wanglab/gogpt-training-data huggingface dataset:
Protein: GPI-anchored protein LLG3 (LORELEI-like-GPI-anchored protein 3) (Q9M0I0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FKT1}; Lipid-anchor, GPI-anchor {ECO:0000255}.
Interaction partners:
- Receptor-like protein kinase ANXUR1
- Probable receptor-like protein kinase At2g21480
- Receptor-like protein kinase ANXUR2
- Pollen-specific leucine-rich repeat extensin-like protein 4
- Protein RALF-like 19
- Probable receptor-like protein kinase At2g39360
- Probable receptor-like protein kinase At5g61350
- Probable receptor-like protein kinase At5g59700
- Probable serine/threonine protein kinase IRE3
- Putative receptor-like protein kinase At5g39000
Sequence:
MKITHHCLVSLLSILLLSGFAFSHHISLDEFESHPSTSRALLQAKATCKEDFAAKNYTIITSKCKGPNYPAKVCCSAFKDFACPFAEVLNDEKTDCASTMFSYINLYGRYPPGIFANMCKEGKEGLDCTDVTPTSSSHASIPLVSTHVLLITVSILFHLF
Protein: Protein kinase C (EC 2.7.11.13) (Q6AZF7)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004318}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- sphingosine kinase
- sphingosine kinase
- DAGKc domain-containing protein.
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Uncharacterized protein
- Serine/threonine-protein kinase TOR
- Uncharacterized protein
- Phosphoinositide phospholipase C.
- Phosphoinositide phospholipase C
Sequence:
MADVFQHNDSTSSSSPLQDVVQRFARKGALRQKNVHEVKNHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFTCPGGDKGPDTDDPRSKHKFKIHNYGSPTFCDHCGSLLYGLIHQGMKCETCDMNVHKVCVINVPSLCGMDHTEKRGRIYLKAEVKGDGLNVIVCDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKKKTKTIRSTLNPNWNESFTFKLKPSDKDRRLSVEVWDWDRTTRNDFMGSLSFGVSELMKMPACGWYKLLNQEEGEYYNVPIPEADDGNLELRQKFEKAKLGPAGNKVINPTGERRPYIPSNNIDSIRLTDFCFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQEKPPFLTQLHSCFQTVDRLYFVMEYVSGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHRKGICYRDLKLDNVMLDFEGHIKIADFGMCKEHMVEGVTTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSMSKEAVSICKGLMTKHPVKRLGCGPEGERDIREHTFFRRIDWDKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQADFEGFSYINTQFFHPSLQCVA
Protein: Uncharacterized protein (Q38DR3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Mitochondrial ribosomal protein S18
- Small ribosomal subunit protein uS5 C-terminal domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- 30S Ribosomal protein S17, putative
- Trans-sialidase
- Ribosomal protein S23 mitochondrial conserved domain-containing protein
Sequence:
MLRRAYIQRRYPFNKRGPREHKSWKHHVLTEPPKPLQWRDPKVWTRDLSVMKSFDAPQWDLWQSRPRSEDMDEALQPFMDMPKSLKDRRYDIPWWANPFGAWYLQNILSLELLKLKSKTNAEKIATYRSYMRSLASGKDNTMSDDDVIRNIIKERWKTLEFGDRNAGYPCTFGDYIQFLNEWFKSLDEEGMQRLREHFDRRIRPLLAVMSPVDILWLEALTQNSPHNKEQLQRKIAFQTSLGTPEFFDMSKRLRYEINEDYKVRDELGPELFALWSKAPERWPPERLSKMYGLDFTLVRKILVWHHFKACYDACVEPDWSLPKRLFALEWIRDVRARKHGLFYGKMRFAEQKITFYSDRFLFRDLVNRREASYANVWEMDDPYRFLQTEQDYEDYWGDNYDVYRRMFPEMIGRTGEPVQQYGQMPIWAGPHRQHANKSEHNWMFAEIGVNVGHEALKKLELDPTNEKRRRFVIRQPDGTLRSAKMSEMRAWYWKEEWADFRFWAPQMEWGIENTPSQEQYQEHVPDTTDADFRKQRRIQSRPVKWFYESHYTRTGSFAGFQPLRFMQRRTEREVRWPDVINAAVQIQKRKPAAYIFKAIPEL
Protein: FGFR1 oncogene partner 2 (Q9NVK5)
Organism: Homo sapiens (Human)
Function: May be involved in wound healing pathway.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- MOB-like protein phocein
- TRAF3-interacting JNK-activating modulator
- Suppressor of IKBKE 1
- Striatin-interacting protein 1
- Striatin-3
- Serine/threonine-protein kinase 25
- Programmed cell death protein 10
- Serine/threonine-protein kinase 24
- Sarcolemmal membrane-associated protein
- Zinc finger MYM-type protein 2
Sequence:
MSCTIEKALADAKALVERLRDHDDAAESLIEQTTALNKRVEAMKQYQEEIQELNEVARHRPRSTLVMGIQQENRQIRELQQENKELRTSLEEHQSALELIMSKYREQMFRLLMASKKDDPGIIMKLKEQHSKIDMVHRNKSEGFFLDASRHILEAPQHGLERRHLEANQNELQAHVDQITEMAAVMRKAIEIDEQQGCKEQERIFQLEQENKGLREILQITRESFLNLRKDDASESTSLSALVTNSDLSLRKS
Protein: Prune homolog 2 with BCH domain (X6R9J3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEFLQRAKSKLNRSKRLEKVHVVIGPKSCDLDSLISTFTYAYFLDKVSPPGVLCLPVLNIPRTEFNYFTETRFILEELNISESFHIFRDEINLHQLNDEGKLSITLVGSSVLASEDKTLESAVVKVINPVEQSDANVEFRESSSSLVLKEILQEAPELITEQLAHRLRGSILFKWMTMESEKISEKQEEILSILEEKFPNLPPREDIINVLQETQFSAQGLSIEQTMLKDLKELSDGEIKVAISTVSMNLEMSRIELFPKGTWLVNRDAFQSRNSGSKCMPGTTVLQCTLRSLQRGK
Protein: mRNA export factor ICP27 homolog (Mta) (ORF57 protein homolog) (Protein EB2) (Protein SM) (Q3KSU1)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Function: Promotes the nuclear export of a subset of early and late viral mRNAs by interacting with mRNAs and cellular export proteins. Additionally may prevent the establishment of cellular antiviral state, by acting as an alternative splicing factor for cellular RNAs such as STAT1, resulting in a STAT1 mRNA incapable of producing the STAT1alpha isoform.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:Q04360}. Host cytoplasm {ECO:0000250|UniProtKB:Q04360}. Note=shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q04360}.
Interaction partners:
Sequence:
MVPSQRLSRTSSISSNEDPAESHILELEAVSDTNTDCDMDPMEGSEEHSTDGEISSSEEEDEDPTPAHAVPAQPSSVVITPTSASFVIPRKKWDLQDKTVTLHRSPLCRDEDEKEETGNSSYTRGHKRRRGEVHGCTDESYGKRRHLPPGARAPRAPRAPRVPRAPRSPRAPRSNRATRGPRSESRGAGRSTRKQARQERSQRPLPNKPWFDMSLVKPVSKITFVTLPSPLASLTLEPIQDPFLQSMLAVAAHPEIGAWQKVQPRHELRRSYKTLREFFTKSTNKDTWLDARMQAIQNAGLCTLVAMLEETIFWLQEITYHGDLPLAPAEDILLACAMSLSKVILTKLKELAPCFLPNTRDYNFVKQLFYITCATARQNKVVETLSSSYVKQPLCLLAAYAAVAPAYINANCRRRHDEVEFLGHYIKNYNPGTLSSLLTEAVETHTRDCRSASCSRLVRAILSPATGSLGLFFVPGLNQ
Protein: Mitochondrial intermediate peptidase, putative (EC 3.4.24.59) (Q389Z4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ferroxidase
- ribonuclease Z
- Xaa-Pro dipeptidase
- Mitochondrial processing peptidase alpha subunit, putative
- Succinate--CoA ligase subunit beta, mitochondrial
- Elongation factor Ts, mitochondrial
Sequence:
MLRRVTPFTLCASGFTACRWAGRVRHGATICSAVSDATAGKQKSACVTDVEEIPTLSFLSSKSILSETVDRTIEVCDALLNEIPKAKSIKEKHDLIDSTSNVLCLLLDPCEFVRQVHPDAEYKQHASYAFQKGYEYMSKVNSRRDLYDVVLQLDSTEGHKELSSEEIKNVAQLRRDMESNGIHLPDKLREKVTEMNIEKEELAMRFLTEQGSKNPFATLRYLLQCRYELSQLLGFESFAEQQLRGTMLENQQRVWHFLCGIAHKYRREAEKEMDIIRSNVGEVRNRQNITDDVRARVAHSLRRDAEPETAAEYFSVANCIRGIQCLCLEVFGVRLEEVQFDKDEIFNNDAKKYHVYDENKAFLGVIVLDLYASEMKYCQAGHLTLQLGCIPHQEALAKVGLKLPKRQYPVVVLTCNVGACSPVQRLPNGRFDDESTLMHPNEVTTVFHEFGHAMHTIFGQTKVQNLAGTRASIDFVETFSQLFEQFLTSHEFLQLWAHRISTREPISFDMVMKRNAAADMFKHLDMMDQVVLSAVDQTLHGPQPYTVYFPRGDQGNLGKRTLGDIGDYGRGTYNLAKVLIDICTPLSIVTPTETGVLGTLSFEHLSGYPAGYYGYLYSLSIARRIWAKKFMKDPLNRDAGRELVQKVMRHGAACNPVDVIENYLEDKLDEIDIWV
Protein: GATA-type domain-containing protein (Q3S1J8)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHYRDANYSISRNKVNLHHEEFMLDGVVGGEDHDMQNTNEVRAELDSLLRLDPDTNSIIDALHISQPIEQENMDYEGKPVEFTLGTSSGGASLAPTSSTTAASIAPFSYNTSATNYYNTTPSSYPMFLNYQYAGGTTVTTDMDAFSGMDMSMNNGVFGTQNNPSYFYPTTQLNTYGYDTLAAATTASGITVNNNQLNVNIVQGNGTIVPQPITQNIISTVSNVQSSVPINNSQPLTPTGLAGCSTSSGSSSASSSSANSTSTPKNTISKANRSSGGANNSQFSTEDRECVNCGVHNTPLWRRDGSGNYLCNACGLYFKMNHHARPLVKPKKRQQNAQKRTGIECVNCRTNTTTLWRRNGEGHPVCNACGLYFKLHKVERPITMKKDGIQTRNRKLSAKGSRRMKKENGGTPTSMGMPTTSSSISSGIELDQSGVWGMKNTQPMLMTPTAYAFPASNFYFNSIEDQLEYKTCPPMMVDFGGQMKNLNLN
Protein: Claspin (E7ESG2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTGEVGSEVHLEINDPNVISQEEADSPSDSGQGSYETIGPLSEGDSDEEIFVSKKLKNRKVLQDSDSETEDTNASPEKTTYDSAEEENKENLYAGKNTKIKRIYKTVADSDESYMEKSLYQENLEAQVKPCLELSLQSGNSTDFTTDRKSSKKHIHDKEGTAGKAKVKSKRRLEKEERKMEKIRQLKKKETKNQEDDVEQPFNDSGCLLVDKDLFETGLEDENNSPLEDEESLESIRAAVKNKVKKHKKKEPSLESGVHSFEEGSELSKGTTRKERKAARLSKEALKQLHSETQRLIRESALNLPYHMPENKTIHDFFKRKPRPTCHGNAMALLKSSKYQSSHHKEIIDTANTTEMNSDHHSKGSEQTTGAENEVETNALPVVSKETQIITGSDESCRKDLVKNEELEIQEKQKQSDIRPSPGDSSVLQQESNFLGNNHSEECQVGGLVAFEPHALEGEGPQNPEETDEKVEEPEQQNKSSAVGPPEKVRRFTLDRLKQLGVDVSIKPRLGADEDSFVILEPETNRELEALKQRFWKHANPAAKPRAGQTVNVNVIVKDMGTDGKEELKADVVPVTLAPKKLDGASHTKPGEKLQVLKAKLQEAMKLRRFEERQKRQALFKLDNEDGFEEEEEEEEEMTDESEEDGEEKVEKEEKEEELEEEEEKEEEEEEEGNQEDSSSKMGYFPTEEKSETDENSGKQPSKLDEDDSCSLLTKESSHNSSFELIGSTIPSYQPCNRQTGRGTSFFPTAGGFRSPSPGLFRASLVSSASKSSGKLSEPSLPIEDSQDLYNASPEPKTLFLGAGDFQFCLEDDTQSQLLDADGFLNVRNHRNQYQALKPRLPLASMDENAMDANMDELLDLCTGKFTSQAEKHLPRKSDKKENMEELLNLCSGKFTSQDASTPASSELNKQEKESSMGDPMEEALALCSGSFPTDKEEEDEEEEFGDFRLVSNDNEFDSDEDEHSDSGNDLALEDHEDDDEEELLKRSEKLKRQMRLRKYLEDEAEVSGSDVGSEDEYDGEEIDEYEEDVIDEVLPSDEELQSQIKKIHMKTMLDDDKRQLRLYQERYLADGDLHSDGPGRMRKFRWKNIDDASQMDLFHRDSDDDQTEEQLDESEARWRKERIEREQWLRDMAQQGKITAEEEEEIGEDSQFMILAKKVTAKALQKNASRPMVIQESKSLLRNPFEAIRPGSAQQVKTGSLLNQPKAVLQKLAALSDHNPSAPRNSRNFVFHTLSPVKAEAAKESSKSQVKKRGPSFMTSPSPKHLKTDDSTSGLTRSIFKYLES
Protein: Oxidation protein CepE (OxyA protein) (p450 monooxygenase) (Q6ZZI8)
Organism: Actinoplanes teichomyceticus
Interaction partners:
Sequence:
MFEEINVVRAAELHRRDRFDPVPQLRSLMAEGPLTTLGTEESPGGRTAWLATGYDEIRQVLSSDDFSARLLYGGTAAGITWPGFLTQYDPPEHTRLRRMVAPAFAVRRMQKFQPQVERVVQDSLDAIEALGGPVDFVPRFGWSVATTATCDFLGIPRDDQADLARSLHASRTERSGKRRTAAGNKFMTYMNKMTARTRRDPGDDMFGVVVREYGDEITDAELTGVAAFVMGAGADQVARFLAAGAWLMADDPEQFALLREKPDTVPDWLDEVIRYLTTDEKTHPRVATDDVRIGDHLIKAGDTVTCSLLAANRRNFPRPEDRFDITRVRPEHLAFGHGIHHCLGRSLAELVFRTAIPALAHRFPTLRLAEPHREIRLGPPPFDVEALLLDW
Protein: ATP synthase small subunit 6-A, mitochondrial (AtMtATP6) (MtATP6) (ATP synthase 6 kDa subunit, mitochondrial) (P0DO44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (Probable). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). Part of the complex F(0) domain (Probable). Confers tolerance to several abiotic stresses (e.g. salt, mannitol, drought, oxidative and cold stresses), probably by providing additional energy needed for cell homeostasis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:15276431}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MRLFDPWPVFFKREWKRCWPFLTGFAVTGVLITKLTAGLTEEDAKNSKFVQQHRR
Protein: Receptor activity-modifying protein 2 (Q9JHJ1)
Organism: Rattus norvegicus (Rat)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60895}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60895}.
Interaction partners:
- Pro-adrenomedullin
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin receptor
- Islet amyloid polypeptide
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 1
- Calcitonin gene-related peptide 2
- Protein ADM2
- Calcitonin
- Neuroendocrine secretory protein 55
Sequence:
MAPLRVERAPGGSQLAVTSAQRPAALRLPPLLLLLLLLLLGAVSTSPESLNQSHPTEDSLLSKGKMEDYETNVLPCWYYYKTSMDSVKDWCNWTLISRYYSNLRYCLEYEADKFGLGFPNPLAESIILEAHLIHFANCSLVQPTFSDPPEDVLLAMIIAPICLIPFLVTLVVWRSKDGDAQA
Protein: RNA polymerase sigma factor (Q5DYR1)
Organism: Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri)
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
- EAL domain protein
- Stationary phase protein, anti sigma-70 factor Rsd
- Transcriptional regulator, AraC family
- Protein RecA
Sequence:
MAYAKLDMRVCEEQGLNDSYSLYLKEINRYQLLTAEEELAYSRLYKKGDVSARNTLIESNLRLVVKVANKYRKRNQTDLAILDIIEEGNLGLIKAIDKFNPELGYRFSTYAVWWIRESIESALFNHSRTVRLPVHITKELNTYLRAARELSKSLKREPSIRDISTYCEEEQIKVSKIISLIPNQLTCHSACSDELSPKFFELSSNNKALEPDSSLSQNNLEMNLSSWIDSLNYREKEIIINRYGLFGCKVKTLEDLGKDLDLSKERVRQIQSETLIKLNTIFKKNKLDLEIALG
Protein: Kelch-like protein 17 (Actinfilin) (Q8K430)
Organism: Rattus norvegicus (Rat)
Function: Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. The BCR(KLHL17) complex mediates the ubiquitination and subsequent degradation of GLUR6. May play a role in the actin-based neuronal function.
Subcellular location: Postsynaptic density {ECO:0000269|PubMed:12063253}. Synapse {ECO:0000269|PubMed:12063253}.
Interaction partners:
- Cullin-3
- Nuclear factor erythroid 2-related factor 2
- Glutamate receptor ionotropic, kainate 1
- Sequestosome-1
- Nucleoside diphosphate-linked moiety X motif 17
Sequence:
MQPRGERPAGRTQSPEHSSPGPGPEAPPPPQPPAPEAERARPRQARPAAPMEGAMQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADTHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEDVYRAVLSWVKHDVDTRRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLLPEQRGVLGTSRTRPRRCEGAGPVLFAVGGGSLFAIHGDCEAYDTRTDRWHVVASMSTRRARVGVAAVGNRLYAVGGYDGTSDLATVESYDPVTNTWQPEVSMGTRRSCLGVAALHGLLYAAGGYDGASCLNSAERYDPLTGTWTSIAAMSTRRRYVRVATLDGNLYAVGGYDSSSHLATVEKYEPQVNSWTPVASMLSRRSSAGVAVLEGALYVAGGNDGTSCLNSVERYSTKAGAWESVAPMNIRRSTHDLVAMDGWLYAVGGNDGSSSLNSIEKYNPRTNKWVAASCMFTRRSSVGVAVLELLNFPPPSSPTLSVSSTSL
Protein: Tight junction protein 2 (A0A8J8Y4W9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}.
Interaction partners:
Sequence:
MEEVIWEQYTVTLQKDSKRGFGIAVSGGRDNPHFENGETSIVISDVLPGGPADGLLQENDRVVMVNGTPMEDVLHSFAVQQLRKSGKIAAIVVKRPRKVQVAPLQGSPPLSHDDRGFEMMDEFDGRSFRSGYSERSRHSSHDMLSHSWEDSRERGRPHQRAQSRERERSRGRSLERGLDHEDYGRSHERSRGRSLERGLDRDFVSRDYSRGRSIDRDYDRDYERSYHQAYEPDYEGRYSPSYDRRAHPETRYERSRSREHLRSRSPTPESRSRQEHKGQHDPDRPIGVLLTKSKANEEYGLRLGSQIFIKEMTRTGLATKDGNLHEGDIILKINGTVTENMSLTDARKLIEKSRGKLQLVVLRDSKQTLINIPSLNDSDSEVEDISEIESNRSFSPEERRQQYSDQEYHSSTEKLKERPSSREETSGRMSRMGATPTPFKSTGDITAAGVTEANKEPRSQEESPVPQPRTASRVFLRPSPEDEAIYGPNTKMVKFKKGDSVGLRLAGGNDVGIFVAGIQEGTSAEQEGLQEGDQILKVNTQDFRGLVREDAVLYLLEIPKGETVTILAQSRADVYRDILACGRGDSFFIRSHFECEKETPQSLAFTRGEVFRVVDTLYDGKLGHWLAVRIGNELEKGLIPNKSRAEQMASVQNAQRENAGDRADFWRMRGQRSGVKKNIRKSREDLAAAVSVSTKFPAYEKVLLREAGFKRPVVLFGPIADIAMERLTTELPDLFQTAKTEPKDAGSEKSSGVVRLNTVRQIIEQDKHALLDVTPKAVDLLNYTQWFPIVIFFNPDSRQGIKTIRQRLNPTSNKSSRKLFDQANKLKKTCSHLFTATINVNSANDGWFGSLKDSIQQQQNEAVWVSEGKMEGMDDDAEDRMSYLTAMGADYLSCDSRLISDFEDTDGEGGAYTDNELDEPAEEPLVSSITRSSEPVQHEESIRKPSPEPRAQMRRAASRDQLRDGSPPPAFKPEPPKVRNQNREDSFNYSKSNLSAMAGSEIPGGSTKGCPPPIAVKPAFGRSILKPSTPVPMPESEEVGESTEEQEEAPKSVLGRVKIFEKMDHKAKLQRMQELQEAQNARIEIAQKHPDIYAVPIKAPKPDAGLPQHMSSRPPEPQKAPSRLYQDTRGSYGSDPEEEEEYRQQLAAHSKRGYYSQPSRYRDTEL
Protein: Histone H2A type 2-C (H2A-clustered histone 20) (Histone H2A-GL101) (Histone H2A/q) (Q16777)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4
- Histone H3.3
- Histone H3.1t
- Histone H3.1
- Histone H3.2
- Histone H4-like protein type G
- Histone H2B type 2-E
- Histone H3-7
- Histone H3.3C
- Histone H1.1
Sequence:
MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHKAKSK
Protein: Proteasome 26S subunit, non-ATPase 7 (H3BNT7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPELAVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLR
Protein: Putative calpain-like cysteine peptidase (Small myristoylated protein 2) (Q5SDH4)
Organism: Leishmania major
Interaction partners:
Sequence:
MGGSNSTNRKIIYKNGRPTFKGDEVVKGFERDNGLLFRIVKRKKGHQTWAFYNDTTQYNMRINVTFAAGCELTALGHTKVVKGERGEWVATVVVMPGKTEMFVEGKIEGFKSNMDAYPVMSDGNGNRLAAGGAVAN
Protein: Ranatuerin-1T (Brevinin-2T) (P82740)
Organism: Rana temporaria (European common frog)
Function: Antibacterial activity against Gram-positive bacterium S.aureus and Gram-negative bacterium E.coli. No activity against C.albicans.
Subcellular location: Secreted {ECO:0000269|PubMed:10333736, ECO:0000269|PubMed:10422869, ECO:0000269|PubMed:34235566}.
Interaction partners:
Sequence:
GLLSGLKKVGKHVAKNVAVSLMDSLKCKISGDC
Protein: Signal peptide, CUB and EGF-like domain-containing protein 1 isoform 2 precursor (Signal peptide, CUB domain, EGF-like 1) (A0A0R4IBT9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MGPACFSWEVCLLFLLINTLDVMGNVGVPDADECSEATDDCHIDALCQNTPKSFKCICKTGYKGDGKHCEDIDECENDYNGGCVHDCINIPGNYRCTCYDGFMLADDGHNCLDVDECLDNNGGCQQICVNTMGSYECQCKDGFFLSDNQHTCIHRSDDGMNCMNKDHGCAHICREITKGGVACECRPGFELAENQRDCKLTCNYGNGGCQHTCDDTDVGPICGCHQKYALHSDSKTCIETCAVNNGGCDRTCKDTATGVRCSCPVGFTLQPDGKTCKDIDECLENNGGCDHFCRNTVGSFECSCQKGHKLLTNERTCQDIDECSFERTCDHVCINYPGSFECVCHKGYSLYGFTHCGDIDECSINNGSCEHGCVNTPGSYECVCPPGQKLHWNKKDCVEAVKCLQNGKPPPRAQLSCTKTGGGEVCSLSCPSNALFLADSENSYTLSCGVPVQPGKAPLKRNITTSSSSSLQTCTEMLAQPVKQKARFKIKDAKCHMRPRNKEKHRDMGKQGLQAGQFPCTDDCQVTFVNLKCDSSKKRRRGRKSPSKEVSHITAEFEMEMKEEEASESCNLDCVREKTKQRLQNAMRTLRKSISKQQFYIQFSGTAYEVAQHALRHTTEGDETCSIGQVFTDGKCVSCVVGTFYSGEQEQCVMCPLGTYQDREGQLSCEPCPRTEGQGIAGAKNVSECGGQCPAGQFSSDGFRPCQPCQLGTFQPEPGRVLCFPCGGGLMTKHTGSTSFRDCEAKVHCALGHYYNATTHRCIRCPAGTYQSESGQNYCITCPGNTTTDFDGANNVSHCKNQICGGELGDFMGYIESPNYPGDYPSNVDCVWTINPPNKRRILIVVPEIFLPIEDECGDVLVMRKSALPTSITTYETCQTYERPIAFTSRSRKLWIQFKSNEGNSGKGFQVPYVTYDEDYQQLIEDIVRDGRLYASENHQEILKDKKLIKALFDVLAHPQNYFKYTVQESKEMFPRSFIKLLRSKVSRFLRPYK
Protein: Serine protease HTRA3 (EC 3.4.21.-) (High-temperature requirement factor A3) (Pregnancy-related serine protease) (Toll-associated serine protease) (Q9D236)
Organism: Mus musculus (Mouse)
Function: Serine protease that cleaves beta-casein/CSN2 as well as several extracellular matrix (ECM) proteoglycans such as decorin/DCN, biglycan/BGN and fibronectin/FN1. Inhibits signaling mediated by TGF-beta family proteins possibly indirectly by degradation of these ECM proteoglycans. May act as a tumor suppressor. Negatively regulates, in vitro, trophoblast invasion during placental development and may be involved in the development of the placenta in vivo. May also have a role in ovarian development, granulosa cell differentiation and luteinization (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P83110}. Note=Secretion increased during decidualization of endometrial stromal cells. {ECO:0000250|UniProtKB:P83110}.
Interaction partners:
Sequence:
MQARALLPATLAILATLAVLALAREPPAAPCPARCDVSRCPSPRCPGGYVPDLCNCCLVCAASEGEPCGRPLDSPCGDSLECVRGVCRCRWTHTVCGTDGHTYADVCALQAASRRALQVSGTPVRQLQKGACPSGLHQLTSPRYKFNFIADVVEKIAPAVVHIELFLRHPLFGRNVPLSSGSGFIMSEAGLIVTNAHVVSSSSTASGRQQLKVQLQNGDAYEATIQDIDKKSDIATIVIHPKKKLPVLLLGHSADLRPGEFVVAIGSPFALQNTVTTGIVSTAQRDGKELGLRDSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVAAGISFAIPSDRITRFLSEFQNKHVKDWKKRFIGIRMRTITPSLVEELKAANPDFPAVSSGIYVQEVVPNSPSQRGGIQDGDIIVKVNGRPLADSSELQEAVLNESSLLLEVRRGNDDLLFSIIPEVVM
Protein: Sensory rhodopsin II transducer (HTR-II) (Methyl-accepting phototaxis protein II) (MPP-II) (P42259)
Organism: Natronomonas pharaonis (Natronobacterium pharaonis)
Function: Transduces signals from the phototaxis receptor sensory rhodopsin II (SR-II) to the flagellar motor. Responds to light changes through the variation of the level of methylation. Also acts as a chemotransducer.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MSLNVSRLLLPSRVRHSYTGKMGAVFIFVGALTVLFGAIAYGEVTAAAATGDAAAVQEAAVSAILGLIILLGINLGLVAATLGGDTAASLSTLAAKASRMGDGDLDVELETRREDEIGDLYAAFDEMRQSVRTSLEDAKNAREDAEQAQKRAEEINTELQAEAERFGEVMDRCADGDFTQRLDAETDNEAMQSIEGSFNEMMDGIEALVGRIERFADAVSEDAEAVRANAESVMEASEDVNRAVQNISDAAGDQTETVQQIALEMDDVSATTEEVAASADDIAKTARQAAETGEAGRETAETAITEMNEVESRTEQAVASMEELNEDVREIGEVSEMIADIAEQTNILALNASIEAARADGNSEGFAVVADEVKALAEETKAATEEIDDLIGTVQDRTQTTVDDIRETSDQVSEGVETVEDTVDALERIVDSVERTNDGIQEINQSTDAQADAAQKATTMVEDMAATSEQTASDAETAAETTETQAESVKEVFDLIDGLSEQADSLSETLSRTDTEEASAADLDDQPTLAAGDD
Protein: DNA-dependent ATPase (A0A1D8PI62)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Recombinase
- DNA repair protein RAD51 homolog
- DNA repair and recombination protein RAD52
- DNA 3'-5' helicase
- DNA repair and recombination protein RAD52
- DNA-dependent ATPase
- DNA 3'-5' helicase
- Rad2 family nuclease
- Helicase ATP-binding domain-containing protein
- DNA repair protein RAD4
Sequence:
MDDYKQLGPGIFSCSRKFPFLTTRLQQYGKSINDLLQYDEASDHAQLARLVDRPMKEINDYYRNLKKDLQVDPTSVNSLLDSEFISTGLPSIDRELGGGIPIGEVTEIFGASGCGKSHFLFQLLSNCGKEFPTSKNIYISTESFLETKRLKDFIGRNSSNIDTDLDRISYIYCQDLESQDHILFTQLPLKLDSDKGKTKLLVLDSIAQHFRREDSIMNSTYLKEKLEVQEGEIADDRSFQEVKRKQMNQLRRFNKSQKYASRTAKLYYICQLYQHLSRLAQDFNIAIVIVNQVSDYSFESSGSFTEAEAGELDYPLNLDFQTAVSSGWDSRTIYNSIPTANITLKNEEIENLEMELAKSLEERSPNKRQKLSNTSSPQKQEHNLNPRERLERQKSLISKSHEMRNRGSKKIVPTLGYPWATRIKNRIMLSKVYKPILKSNMDGDIVNDDQSLQTNSIHDKRSSAELYKSFVSIDGWQVERFAKVVTSTHGYNPNRFKRYRFIINSQGLAEV
Protein: Protein RESISTANCE TO POWDERY MILDEW 8.2 (AtRPW8.2) (Q9C5Z6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance (R) protein that induces localized, salicylic acid-dependent defenses. Confers resistance to powdery mildew (e.g. Erysiphe cichoracearum UCSC1).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIAEVAAGGALGLALSVLHEAVKRAKDRSVTTRFILHRLEATIDSITPLVVQIDKFSEEMEDSTSRKVNKRLKLLLENAVSLVEENAELRRRNVRKKFRYMRDIKEFEAKLRWVVDVDVQVNQLADIKELKAKMSEISTKLDKIMPQPKFEIHIGWCSGKTNRAIRFTFCSDDS