKWEKLNPSKESFMLTGTDEHGLKIQSTAEKLGLEPKVLVDKVSQNFSKLAEQFDVNYDRFIRTTDNDHIELVRYFWNLMMEKGFIYTDTHSGWYSISDETFFPETQIEEVVKNGKAVKISSETKNEVVYQKETNYFFKLSMFQEQLIQFLKQNPEFIKPKHRYQFILKELEDTKLPDLSISRPSSRLKWSIEVPNDSTQKIYVWFDALLNYLTATKFPHGFEVQDSKFVTPENSIWPATHVIGKDIIRFHCIYWPIFLMAAGIELPKQVIVHSHWLCDGFKMSKSLGNVVDPMEISEYYGVDPVRFFLVENSNIDDDCKFSEELLQRSRDAVLGKYCNLISRIGGKNFSIEEAVKSSASGEFNNIREIIETYTINKDSVEGLLSSSSKLTTDLNDLYNQMDHYFTNFDYIRAIQCWWSVINQANQIFQSAEPWTYVKLINSPETPAELKEKYRILNNYFVYLCAETTRISSILIQPVMPQLSKKILDRLNVSGRTSEFTTFGADLQYGSGANSKSHKVPLEKIAPRDIK
Protein: Mevalonate kinase (Q9N4Z7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVVIGGDQALDSPSGSTSRAGSSVSATASPMHRNTTSQHGGLFVSAPGKIILFGEHAVVYGRTAIAGSIDLRTYVSLYTSADGRIYLSLPDLGVEKTWMLKDLLKAADRLAAEYPIEEDQPPSLEILVPIARKLSGSCEDQCGVQHLAILAFWYLLLGVAHRKSGLSRLARGLPAPPLPEGLHRTNLSVIGATSAQPEKSEAEIALSLPVPPLTPLPSPGAQSTAPPVFPTSTPTPTSTPTPLLPGNLRADSPAVQQDLLAVKATVRFKLPSCVGLGSSGAYCVCIATSLLQTAGLIPPPSIVADEQGNLTWEEDHLDIIRKWATAAESLIHGRASGLDAAVCTFGGVASFKPGHRIEHLKNLPDLRVILVNSKVERNTARMVQTVKERLKKFPEVVDAMFGSIDAISLDAAKILHRPLLEENGGGDTGSTVQENGLGPFGGNMVEQDHHSLQPTRTASVRSSSLSSYVGGGKRNSSASVISATSEKGENVDTFSKLNDLCRINNQLLIALGVGHPKVDLICTTLARYGIHPKMTGAGGGGSVFAFLKPNTPQTLLDMIDGELRSHGFEVWQPPLGGPGVVEHQTRPELFQTPVSSTQCSTPASKHK
Protein: B6.1 (Q90746)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MDFNSPFILQCLLVITTVTDGSATMIGALSGSSAKFPLGVENFQNVPKMSWNNNNCSTAVVDDTLSAECHPSSKRCLKLENGSLVLRRVEKEDEGNYEFFFNDTKVLFTLKVFEPIIDARCFPNGTADLTCNVDSNENMTFEWKLNNSWPNANGACVKDGGKKVRLEKTVPGEFVCKVTYNNDFVWTRPIVLSCSYGDLLQYPWFIYILAGCAGAAAILVAVVSSLICCCMRRKHKFLPVPSDEEKDDGITMSVVSSEGVKSPPNGDHVEAQAAQIACPPMPDAARPDSGIVPQPMVEENFPVAVEPGEMPDPEMIADVESQENASNCFPDPIDN
Protein: Nectin-2 (Herpes virus entry mediator B) (Herpesvirus entry mediator B) (HveB) (Nectin cell adhesion molecule 2) (Poliovirus receptor-related protein 2) (CD antigen CD112) (Q92692)
Organism: Homo sapiens (Human)
Function: Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive. Probable cell adhesion protein.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Afadin
- Nectin-3
- CD226 antigen
- T-cell immunoreceptor with Ig and ITIM domains
- T-cell surface protein tactile
- Transmembrane protein PVRIG
- Atypical chemokine receptor 1
- NKG2-D type II integral membrane protein
- Natural cytotoxicity triggering receptor 3
- Nectin-1
Sequence:
MARAAALLPSRSPPTPLLWPLLLLLLLETGAQDVRVQVLPEVRGQLGGTVELPCHLLPPVPGLYISLVTWQRPDAPANHQNVAAFHPKMGPSFPSPKPGSERLSFVSAKQSTGQDTEAELQDATLALHGLTVEDEGNYTCEFATFPKGSVRGMTWLRVIAKPKNQAEAQKVTFSQDPTTVALCISKEGRPPARISWLSSLDWEAKETQVSGTLAGTVTVTSRFTLVPSGRADGVTVTCKVEHESFEEPALIPVTLSVRYPPEVSISGYDDNWYLGRTDATLSCDVRSNPEPTGYDWSTTSGTFPTSAVAQGSQLVIHAVDSLFNTTFVCTVTNAVGMGRAEQVIFVRETPNTAGAGATGGIIGGIIAAIIATAVAATGILICRQQRKEQTLQGAEEDEDLEGPPSYKPPTPKAKLEAQEMPSQLFTLGASEHSPLKTPYFDAGASCTEQEMPRYHELPTLEERSGPLHPGATSLGSPIPVPPGPPAVEDVSLDLEDEEGEEEEEYLDKINPIYDALSYSSPSDSYQGKGFVMSRAMYV
Protein: Membrin-12 (AtMEMB12) (Golgi SNAP receptor complex member 2-2) (Q9FK28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Bet1-like SNARE 1-2
- Bet1-like SNARE 1-1
- Syntaxin-31
- Syntaxin-32
- Golgi SNAP receptor complex member 1-2
- Golgi SNAP receptor complex member 1-1
- VAMP-like protein YKT62
- VAMP-like protein YKT61
- 25.3 kDa vesicle transport protein SEC22-1
- SNARE-like superfamily protein
Sequence:
MASGTVGGLSEVYSSAKRILLRARNGIEKLERFDSDPTDLASSVKRDITEVQSLCSNMDGLWRSIPVKSQRDLWRRKSEQVGEEAEYLNQSLEKYMWRNQRKMLEAKERADLLGRGSGEGAHILQIFDEEAQGMNSVKNSKRMLEDSFQSGVAILSKYAEQRDRLKSAQRKALDVLNTVGLSNSVLRLIERRNRVDTWIKYAGMIATLVILYLFIRWTR
Protein: 14-3-3-like protein GF14 iota (General regulatory factor 12) (Q9C5W6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- Dual specificity phosphatase Cdc25
Sequence:
MSSSGSDKERETFVYMAKLSEQAERYDEMVETMKKVARVNSELTVEERNLLSVGYKNVIGARRASWRIMSSIEQKEESKGNESNVKQIKGYRQKVEDELANICQDILTIIDQHLIPHATSGEATVFYYKMKGDYYRYLAEFKTEQERKEAAEQSLKGYEAATQAASTELPSTHPIRLGLALNFSVFYYEIMNSPERACHLAKQAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDLPEDGGEDNIKTEESKQEQAKPADATEN
Protein: DNA-damage inducible protein DDI1-like protein (Q38FA2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
- UV excision repair protein RAD23
- UV excision repair RAD23 protein, putative
Sequence:
MKITCTDESGNVYSAELDPTAMVEDLSVLVEVEIGIPVEEQLLMAPTGAILRLDETFGAQGITTDCCVTVRRQVLGGGLKRPAEERPDRIPEVQASEERSHILELYATELMSDQDQLQQLVSPEFDETDPAIQSRIYEEISKRNVEENLANALEFAPEAFTRVSMLHVTVEINKVKVKALVDCGAQTSVVSAATAERCGINWLVDKRAVGTVHGVGEQRSLGRIHLTQANLGGLFIPISLVVLESETFDLIIGLDQMKKHRMIIDLKDDCLRVGGTAIPFLSDSEVSEEPHRGTPFVLGGGDGNEDNNAADVPTAGANQGTAAKRSTAPSGPNISSAEKEQAIETFVSLTHLERQQAIALLEAVNWNPHAAMSLLMEE
Protein: Polygalacturonase (PG) (EC 3.2.1.15) (PGase SM) (Pectinase) (P47180)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein ISD11
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL21B
- Large ribosomal subunit protein eL21A
Sequence:
MISANSLLISTLCAFAIATPLSKRDSCTLTGSSLSSLSTVKKCSSIVIKDLTVPAGQTLDLTGLSSGTTVTFEGTTTFQYKEWSGPLISISGSKISVVGASGHTIDGQGAKWWDGLGDSGKVKPKFVKLALTGTSKVTGLNIKNAPHQVFSINKCSDLTISDITIDIRDGDSAGGHNTDGFDVGSSSNVLIQGCTVYNQDDCIAVNSGSTIKFMNNYCYNGHGISVGSVGGRSDNTVNGFWAENNHVINSDNGLRIKTVEGATGTVTNVNFISNKISGIKSYGIVIEGDYLNSKTTGTATGGVPISNLVMKDITGSVNSTAKRVKILVKNATNWQWSGVSITGGSSYSGCSGIPSGSGASC
Protein: Putative pentatricopeptide repeat-containing protein At1g12700, mitochondrial (P0C7Q7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Cleavage stimulating factor 64
Sequence:
MMIKRSITTNMKALRLIQPHLLKTGSLRTDLLCTISSFFSSCERDFSSISNGNVCFRERLRSGIVDIKKDDAIALFQEMIRSRPLPSLVDFSRFFSAIARTKQFNLVLDFCKQLELNGIAHNIYTLNIMINCFCRCCKTCFAYSVLGKVMKLGYEPDTTTFNTLIKGLFLEGKVSEAVVLVDRMVENGCQPDVVTYNSIVNGICRSGDTSLALDLLRKMEERNVKADVFTYSTIIDSLCRDGCIDAAISLFKEMETKGIKSSVVTYNSLVRGLCKAGKWNDGALLLKDMVSREIVPNVITFNVLLDVFVKEGKLQEANELYKEMITRGISPNIITYNTLMDGYCMQNRLSEANNMLDLMVRNKCSPDIVTFTSLIKGYCMVKRVDDGMKVFRNISKRGLVANAVTYSILVQGFCQSGKIKLAEELFQEMVSHGVLPDVMTYGILLDGLCDNGKLEKALEIFEDLQKSKMDLGIVMYTTIIEGMCKGGKVEDAWNLFCSLPCKGVKPNVMTYTVMISGLCKKGSLSEANILLRKMEEDGNAPNDCTYNTLIRAHLRDGDLTASAKLIEEMKSCGFSADASSIKMVIDMLLSGELDKSFLDMLS
Protein: Actin, aortic smooth muscle (EC 3.6.4.-) (Alpha-actin) [Cleaved into: Actin, aortic smooth muscle, intermediate form] (P08023)
Organism: Gallus gallus (Chicken)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Myosin-11
- Myosin regulatory light chain 2, smooth muscle major isoform
- Myosin-9
- Myosin light polypeptide 6
- Tropomyosin alpha-1 chain
- Transgelin
- Vinculin
- Dynactin subunit 2
- Calponin
- Calponin
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILSERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: Ornithine aminotransferase (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase) (Q92413)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm.
Interaction partners:
- Arginase
- Acetylglutamate kinase
- Hypothetical arginase family protein
- Ornithine decarboxylase
- Glutamate 5-kinase
- L-glutamate gamma-semialdehyde dehydrogenase
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Aldehyde dehydrogenase domain-containing protein
- Ornithine carbamoyltransferase, mitochondrial
- argininosuccinate lyase
Sequence:
MTSNGTNGSATAYHASSTQEAIQAENDFAAHNYHPLPVVFARAQGTSVWDPEGRHYLDFLSAYSAVNQGHCHPKLVAALVDQASRLTLSSRAFYNDVFPKFAEMVTKYFGFDMVLPMNTGAEAVETGIKIARKWGYKVKGIPENEAIILSAENNFHGRTMAAISLSSDPESRENYGPYVPNIGCTIPGTEKPITYNDKAALREAFEKAGSNLAAFLVEPIQGEAGIIVPDDDYLQLARSLCDQHNVLLICDEIQTGIARTGKLLCHEWSGIKPDMVLLGKAISGGMYPVSCVLGRKDVMLTVEPGTHGSTYGGNPLACAVAIRALEVVQEENMVERAEKLGQAFRSGLEAIQNPIIQTVRGKGLLNAIVIDESKTNGHTAWDLCMLMKEKGLLAKPTHQNIIRLAPPLVITEEEIAKALEIIKAAVAELPNLKGAAEDKVVPPPEKKVKITLEN
Protein: Mortality factor 4-like protein 2 (Q5JXX1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSRKQGSQPRGQQSAEEENFKKPTRSNMQRSKMRGASSGKKTAGPQQKNLEPALPGRWGGRSAENPPSGSVRKTRKNKQKTPGNGDGGSTSEAPQPPRKKRARADPTVESEEAFKNRMEVKVKIPEELKPWLVEDWDLVTRQKQLFQLPAKKNVDAI
Protein: tRNA endonuclease VMS1 (EC 3.1.-.-) (VCP/CDC48-associated mitochondrial stress-responsive protein 1) (Q04311)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway. Component of an evolutionarily conserved system for ubiquitin-mediated mitochondria-associated protein degradation (MAD), which is necessary to maintain mitochondrial, cellular, and organismal viability.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21070972}. Mitochondrion {ECO:0000269|PubMed:21070972}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:21148305}; Peripheral membrane protein. Note=translocates from the cytosol to mitochondria upon mitochondrial stress. {ECO:0000269|PubMed:21070972}.
Interaction partners:
- Cell division control protein 48
- Nuclear protein localization protein 4
- Ribosome quality control complex subunit 2
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM22
- Mitochondrial import receptor subunit TOM40
- E4 ubiquitin-protein ligase UFD2
- UBX domain-containing protein 2
- Sorting assembly machinery 35 kDa subunit
- Ubiquitin fusion degradation protein 1
Sequence:
MNSQKASKMTGSLKKNDLYIFDLSEQLLNSLKLMSFDSTLREVEVEKTSDNDRNKESGDLQIARKKVTSNVMRCSVCQMSFDSRNEQKAHYQTDYHLMNVKRNLRGLDILSVEEFDALISKEHGIKSEDENSGGEQTSSDHEESEEASDRDPDLQTNNYMETIIENDLQKLGFQKDESDAISHINTQSPYIYFKSKYLQKNEVLAIYKSLFNKRSLSNPNEALTFWNSQENPMAISALFMVGGGHFAGAIVSHQRLNVKGNAHKKDETLIEQAVNFLEHKTFHRYTTRRKQGGSQSAMDNAKGKANSAGSALRRYNESALKTDIQGVLKDWEPYLSKCDNIFIRARNVSDKKIFTDNTVLNKGDERIKSFPFTTNRPTVLELKKAWCELSYLKILPKPEPLAVKETVQKLEVSNKKDEFKEKQEPLLEEIQTEEIISLLKKGRAPLLISFLKKNKLDGNFRLKPESKYSLTPTMLHYASQQGMKQMALILLSNIKCDPTIKNRLGRTAWDLNRNDDVRHAFQIARYNLGESFTNWDETHIGQPLSREQVDEINEKKKAIENEKAEKLIKLELEAAKEKQRFAKDAERGPGKKLTNIPSIQQQNLNSLTDEQRRRLMREQRARAAEERMKKKY
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (Q6DG22)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. May act as a positive regulator of T-cell coactivation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}.
Interaction partners:
- Adenosine kinase
- Adenosine kinase b.
- Adenosine deaminase 2-A
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Adenosine deaminase RNA-specific.
- Purine nucleoside phosphorylase
- adenosine deaminase
Sequence:
MNGKPAFDKPKVELHVHLDGAIRLKTVLDVAKRRGISLPVSMEEELKELCTVNEPATLTEFLGKFSHFMHVIAGDREAIKRIAYEFVETKAKEGVIYVEARYSPHFLANKGVEPLPWDQKPGDITPDDVVDLVNQGFKEGEQAFKTKARSILCCMRHMPNWSMEVVELCKKFHKDGVVAIDLAGDESMNCESYPGHKKAFEEAVRSNVHRTVHAGEVGPASVVREAVEVLKAERIGHGYHTLEDQNLYKQLLHQNMHFEMCPVSSRLTGACEPDFTKHPLITFKKDKANYSLNTDDPTIFNSTLNSDYEVVQKYMDFTEEEFKRLNINAAKSCFLPEKEKEKLLNQLYEAYGMRKSTSF
Protein: Rhotekin (Q9BST9)
Organism: Homo sapiens (Human)
Function: Mediates Rho signaling to activate NF-kappa-B and may confer increased resistance to apoptosis to cells in gastric tumorigenesis. May play a novel role in the organization of septin structures.
Interaction partners:
- Transforming protein RhoA
- Solute carrier organic anion transporter family member 6A1
- Protein lin-7 homolog B
- Rho-related GTP-binding protein RhoC
- Rho-related GTP-binding protein RhoB
- Cell division control protein 42 homolog
- Rhophilin-1
- Serine/threonine-protein kinase N1
- Uncharacterized protein C17orf47
- Tax1-binding protein 3
Sequence:
MFSRNHRSRVTVARGSALEMEFKRGRFRLSLFSDLPEDTELQRKLDHEIRMREGACKLLAACSQREQALEATKSLLVCNSRILSYMGELQRRKEAQVLGKTSRRPSDSGPPAERSPCRGRVCISDLRIPLMWKDTEYFKNKGDLHRWAVFLLLQLGEHIQDTEMILVDRTLTDISFQSNVLFAEAGPDFELRLELYGACVEEEGALTGGPKRLATKLSSSLGRSSGRRVRASLDSAGGSGSSPILLPTPVVGGPRYHLLAHTTLTLAAVQDGFRTHDLTLASHEENPAWLPLYGSVCCRLAAQPLCMTQPTASGTLRVQQAGEMQNWAQVHGVLKGTNLFCYRQPEDADTGEEPLLTIAVNKETRVRAGELDQALGRPFTLSISNQYGDDEVTHTLQTESREALQSWMEALWQLFFDMSQWKQCCDEIMKIETPAPRKPPQALAKQGSLYHEMAIEPLDDIAAVTDILTQREGARLETPPPWLAMFTDQPALPNPCSPASVAPAPDWTHPLPWGRPRTFSLDAVPPDHSPRARSVAPLPPQRSPRTRGLCSKGQPRTWLQSPV
Protein: HTH-type transcriptional regulator EthR (A0R666)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Involved in the repression of teh monooxygenase EthA which is responsible of the formation of the active metabolite of ethionamide (ETH).
Interaction partners:
- D-inositol 3-phosphate glycosyltransferase
- FAD-containing monooxygenase EthA
- DNA polymerase IV
- Probable transcriptional regulatory protein
- Enoyl-[acyl-carrier-protein] reductase
- Serine/threonine specific protein phosphatase
- HTH-type transcriptional repressor KstR2
- HTH-type transcriptional regulator LysG
- Transcriptional regulator, TetR family protein
Sequence:
MTTASQTRTPRGRRSARPSGDDREAAILATAQRLLETKKFAEISVDDLAKGAGISRPTFYFYFPSKEAVLLSLIDPLIKRADSGFDNAVESMPADPQRAIRRGIEIFFNSFGSHPATARAGTEALKSSPEFKEFWSGLMQKWIAATAALITAERERGAAPDTIPALDLATSLNLMNERTMMAALADEQPGVAPEKVVATLTHIWLNSIYGTLPVGTA
Protein: FI01009p (Vrille, isoform C) (Vrille, isoform E) (Q7KTN9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPEVLSGTPTNSHNKANIAMMNNVRLSNISPTLSMNGSSNEASNLHPLSMYGGSISPQSNDSGMSDSLGKYVPGSGYGDGMMAQSPSQGGNGPQSALTAAQKELFSQRKQREFTPDNKKDESYWDRRRRNNEAAKRSREKRRYNDMVLEQRVIELTKENHVLKAQLDAIRDKFNISGENLVSVEKILASLPTSEQVLSNTKRAKMSGSGGSSSGSSPSGSGSGEGSPQGGHNGYPVGPPLSPLIYGPNGNARPEATVKSVHHIHHAGVAPPPTHLQQLVVPQSQTQHLYQPQPQQHQPHQQQQISQPPQQQQQQQEPSPSAGSSSPVISDPHNRPPSTTIANLQVQLQQALNRNVRPEDLDSLRKVVAAGALYNAAAVVGAPPPPPSAGLYVPAPSAYKDHLEAAAAWSHNVEAAVSSSAVDAVSSSSVSGSAASVLNLSRRACSPSYEHMLSSTTSSTLSSASSSGAVSGDDEQEHEPAHMAPLQLQRSSPQQGSDANNCLPLKLRHKSHLGDKDAAATALLSLQHIKQEPNCSRASPPAWNDGGDNSSDERDSGISIASAEWTAQLQRKLLAPKEANVVTSAERDQMLKSQLERLESEVASIKMILAE
Protein: Multisite-specific tRNA:(cytosine-C(5))-methyltransferase trm4a (EC 2.1.1.-) (EC 2.1.1.203) (tRNA (cytosine-5-)-methyltransferase trm4a) (Q9HGQ2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: tRNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in tRNAs at position 34 and 48. Trm4a and trm4b methylate different sets of tRNAs. Also methylates cytosine to m5C at positions (60, 61 and 62) in tRNA(Asp).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- tRNA
- tRNA
- tRNA
- 25S rRNA
- tRNA
- 60S ribosome subunit biogenesis protein nip7
- Pumilio homology domain family member 6
- Probable rRNA-processing protein ebp2
- Uncharacterized RNA-binding protein C1827.05c
- Uncharacterized NOC2 family protein C1142.04
Sequence:
MGRKHYSSKKNRSKKGEFVNWDLIERKNENFEKYYRLQKLVTEDDFILLKQKLTEQLPTTFRITASIPHATQVRDYFIEHYYPLIENARTEDAKIPLPVSLPWYPDGMAFMLDISKEVIRKSPHLKALQEFLVLETEAGDINRQESVSMVPPLLLNVESHHKVLDMCAAPGSKTAQLLEALHKPTKKEDITTLLPSGIVIANDSDNKRAHMLVHQIKRLNSPNVLIVNHDASFLPNFHLSSPDGKKFLKFDRILADVPCSGDGTFRKNIALWNEWSLKTALGLHATQIKILMRGLQLLEKGGRLVYSTCSLNPIENEAVVSAVLNATRGSVRLVDVSSELPQLKRSQGVDNWVVCDSDLNIYPSFDTLPKELYEKMPPTLWPLPKKELAELNIQNCLRIYPHFQNTGGFFVAVLEKYENLTSSMKTAVDDNKVFLREQKLPSEQASKKRKQDTQETSSDSKLAEVKPKGKNGGNRFHELDPFVYIKEDDQALEKIYKKFGIDEAIIKKNQFFVRNVNGVPTKAIYISNDLFRNVIENNRNRVKFVHGGLKIFVRQDFGSLSREIAEKNGTCVFRVQSDGANLASHFIAESCLFHTTLSDLFILLDHEAVTIDDFPEDSLFRKEYNHLDLGSTLLHVDLAKEESVIKKQVYIPLWKSVRICNVLLSNSEKRTLKLQIEGPQSSIHKHNT