wanglab/gogpt-training-data huggingface dataset:
Protein: Disease resistance protein RPP13 (Resistance to Peronospora parasitica protein 13) (Q9M667)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. In contrast to other resistance proteins, it works independently of ESD1 and NSD1 proteins and does not require the accumulation of salicylic acid, suggesting the existence of an independent signaling pathway. The specificity to avirulence proteins differs in the different cultivars.
Interaction partners:
- Disease resistance protein RPP5
- Disease resistance protein RPP4
- Toll/interleukin-1 receptor-like protein
- Disease resistance protein RLM3
- Protein EDS1
- UNC93-like protein 2
- LRR protein
- Disease resistance protein RML1A
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- DELLA protein GAI
Sequence:
MVDAITEFVVGKIGNYLIEEASMFMAVKEDLEELKTELTCIHGYLKDVEAREREDEVSKEWSKLVLDFAYDVEDVLDTYHLKLEERSQRRGLRRLTNKIGRKMDAYSIVDDIRILKRRILDITRKRETYGIGGLKEPQGGGNTSSLRVRQLRRARSVDQEEVVVGLEDDAKILLEKLLDYEEKNRFIISIFGMGGLGKTALARKLYNSRDVKERFEYRAWTYVSQEYKTGDILMRIIRSLGMTSGEELEKIRKFAEEELEVYLYGLLEGKKYLVVVDDIWEREAWDSLKRALPCNHEGSRVIITTRIKAVAEGVDGRFYAHKLRFLTFEESWELFEQRAFRNIQRKDEDLLKTGKEMVQKCRGLPLCIVVLAGLLSRKTPSEWNDVCNSLWRRLKDDSIHVAPIVFDLSFKELRHESKLCFLYLSIFPEDYEIDLEKLIHLLVAEGFIQGDEEMMMEDVARYYIEELIDRSLLEAVRRERGKVMSCRIHDLLRDVAIKKSKELNFVNVYNDHVAQHSSTTCRREVVHHQFKRYSSEKRKNKRMRSFLYFGEFDHLVGLDFETLKLLRVLDFGSLWLPFKINGDLIHLRYLGIDGNSINDFDIAAIISKLRFLQTLFVSDNYFIEETIDLRKLTSLRHVIGNFFGGLLIGDVANLQTLTSISFDSWNKLKPELLINLRDLGISEMSRSKERRVHVSWASLTKLESLRVLKLATPTEVHLSLESEEAVRSMDVISRSLESVTLVGITFEEDPMPFLQKMPRLEDLILLSCNYSGKMSVSEQGFGRLRKLDLLMRSLDELQIEEEAMPNLIELEISVSKRETKLIIPNRLRAFGQIYC
Protein: Variable charge X-linked protein 1 (Variable charge protein on X with ten repeats) (VCX-10r) (Variably charged protein X-B1) (VCX-B1) (Q9H320)
Organism: Homo sapiens (Human)
Function: May mediate a process in spermatogenesis or may play a role in sex ratio distortion.
Interaction partners:
- Variable charge X-linked protein 3B
- Steryl-sulfatase
Sequence:
MSPKPRASGPPAKATEAGKRKSSSQPSPSDPKKKTTKVAKKGKAVRRGRRGKKGAATKMAAVTAPEAESAPAAPGPSDQPSQELPQHELPPEEPVSEGTQHDPLSQEAELEEPLSQESEVEEPLSQESQVEEPLSQESEVEEPLSQESQVEEPLSQESEVEEPLSQESQVEEPLSQESEMEEPLSQESQVEEPPSQESEMEELPSV
Protein: Actin-like protein 6B (BRG1-associated factor 53B) (BAF53B) (P86173)
Organism: Rattus norvegicus (Rat)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth. Essential for neuronal maturation and dendrite development (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12368262}.
Interaction partners:
- Zinc finger protein neuro-d4
- Double PHD fingers 3
- PHD finger protein 10
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
- Protein polybromo-1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
Sequence:
MSGGVYGGDEVGALVFDIGSFSVRAGYAGEDCPKADFPTTVGLLAAEEGGGLELEGEKEKKGKIFHIDTNALHVPRDGAEVMSPLKNGMIEDWECFRAILDHTYSKHVKSEPNLHPVLMSEAPWNTRAKREKLTELMFEQYNIPAFFLCKTAVLTAFANGRSTGLVLDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFISMQCRELFQEMAIDIIPPYMIAAKEPVREGAPPNWKKKEKLPQVSKSWHNYMCNEVIQDFQASVLQVSDSPYDEQVAAQMPTVHYEMPNGYNTDYGAERLRIPEGLFDPSNVKGLSGNTMLGVGHVVTTSIGMCDIDIRPGLYGSVIVTGGNTLLQGFTDRLNRELSQKTPPSMRLKLIASNSTMERKFSPWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
Protein: Factor of DNA methylation 4 (Q9LMH6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts in association with FDM3 and FDM5 for RNA-directed DNA methylation (RdDM).
Interaction partners:
- Zinc finger CCCH domain-containing protein 42
- Zinc finger CCCH domain-containing protein 5
- Protein SUPPRESSOR OF GENE SILENCING 3
- Protein IDA-LIKE 2
Sequence:
MYSRRELEDLEYRYYSEMKDGTRKVKISESLFRCPFCYIDRKRDYQFDDLLRHASGIGGSSRTKDGRDKARHLALERYMRKYLRPRERPRPSPTSDVSSLPKEEFTGKWKSTLSTTEEGEFITTENSSSPHIVKAEPKFVSGDDSGRSGEERLKFSDKPDPFFSNEDKSYPAKRPCLVSGAKEGDEPVQRIGLSHGASFAPTYPQKLVSLGAGNGDQMYVHPWKGILANMKRTFNEKTRKYAGESGSKIREDLIKKGFNPHKVTPLWNGRLGFTGFAIVDFGKEWEGFRNATMFDKHFEVSQCGKRDHDLTRDPGDKLYGWVAKQDDYYSRTAIGDHLRKQGDLKSVSGKEAEDQRKTFTLVSNLENTLVTKSDNLQQMESIYKQTSSVLEKRMKEKDEMINTHNEKMSIMQQTARDYLASIYEEHEKASQHLEAQRKEYEDRENYLDKCQAKNKTERRKLQWQKHKNLMATQEQNKADEDMMRLAEQQQREKDELRKQVRELEEKIDAEQALELEIERMRGDLQVMGHMQEGEGEDSKIKEMIEKTKEELKEKEEDWEYQESLYQTLVVKHGYTNDELQDARKALIRSMRELTTRAYIGVKRMGALDETPFKKVAKEKYPAVEADKKAEELCSLWEEHLGDSAWHPIKVVEKDGIAKEELNEEDEKLQELRKELGEEVYAAVTQALKERNEYNGSGRYIVPELWNFKQNRKASIKEGVVYLVNSWKQKKPKPKRR
Protein: 1,3-beta-glucanosyltransferase GAS4 (EC 2.4.1.-) (Glycolipid-anchored surface protein 4) (Q08271)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in spore wall assembly.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10383953}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953}.
Interaction partners:
- Deoxyribodipyrimidine photo-lyase, mitochondrial
Sequence:
MMVFSSTFIFLILELVVLCEASVHTIQIKDKHFVDTVTGKPFFIKGVDYQPGGSSDVSEKQDPLSNPDACARDILLFQELGINTVRIYSINPDLNHDACMTMLAMAGIYLILDVNSPLQNQHLNRYEPWTTYNEVYLEHVFKVVEQFSHYNNTLGFFAGNEIVNDKRSAQYSPAYVKELIGTMKNYISAHSPRTIPVGYSAADDLNYRVSLSEYLECKDDDKPENSVDFYGVNSYQWCGQQTMQTSGYDTLVDAYRSYSKPVFFSEFGCNKVLPRQFQEIGYLFSEEMYSVFCGGLVYEFSQEDNNYGLVEYQEDDSVQLLADFEKLKSHYQNIEFPSMKTLKETVQMEETPSCAEDYENLKIESKIAKNLGSSLIKKGVKVEKGKYIDIHEDQLSTNVTILDKHGDRWNGPKKIEIRQSLTLADLEGEEQEDADEDKDDLKRKHRNSASISGPLLPLGLCLLFFTFSLFF
Protein: General transcription factor IIH subunit 3 (General transcription factor IIH polypeptide 3) (A0A087WYD5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368090}.
Interaction partners:
Sequence:
MNKEVKDNQEMKSRILVIKAAEDSALQYMNFMNVIFAAQKQNILIDACVLDSDSGLLQQACDITGGLYLKVPQMPSLLQYLLWVFLPDQDQRSQLILPPPVHVDYRAACFCHRNLIEIGYVCSVCLSIFCNFSPICTTCETAFKISLPPVLKAKKKKLKVSA
Protein: Nuclear receptor coactivator 6 (Nuclear receptor coactivator-6 beta) (F6M2K2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVLDDLPNLEDIYTSLCSSTMEDSEMDFDSGLEDDDTKSDSILEDSTIFVAFKGNIDDKDFKWKLDAILKNVPNLLHMESSKLKVQKVEPWNSVRVTFNIPREAAERLRILAQSNNQQLRDLGILSVQIEGEGAINLALAQNRSQDVRMNGPMGAGNSVRMEAGFPMASGPGIIRMNNPATVMIPPGGNVSSSMMAPGPNPELQPRTPRPASQSDAMDPLLSGLHIQQQSHPSGSLAPPHHPMQPVSVNRQMNPANFPQLQQQQQQQQQQQQQQQQQQQQQQQQQLQARPPQQHQQQQPQGIRPQFTAPTQVPVPPGWNQLPSGALQPPPAQGSLGTMTANQGWKKAPLPGPMQQQLQARPSLATVQTPSHPPPPYPFGSQQASQAHTNFPQMSNPGQFTAPQMKSLQGGPSRVPTPLQQPHLTNKSPASSPSSFQQGSPASSPTVNQTQQQMGPRPPQNNPLPQGFQQPVSSPGRNPMVQQGNVPPNFMVMQQQPPNQGPQSLHPGLGGMPKRLPPGFSAGQANPNFMQGQVPSTTATTPGNSGAPQLQANQNVQHAGGQGAGPPQNQMQVSHGPPNMMQPSLMGIHGNMNNQQAGTSGVPQVNLSNMQGQPQQGPPSQLMGMHQQIVPSQGQMVQQQGTLNPQNPMILSRAQLMPQGQMMVNPPSQNLGPSPQRMTPPKQMLSQQGPQMMAPHNQMMGPQGQVLLQQNPMIEQIMTNQMQGNKQQFNTQNQSNVMPGPAQIMRGPTPNMQGNMVQFTGQMSGQMLPQQGPVNNSPSQVMGIQGQVLRPPGPSPHMAQQHGDPATTANNDVSLSQMMPDVSIQQTNMVPPHVQAMQGNSASGNHFSGHGMSFNAPFSGAPNGNQMSCGQNPGFPVNKDVTLTSPLLVNLLQSDISAGHFGVNNKQNNTNANKPKKKKPPRKKKNSQQDLNTPDTRPAGLEEADQPPLPGEQGINLDNSGPKLPEFSNRPPAPSQNLVSKETSTTALQASVARPELEVNAAIVSGQSSEPKEIVEKSKIPGRRNSRTEEPTVASESVENGHRKRSSRPASASSSTKDITSAVQSKRRKSK
Protein: Fructose-1,6-bisphosphatase (Q72BU5)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Transketolase
- fructose-bisphosphate aldolase
- Transaldolase, putative
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Fructose-1,6-bisphosphatase class 1
- mannose-1-phosphate guanylyltransferase
- 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
- Arginine N-succinyltransferase, beta subunit, putative
- Uncharacterized protein
Sequence:
MEAPEKNLALDLVRVTEAAALASARWLGKGNNDAGDQAAVDALRLSFNSLHVKGRVIIGEGEKDNAPMLFNGEEVGTGHGPALDVAVDPVEGTKLLAYGRPNAISVVGIAPAGTMYNPGPSFYMQKLVVPPAARDVVDIDAPVKENLKNIAKSLGKDVDDLVVFVLDKPRHEKLIHKIREAGARIQLHTDGDVAGALMAVDPRSEVDVMMGTGGTPEGVLAACAIKGIGGQMLARLDPQSYVEKEAIREAGIDTRDILTVDTLVRSDEVFFAATGISGGTFLRGVQYLGNGAVTHSMVIRGKTGTLRYIESYHNWDRLMKISSVKYD
Protein: Hsp70-Hsp90 organizing protein 1 (GmHop-1) (Heat shock protein STI) (GmSTI) (Stress-inducible protein) (Q43468)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Mediates nuclear encoded chloroplast preproteins binding to HSP90 prior to chloroplastic sorting (By similarity). Mediates the association of the molecular chaperones HSP70 and HSP90.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit epsilon
- PHP
- Heat shock 70 kDa protein
- Heat shock 70 kDa protein
- Anaphase-promoting complex subunit 4
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit beta
Sequence:
MAEEAKAKGNAAFSAGDFAAAVRHFSDAIALSPSNHVLYSNRSAAHASLQNYAEALADAQKTVDLKPDWPKAYSRLGAAHLGLRRHRDAFSAYKTGLQLDPDNAALKSGLADAQAAASRPPPTSPFATAFSGPDMWARLTADPTARANLQDPEFVKIMQDIQKDPNKFNLHLSDQRVMHAIGVLLNVKIQTPNHDENDHDADDDVSEDEVVSQPEPEHEPEAAVEVAEEEEEEEKETRDRKGQAQKEKEAGNAAYKKKDFETAIGHYSKALELDDEDISYLTNRAAVYLEMGKFEDCIKDCEKAVERGKELRSDYKMIARALTRKGTALAKMAKCSKDFEPAIEIFQKALTENRNPDTLKKLNEAEKAKKELEQQEYFDPKLADEAREKGNELFKQQKYPEATKHYTEAIKRNPKDAKAYSNRAACYTKLGAMPEGLKDAEKCIELDPTFSKGYTRKGAVQFSMKEYDKALETYREGLKHDPNNQELLDGIRRCVEQINKASRGDFTPEELKERQAKAMQDPEIQSILQDPVMTQVLTDFQENPRAAEEHVKNPMVMNKIQKLISAGIVQMR
Protein: Complement component C9 (B8A565)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}. Target cell membrane {ECO:0000256|ARBA:ARBA00004276}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004276}.
Interaction partners:
- Complement component 8, alpha polypeptide
- Complement C5
- Complement component 7b.
- Complement component C8 beta chain
- Complement component 8, gamma polypeptide
- Aerolysin-like protein
- MAC-inhibitory protein
- Complement component 6.
- Complement C3a, tandem duplicate 6
- Complement component c3a, duplicate 1.
Sequence:
MKALAALCVTICLLYQANGKSITDPVQGSRREVRQINDPPPVDCKMSAWSQWSPCDPCTNTTYRSRSIEVFGQFKGTVCSNPIGDRRLCVPKTKCQMDDPPVCKSSQWQCTFTRMCINKNLRCNGDNDCGPTDESDEEDCDVIRSPCGKTAVFESDIALKAGYGINILGSGPRNNPFDNKVYNGQCNRIRDPNSMEYNRLPWNVGVLHYETKVEESSSKEMYEDIHSLIKEITRETSSTFEIGLNFKFTPTETSKNDEGGNAGSAGEGGNAGSAGEGGNAGSAGEGGEVASPNEGGAAAGPVEGGGGEGPATSGGAGVGGDPGVSGGIPDAAPGFGISGSAGANYKQTTTNIIKQLSELTTTKRKTFMRVKGRVELATYRMRQRGLEVSSTFLDDVDALPLQYEKGQYFSFLEEYGTHFTKNGKSGGEYQLVYVMNEDIRKQKHVTEATVKKCFELGLKADFQLTPAAEGGGEVKPLNDCNSLTNTDTDEKNNKGVIDKVLIEVKGGSAASAVAMKSQLTKDGILDYNQYVEWAKTITILPALIQSEPEPIYNAIPLSFPDAQPRRDNLKRALDEYVAEYSVCKCQPCQNGGTVIQIDGQCKCMCLPGSEGVACQIIDMEMMKGKTFEQLGNWGCWSAWSHCSGGRRTRSRSCNNRGLTNGICKGDKTSEDYC
Protein: GPI-anchored hemophore RBT5 (Repressed by TUP1 protein 5) (Q59UT4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: GPI-linked hyphal surface heme-binding protein involved in heme-iron utilization. Heme transfer occurs between PGA7, RBT5 and CSA2 supporting a model in which the 3 CFEM proteins cooperate in a heme-acquisition system and form a cross-cell wall heme-transfer cascade. The ability to acquire iron from host tissues is a major virulence factor of pathogenic microorganisms. Required for biofilm formation.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:18227255, ECO:0000269|PubMed:18466294, ECO:0000269|PubMed:25275454}. Cell membrane {ECO:0000269|PubMed:15306022, ECO:0000269|PubMed:18466294}; Lipid-anchor, GPI-anchor {ECO:0000303|PubMed:12845604}. Note=Found anchored in the cell membrane as well as a covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000269|PubMed:18466294}.
Interaction partners:
- Agglutinin-like protein 3
- ferric-chelate reductase
- High-affinity iron permease
- GPI-anchored hemophore PGA7
- Siderophore transporter
- Hyphally regulated cell wall protein 1
Sequence:
MLALSLLSIVSIASAAGVTAIPEGDNPYTIFPSVAKTASINGFADRIYDQLPECAKECVKQSTSSTPCPYWDTGCLCVMPQFAGAVGNCVAKNCKGKEVGSVESLATSICSSAGVWEPYWMIPSSVSDALAKAADAAAETTAESTTAESTAAETTKAEETSAKETTAAETSKAAESSAPAETSKAEETSKAAETTKAEESSVAQSSSSAADVASVSVEAANAGNMPAVAIGGVIAAVAALF
Protein: Mitochondrial inner membrane m-AAA protease component paraplegin (EC 3.4.24.-) (EC 3.6.-.-) (Paraplegin) (Spastic paraplegia 7 protein) (Q3ULF4)
Organism: Mus musculus (Mouse)
Function: ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:22563492}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Peptidyl-prolyl cis-trans isomerase F, mitochondrial
- Mitochondrial inner membrane m-AAA protease component AFG3L1
- Non-selective voltage-gated ion channel VDAC1
- Prohibitin 1
- Lon protease homolog, mitochondrial
- Prohibitin-2
- ATP-dependent clpX-like chaperone, mitochondrial
- ADP/ATP translocase 2
- ADP/ATP translocase 1
Sequence:
MAAALLLLRGLRPGPEPRPRRLWGLLSGRGPGLSSGAGARRPYAARGTPVGPAAAGGHAPQSLLLRILTPSFEGISGLLLKQHIVPNAVRLWPLSGSTLYFNTSRMKQKNKDNDKPKGKTPEDDEEEKRRKEREDQMYRERLRTLFIIALVMSLLNSLSTSGGSISWADFVNEMLAKGEVQRVQVVPESDVVEVYLHPGAVVFGRPRLALMYRMQVANIDKFEEKLRAAEDELNIESKDRIPVSYKRTGFFGNALYALGMTAVGLAILWYVFRLAGMTGREGGFSAFNQLKMARFTIVDGKTGKGVSFQDVAGMHEAKLEVREFVDYLKSPERFLQLGAKVPKGALLLGPPGCGKTLLAKAVATEAQVPFLAMAGPEFVEVIGGLGAARVRSLFKEARARAPCIVYIDEIDAVGKKRSTSMSGFSNTEEEQTLNQLLVEMDGMGTTDHVIVLASTNRADVLDNALMRPGRLDRHVFIDLPTLQERREIFEQHLKGLKLTQPSSFYSQRLAELTPGFSGADIANICNEAALHAAREGHTSVHTFNFEYAVERVIAGTAKKSKILSKEEQRVVAFHESGHALVGWLLEHTEAVMKVSIAPRTNAALGFSQMLPRDQYLFTKEQLFERMCMALGGRAAEAISFSRVTSGAQDDLRKVTRIAYSMVKQFGMAPSIGPVSFPEAQEGLMGIGRRPFSQGLQQMMDHEAKLLVAKAYRHTEKVLLDNLDKLQALANALLEKEVINYEDIEALIGPPPHGPKKMIAPQKWIDAEKERQASGEEEAPAP
Protein: Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily (E0SFZ7)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}. Cell membrane {ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Peptide transport periplasmic protein
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Peptide transport system ATP-binding protein
- Peptide transport system ATP-binding protein
- Dipeptide transporter membrane component of ABC superfamily
- Putative transporter, permease protein
- ABC transport protein inner membrane component
- Dipeptide binding protein
- Dipeptide ABC transporter, periplasmic component
- D-ala-D-ala transporter subunit
Sequence:
MHSDNIYGEKELPSRWRDTWNVFRQDRMAMVGFYGFLLLLGLCLFGDTLAPYALDQQFLGYQLLPPSWSRYGEVSFFLGTDDLGRDLLSRLLSGTAPTFGSALLVTLAAMLAGILIGLLAGVTHGLRSAILNHILDPLLSIPSLLLAMVVIAFIGPQLTHAMLAVWMALLPRMVRTIYTAVHDELEKEYVTAARLDGASTRYIIWYAVVPNILPLLVSEVTRALSIAILDIAALGFLNLGAQLPTTEWGVLLGNSLELVYAAPWTVMLPGAAITLSVLIVNLLGDGIRRALLAQTE
Protein: Transcription factor BTF3 (Nascent polypeptide-associated complex subunit beta) (NAC-beta) (RNA polymerase B transcription factor 3) (Q64152)
Organism: Mus musculus (Mouse)
Function: When associated with NACA, prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. BTF3 is also a general transcription factor that can form a stable complex with RNA polymerase II. Required for the initiation of transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus. Note=The heterodimer with NACA is cytoplasmic. {ECO:0000250}.
Interaction partners:
- Nascent polypeptide-associated complex subunit alpha, muscle-specific form
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL1
Sequence:
MRRTGAPTQADSRGRGRARGGWPGAEATPSLPLGGSRGRESQMKETIMNQEKLAKLQAQVRIGGKGTARRKKKVVHRTATADDKKLQFSLKKLGVNNISGIEEVNMFTNQGTVIHFNNPKVQASLAANTFTITGHAETKQLTEMLPSILNQLGADSLTSLRRLAEALPKQSVDGKAPLATGEDDDDEVPDLVENFDEASKNEAN
Protein: Cytochrome c biogenesis ATP-binding export protein CcmA (EC 7.6.2.5) (Heme exporter protein A) (P33931)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01707}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01707}.
Interaction partners:
- Heme exporter protein D
- Heme exporter protein C
- Heme exporter protein B
- Cytochrome c-type biogenesis protein CcmE
- Cytochrome c-type biogenesis protein CcmF
- Cytochrome c-type biogenesis protein CcmH
- Thiol:disulfide interchange protein DsbE
- Periplasmic nitrate reductase, electron transfer subunit
- Cytochrome c-type protein NapC
- Formate-dependent nitrite reductase complex subunit NrfF
Sequence:
MGMLEARELLCERDERTLFSGLSFTLNAGEWVQITGSNGAGKTTLLRLLTGLSRPDAGEVLWQGQPLHQVRDSYHQNLLWIGHQPGIKTRLTALENLHFYHRDGDTAQCLEALAQAGLAGFEDIPVNQLSAGQQRRVALARLWLTRATLWILDEPFTAIDVNGVDRLTQRMAQHTEQGGIVILTTHQPLNVAESKIRRISLTQTRAA
Protein: Uncharacterized protein C146.02 (Q9Y807)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MNGIRKKPATLQLHNIKTSCFIDGSDDQSDRTRSSSGDSTSNSLKLSHHISDELINAIYKELKSPVSPWDKNISQHSPWLLEAASNSIGDSSPLLSPISPLKLRFHKYSVSKQLNSVGKQGFGLSSNHSRYASPSSPARLARGALGEELSNSQYRLECAAIQKLVAQKRANRRSSKSTLKNSANDIEFFDIEEVSSRKGLIDRTPSKRNVTSRVSDAYSRLKSAVKGESSLSFKRNRSKSKRKIQHLGLTEFNGWEHHQCDWL
Protein: NUMB endocytic adaptor protein (Protein numb homolog isoform X1) (F1RDZ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNKLRQSFRRKKDVYVPESSRPHQWQTDEEAVRGGKCSFAVKYLGHVEVEESRGMHICEDAVKKLKTAGKKAVRAVLWVSADGLRVVDDKTKDLILDQTIEKVSFCAPDRNFEHAFSYICRDGTTRRWICHCFMAIKDSGERLSHAVGCAFAACLERKQKREKECGVTATFDANRTTFTREGSFRVTTATEQAEREEVMRQLQDNKKDSDLVISSSSGGSCNPVVVTLAGPNGSSSPPLPMAPLGLQDGNPHVIPRRHAPVEALARQGSFRGFPALSQKTSPFKRQMSLRMNELPSTMQRKSDFPIKNTVPEVEGEVDSISSLCTQITSTFSGPPEDPFSSAPMPKPASSPQSPAAPVNGAVPAFPPPSVTVTTAANSPVLPPPPLPVRETNPWAKAPNTAPAHAAHTGSEWPSPSPSTGALPAVSATLSTPTSAHKRTPSEADRWLEEVTKSVRAHQPASTARTSTPPAQQPFPAPVPVPLPPSAPFMPPIPPSAVPSVPPRQPAFHAQAPVSFPVSNGIPYAQPTFPIVGITPSQMVANVFGSATQTQPISVPVPVAQTQLQSSPFSTPPATQFEPQPVCSPFGKPLLPPVPNTVVLQPPPKPSPAFNGANSWAAAASAGQAGANPPQADAFEAQWAALESRSQQRTAPSPTNPFSSELHKTFEIQL
Protein: Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B) (Q00729)
Organism: Rattus norvegicus (Rat)
Function: Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. 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 {ECO:0000250|UniProtKB:P70696}. Chromosome {ECO:0000250|UniProtKB:P70696}.
Interaction partners:
- Histone H2A type 4
- Histone H3.1
- Histone H3
- Histone H4
- Histone H3.3
- Histone H3
- Histone H3
- Histone H3
- Plasminogen
- Histone H2A type 2-A
Sequence:
MPEVSAKGTTISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Homeobox protein Scarecrow (Q9NCG1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
NLSSIHHLQNLHSQHQSTLFNSNHSTPFSVTDILSPIEESYRKLELNGNPPSPFRSNSSSSSINSPGTLTTSTMANPYAMGTLYHSPGVQTYCGPTDNLSLAGHYTDMRNSASWYGSTANDPRFAISRLMSSSASGTMSHMGNMSGLAACSVSDSKPLQFPLAQRRKRRVLFTQAQVYELERRFKQQRYLSAPEREHLASLIHLTPTQVKIWFQNHRYKCKRQAKRKAMAEQNQHNQPASSPRRVAVPVLVKDGKPCSGNNSSSQSQQHGTNSTSAGNNTGSANNGNANSGIVSVTANVSGGLNLITGDAPNSHSPDTSSSLLASYGTVGGSNVAMLQQPCNNTLMSNSLAMAYRNQNNFIFNGHQQQCGGYLPLQGRAW