wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein eS7x (40S ribosomal protein S7-3) (Q8LD03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein uS9x
- Small ribosomal subunit protein eS10x
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein uS15z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein eS1y
- Small ribosomal subunit protein eS1z
Sequence:
MFSAQNKIKKDKNAEPTECEEQVAQALFDLENTNQELKSELKDLYINQAVHMDISGNRKAVVIYVPFRLRKAFRKIHPRLVRELEKKFSGKDVIFVTTRRIMRPPKKGAAVQRPRNRTLTSVHEAMLEDVAFPAEIVGKRTRYRLDGSKIMKVFLDAKEKNNTEYKLETMVGVYRKLTGKDVVFEYPVEA
Protein: Protein PATRONUS 2 (Q94CK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Not required for protection of centromeric cohesion.
Interaction partners:
- SHUGOSHIN 2
- SHUGOSHIN 1
- Exocyst complex component SEC10b
- Shugoshin
- Separase
- Annexin D8
- Cell division cycle 20.1, cofactor of APC complex
- Cell division cycle protein 27 homolog B
- Separase
Sequence:
MANTILRGQMIFQDENALAALGKKAVAAGKGKSSLAAPKKNGAGFGSRKALHDITNKSKLQPQASSTTRKDVEGVDFDIAKEGFLHDHSKCIEEQQQDQWDSYFSEHIILHGHETNIKEGVPQYNNIQEIDAENSWDELKEIPMEEFSDLLECSTQWRSPPDSLSHHHSSLPSSPLPWHFETVEFKLKEDEDTT
Protein: Transcription factor MYBS2 (Myb-related protein S2) (OsMYBS2) (Q7XC51)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that binds to 5'-TATCCA-3' elements in gene promoters. Derepresses weakly the sugar-repressed transcription of promoters containing SRS. Contributes to the sugar-repressed transcription of promoters containing 5'-TATCCA-3' elements.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
Sequence:
MEQHEEAAERKPSPPVIFRLFGVEVRGGGGGVDEEEYEEEEVEGGLFIKKSSSMPNLTSIDPLPVPADGGKRRASDDSELASGQQKRRRRKVQERKKGVPWTEEEHKKFLEGLRQLGKGDWRGISKNFVTSRTATQVASHAQKYFLRQTNPGKKKRRASLFDVVAECSDDQLPSPQSVGTKPPTQDIIHTDRGDVPILSYPVARGFRGDSVQVDELTEYVKRLKAAEDMSLSMISGLEMASSSISSLELSIAPPHCAIEAAIKVL
Protein: E3 ubiquitin-protein ligase ipaH9.8 (EC 2.3.2.27) (Invasion plasmid antigen 9.8) (Q8VSC3)
Organism: Shigella flexneri
Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell. Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), a ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG. Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection. Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme. Mediates polyubiquitination of host U2AF1, leading to its proteasomal degradation.
Subcellular location: Secreted {ECO:0000269|PubMed:11115111}. Host cytoplasm {ECO:0000269|PubMed:11418613, ECO:0000269|PubMed:29144452}. Host nucleus {ECO:0000269|PubMed:11418613}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm (PubMed:11115111, PubMed:11418613). Transported into the host nucleus (PubMed:11418613). This transport is independent of cytosolic factors, but dependent on temperature and partly on ATP/GTP (PubMed:11418613). {ECO:0000269|PubMed:11115111, ECO:0000269|PubMed:11418613}.
Interaction partners:
Sequence:
MLPINNNFSLPQNSFYNTISGTYADYFSAWDKWEKQALPGEERDEAVSRLKECLINNSDELRLDRLNLSSLPDNLPAQITLLNVSYNQLTNLPELPVTLKKLYSASNKLSELPVLPPALESLQVQHNELENLPALPDSLLTMNISYNEIVSLPSLPQALKNLRATRNFLTELPAFSEGNNPVVREYFFDRNQISHIPESILNLRNECSIHISDNPLSSHALPALQRLTSSPDYHGPRIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYPQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLPENGSQLHHS
Protein: V-type ATPase, C subunit, putative (EC 3.6.3.14) (Q586H7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- V-type proton ATPase subunit F
- 
- V-type proton ATPase subunit
- ATP synthase, putative
- Uncharacterized protein
- Vacuolar proton pump subunit B
- V-type proton ATPase subunit a
- Vacuolar ATP synthase subunit D, putative
- H
- V-type proton ATPase subunit H
Sequence:
MAVESDVLPPLTRLPPDEALSFIWKITRSILILVFVIFAVIPALCGTVYPPFSALWDVIAAISPYTWGSVGIGIGISLSIGGAAWGILTTASSLSGAAIRAPQIRSKNLISIIFCEAVAIYGVILSIIMMGKMEADGKAVDSSGIFTYRAAAAGFTLFAAGLAVGLGNMCCGIAVGVVGSSCAIADAHSSSLFVKILVIEIFASALGIFSVIVGILMAQKAVMV
Protein: Zinc finger FYVE domain-containing protein 9 splice variant Z2.1 (Zinc finger, FYVE domain containing 9) (A0S860)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNLNKMKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGTEVPQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVATSPLPTEADTSLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVGSLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLLLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEDPQEQIHIQWVDDDKTVNKGVVSPIDGKSMESITNVKIFHGSEYKANGKVIRWTEVFFLENDDHHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIA
Protein: Uncharacterized protein (Q38A86)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSTTCLVGPTWVAPQLVITITIINIVDVISSHFVVWVSSLCSVLPCRCGCIHALHCGLLFVFFCLHVTPHLKKKNTRQFKMYSDSESIISEFDDFTSDEDPEMDDFDRLLDEQVEHQEDSLYTLRLSYLRLFEDEDGPLRSAFPDLYVPSKEILLDLSNVLSCEGDCEEDGENVEYEGEDIDWEAAAKDHEAFDKHGEEGGDDGDAEENHDVRLQPENGCAETTLRTVGKPSPATKFMDKHRGNSLLVEVGLTVSRSELRERHVAQYPDIDFVVGYIQREPTGWALLMTEDPNTVEGIKSYYPSHRLATESDYVMFFRSTHPKKTGFVTIPNPPQRQQKKGRRQYIRQMQSSAALSAHIEAMGGMQNAIFVFLDVEAAVVQKNSVPLPLEIALVPSGGDHSFQPFHCFLHPGVIENSQVALGLSCGAIPSSHHVPLNNVTFLRRDYTKVAEEISQFLSCERVVLINKGSLMDVQALRWVFGAARIAESSNMPIPKLEDIACFDIQALKKLLAQGEWRETKGDAAETHGEFCWYHAGMQEGLRREIVGYTESHCALKDAQVIHGVVQRYL
Protein: NEK6-subfamily protein kinase (EC 2.7.11.34) (Q5TBG1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSL
Protein: Sodium-dependent nutrient amino acid transporter 1 (B3MRS1)
Organism: Drosophila ananassae (Fruit fly)
Function: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity).
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
Sequence:
MELKPNGNHNNNNAAEKSEDTEKAKAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSICPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSFCREDWQNCVDSRPAEYTENLITGLASNASTLASNLTTPFSNRGVSLLADNETVKLQSSSEIYFLDVVIKEKLDISDGIGSPDWKLTLALLASWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGIIFFLQPQWGELLNPTVWKNAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLNIENIQDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGLKYWKVALGTSMCGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWIYGLQNFCDDIEFMCNRRVSLYWRMCWSFFTPVMMIIIFIYSMVTIEPIKYSELYFPEAGNVAGWLLFGIGAAQFPLWGLWYVSRHREGSFCSSIMASLKPSEKWGPANAEVKREWQIFKSQKAAQRAVQKESSKLGFFWRKITNFCGSNI
Protein: Thioredoxin H9 (AtTrxh9) (Thioredoxin 9) (AtTRX9) (Q9C9Y6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol-disulfide oxidoreductase that may play a role in intercellular communication due to its ability to move from cell to cell.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20133584}.
Interaction partners:
- Thioredoxin domain-containing protein 9 homolog
- AT5g02160
- Sulfhydryl oxidase 2
- At4g35750
- Monothiol glutaredoxin-S9
- Bifunctional TH2 protein, mitochondrial
Sequence:
MGSCVSKGKGDDDSVHNVEFSGGNVHLITTKESWDDKLAEADRDGKIVVANFSATWCGPCKIVAPFFIELSEKHSSLMFLLVDVDELSDFSSSWDIKATPTFFFLKNGQQIGKLVGANKPELQKKVTSIIDSVPESPQRP
Protein: Probable glutathione-independent glyoxalase hsp3104 (EC 4.2.1.130) (Glyoxalase 3 homolog 4) (Heat shock protein 31 homolog 4) (Q10092)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable hydroxyacylglutathione hydrolase SPCC13B11.03c
- Lactoylglutathione lyase
- Probable hydroxyacylglutathione hydrolase glo2
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- 2-hydroxyacid dehydrogenase homolog 2
- Glutathione-independent glyoxalase DJ-1
- Probable nudix hydrolase C6G9.05
- Threonine dehydratase, mitochondrial
- Tryptophan synthase
- Copper amine oxidase 1
Sequence:
MVLFMKTVQRPEHISLKSCIPFKSLQRQGIVFRLSVRMVMLADDHSISDSALSDSDKNAFKDKNNDFWKAIKNAKNASDINFSDYSIFFAAGGHGTLFDFPSATNLHKGAAKIYSMGGVIAAVCHGPVILPCIKDSTGFSIVKGKTVTAFNEIAEQQMNLMPTFEKYHFKTLNKLFQEAGSNFVDPQEPFDDFVKTDGKLVTGANPASAASTAKAALNSLNS
Protein: Thioredoxin M5, chloroplastic (OsTrxm5) (Q9ZP20)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Thiol-disulfide oxidoreductase probably involved in the redox regulation of chloroplastic enzymes. Required for chloroplast biogenesis and differentiation. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in hydrogen peroxide scavenging system in chloroplasts. Possesses reducing activity towards insulin disulfide bonds.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18723667}.
Interaction partners:
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Peptide methionine sulfoxide reductase A4, chloroplastic
- Thioredoxin F, chloroplastic
- Peptide methionine sulfoxide reductase A5
- Peptide methionine sulfoxide reductase A2-1
- Peptide methionine sulfoxide reductase A2-2
Sequence:
MALETCFRAWATLHAPQPPSSGGSRDRLLLSGAGSSQSKPRLSVASPSPLRPASRFACQCSNVVDEVVVADEKNWDSMVLGSEAPVLVEFWAPWCGPCRMIAPVIDELAKEYVGKIKCCKVNTDDSPNIATNYGIRSIPTVLMFKNGEKKESVIGAVPKTTLATIIDKYVSS
Protein: Uncharacterized protein (Q38A52)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEESLTFAEVVARKNRGSQSELVGADDSVASLPSHGALQNGLIVLPSRPSVGESYADAVKSASVKLGGVPVNVSKLDGHESVTNSTLQEQESVLSSWADDDECFFDSVRNALQNRNDEFELRGYPNNSLSYVNVGNNGSNNVYGNSNNNYGGYSNFRRGRGSRGWRFINGNEANSSNGNTHSNNNKKRKGYNNKTWGSYNPPCGVDSLNHFGGGRFSGFR
Protein: Metallothionein-like protein 2C (Class I metallothionein-like protein 2C) (OsMT-I-2c) (OsMT2b) (A3AZ88)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals (Probable). Acts as reactive oxygen species (ROS) scavenger in the cytosol. Possesses superoxide anion and hydroxyl radical scavenging activities in vitro. Plays a role during root development, lateral root initiation and seed embryo germination, possibly by regulating levels of cytokinin.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15220467}.
Interaction partners:
Sequence:
MSCCGGNCGCGSGCQCGGGCGGCKMFPDVEATATTKTFVLAAPSNKASSGGMEMAVESGENGGCGCNTCKCGTSCSGCSCCSCN
Protein: Hsk1-interacting molecule 1 (DNA repair protein rad35) (O59836)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Activates hsk1 kinase and is essential for G1/S transition. Has a role in S-phase checkpoint control induced by replication fork blocks after nucleotide deprivation and DNA damage.
Subcellular location: Nucleus {ECO:0000269|PubMed:10409743}.
Interaction partners:
- Cell cycle serine/threonine-protein kinase hsk1
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm5
- DNA replication licensing factor mcm6
- DNA replication licensing factor mcm3
- DNA replication licensing factor mcm7
- Cell cycle protein kinase spo4
- Serine/threonine-protein kinase cds1
- DNA replication licensing factor mcm10
Sequence:
MNLGRCPLAPRSANIVLPKHDAVSKQKEYRIEEKTNEAQREEIITWKDNREDEGEVKTDFEVVNNENIITTTPKHQTVITPKSYRKSVKRIKHDAPQNEDIPVMKGLAPINADTESKAESMAAGKVLGSKNSSQKARLQEWKRQYKKAFPHFRFYLDGCDPSVAHRVKKQIQQLGGHVETFFSGNVTHVATVRAIQDVSVKYAKQDVITKARQLNMKIWSMEKLCNRVLKTLMENDQCTTNAPTKQGNDLSYLLYVEKVQGTNERDLSVPRQDFVHFRGPYLYVHDIANIYKPILLREWQKPLPDRDVPWPTFRATSIGRCPFVPETKYRLSTSKSLVAKNDQQLLQRQSQEPSLILRANSMKASLPDISNTGISGMNTNTTYNTNINNTPQTAISGITQDTSPSIRTNCHHCLDDGMQASGIVQSNLTSAAMSNNSAIRSGSAASVPVVTINGRDIAELKKRIIQQKSGMIGKDYSYKAMLHNTSQRKIRVDAKPGYCENCREKFDNFESHIRSSRHRRFAENNDNFKDLDELFALVQRPLRPD
Protein: Baculoviral IAP repeat-containing 2 (Q6P6S1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- TNF receptor-associated factor
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Mitogen-activated protein kinase kinase kinase 7
- TNF receptor-associated factor
- Caspase-9
- Diablo IAP-binding mitochondrial protein
- Diablo IAP-binding mitochondrial protein
- RING-type E3 ubiquitin transferase
- Toll-like receptor 4
Sequence:
MENSTVLSNWTKENKEKMKYDFSCELYRMSTYSAFPRGVPVSERSLARAGFYYTGVNDKVKCFCCGLMLDNWKQGDSPTEKHRQFYPSCSFVQTLLSGGLQSAAKNTSPAKSRFAHSLPLEQGGIHSSLPSNPLNSRAVEDFSLRMNPCSYAMSTEEARFLSYSMWPLSFLSPAELAKAGFYYTGPGDRVACFACGGKLSNWEPNDDPLSEHRRHFPHCPFLENTSETQRFSVSNLSMQTHSARMRTFLYWPSSVLVQPEQLASAGFYYVDHNDDVKCFCCDGGLRCWEPGDDPWIEHAKWFPRCEFLIRMKGQEFVDEIQARYPHLLEQLLSTSDTSEEENADPPVVHLGPGENWEDAVMMNTPVVKAALDMGFSRSLVRQTVQRQILATGENYRTVSDIVSALLNAEDERREEEKERQSEETASGDLSLIRKNRMALFQQLTCVIPILDDLLEASVLTKEEHDIIRQKTQIPLQARELIDTILVKGNAAASVFKNSLKEVDSTLYEHLFVEKTMKYIPTEDVSGLSLEEQLRRLQEERTCKVCMDREVSIVFIPCGHLVVCRECAPSLRKCPICRGTIKGTVRTFLS
Protein: Histone-lysine N-methyltransferase, H3 lysine-79 specific (EC 2.1.1.360) (Histone H3-K79 methyltransferase) (Q6AW06)
Organism: Caenorhabditis elegans
Function: Histone methyltransferase, which in complex with zfp-1, methylates 'Lys-79' of histone H3 to activate transcription (Probable). During stress, the zfp-1-dot-1.1 complex also plays a role in the deubiquitination of histone H2B sites, which negatively modulates the RNA polymerase II-induced transcription of highly expressed genes. Involved in controlling tissue-specific gene expression, particularly in the epidermis.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU271113, ECO:0000305|PubMed:23806335}. Chromosome {ECO:0000305|PubMed:23806335}. Note=zfp-1 and dot-1.1 colocalize to promoters of highly expressed genes (PubMed:23806335). zfp-1 recruits dot-1.1 (PubMed:23806335). {ECO:0000269|PubMed:23806335}.
Interaction partners:
- Zinc finger protein zfp-1
- Multifunctional procollagen lysine hydroxylase and glycosyltransferase
- Transmembrane protein
- Uncharacterized protein
Sequence:
MSEADAGARDESPSRTAEEPAAAMRIKEERRSSSVDVVDVGNGELLVLHSIFYQGKTLRLPGNRAHMYPVVFQMIKGVCSLVKQLVVAFPKGWDQNTPSISEIAALTKSFNRVAKPFASNWSGSYNTDTLKEWGEPNCSAEVAKAITTYAYECAVPRPADLNQHYKSFTSETYGETNPEQLISIIDELNIGPQDVFVDLGSGIGQLVCLTAAYAKCKKSVGIELSQVPSNFAQDLAGYFKKFMSHFGKNHGKFEHIQGDFLNPKFKQLICEEATVIFINNFAFDAALMLRINTELLQDLKHGTRIVTTKELGTNKKEITFRSTSDINAISHTTELKTTESAVSWTSSHVKFWLTTIDHTKLIKYYEDQRRRQEVKSSREGSEISDGRDMGLKKRKSQRESSVHPDKLQKTEQAAASSHQSPKWNEPDTDYTPPAKKPKKEKLLREQQDATPASSHHHGASSSSGKDREKEKEKKKNKIYEEKKVKTPKPPKSSSSRYSSETPTSHHHHHRSNSISHSSDVIRPSQPKATAPPPPLVPAPARATASTPPPAPPAARAQSPKREEPLEPPTDLIHHGGGQLDAKTMNALHTIREAATTSAQAAAIQDAINSVLSQPTEASPSAFGPPLAHLPAPVAIYPTPPPPPAPAPAAPQQASAAPAAPNVMPVCTEIAAEQRHTFMIPPTDPFYNMIVSYYFAMKQFCNQSKTADPEFVGRLRLDIEAEEARRAELKESITLTSTQIDELLATGVNTLKSRLDELGMPSVTDVTELLAGSKQIVTQHKGLTNTVAQMENSVAVEEQKLRLIGGPDAVRYFDEAMSHPNVDIAKLTDLVITTRPPNFVAQILLPDDSPTASIDSKVSPSSSSSRRPRQPKPRANNTAAGAGGGGKRGTSGGRKSDGGGGGGATEDVELEIRQFVQHALKVDNAVKEKERKARGNFMAAAADRIPR
Protein: Diaminopimelate epimerase (DAP epimerase) (EC 5.1.1.7) (PLP-independent amino acid racemase) (P9WP19)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Putative succinyl-diaminopimelate desuccinylase DapE
- Diaminopimelate decarboxylase
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
- 4-hydroxy-tetrahydrodipicolinate reductase
- Aspartate-semialdehyde dehydrogenase
- 4-hydroxy-tetrahydrodipicolinate synthase
- 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase
- Aspartokinase
- GTPase HflX
- Probable aminotransferase Rv1178
Sequence:
MIFAKGHGTQNDFVLLPDVDAELVLTAARVAALCDRRKGLGADGVLRVTTAGAAQAVGVLDSLPEGVRVTDWYMDYRNADGSAAQMCGNGVRVFAHYLRASGLEVRDEFVVGSLAGPRPVTCHHVEAAYADVSVDMGKANRLGAGEAVVGGRRFHGLAVDVGNPHLACVDSQLTVDGLAALDVGAPVSFDGAQFPDGVNVEVLTAPVDGAVWMRVHERGVGETRSCGTGTVAAAVAALAAVGSPTGTLTVHVPGGEVVVTVTDATSFLRGPSVLVARGDLADDWWNAMG
Protein: RecBCD enzyme subunit RecD (EC 5.6.2.3) (DNA 5'-3' helicase subunit RecB) (Exonuclease V subunit RecD) (ExoV subunit RecD) (Helicase/nuclease RecBCD subunit RecD) (P9WHJ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD.
Interaction partners:
- RecBCD enzyme subunit RecC
- RecBCD enzyme subunit RecB
- Transcriptional repressor NrdR
- Cobalamin biosynthesis protein CobN
- DNA polymerase I
- DNA polymerase IV 1
Sequence:
MKLTDVDFAVEASGMVRAFNQAGVLDVSDVHVAQRLCALAGESDERVALAVAVAVRALRAGSVCVDLLSIARVAGHDDLPWPDPADWLAAVRASPLLADPPVLHLYDDRLLYLDRYWREEEQVCADLLALLTSRRPAGVPDLRRLFPTGFDEQRRAAEIALSQGVTVLTGGPGTGKTTTVARLLALVAEQAELAGEPRPRIALAAPTGKAAARLAEAVRREMAKLDATDRARLGDLHAVTLHRLLGAKPGARFRQDRQNRLPHNVIVVDETSMVSLTLMARLAEAVRPGARLILVGDADQLASVEAGAVLADLVDGFSVRDDALVAQLRTSHRFGKVIGTLAEAIRAGDGDAVLGLLRSGEERIEFVDDEDPAPRLRAVLVPHALRLREAALLGASDVALATLDEHRLLCAHRDGPTGVLHWNRRVQAWLAEETGQPPWTPWYAGRPLLVTANDYGLRVYNGDTGVVLAGPTGLRAVISGASGPLDVATGRLGDVETMHAMTIHKSQGSQVDEVTVLMPQEDSRLLTRELLYTAVTRAKRKVRVVGSEASVRAAIARRAVRASGLRMRLQSTGCG
Protein: Glycoprotein (P04882)
Organism: Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan) (VSNJV)
Function: Attaches the virus to host cellular receptor, inducing clathrin-dependent endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane. In neurons, neo-synthesized glycoproteins are sorted to the dendrites, where the virus buds (By similarity).
Subcellular location: Virion membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}. Host membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}.
Interaction partners:
Sequence:
MLSYLIFALAVSPILGKIEIVFPQHTTGDWKRVPHEYNYCPTSADKNSHGTQTGIPVELTMPKGLTTHQVEGFMCHSALWMTTCDFRWYGPKYITHSIHNEEPTDYQCLEAIKSYKDGVSFNPGFPPQSCGYGTVTDAEAHIVTVTPHSVKVDEYTGEWIDPHFIGGRCKGQICETVHNSTKWFTSSDGESVCSQLFTLVGGIFFSDSEEITSMGLPETGIRSNYFPYISTEGICKMPFCRKQGYKLKNDLWFQIMDPDLDKTVRDLPHIKDCDLSSSIITPGEHATDISLISDVERILDYALCQNTWSKIESGEPITPVDLSYLGPKNPGVGPVFTIINGSLHYFTSKYLRVELESPVIPRMEGKVAGTRIVRQLWDQWFPFGEVEIGPNGVLKTKQGYKFPLHIIGTGEVDSDIKMERVVKHWEHPHIEAAQTFLKKDDTGEVLYYGDTGVSKNPVELVEGWFSGWRSSLMGVLAVIIGFVILMFLIKLIGVLSSLFRPKRRPIYKSDVEMAHFR
Protein: COP9 signalosome complex subunit 5 (SGN5) (Signalosome subunit 5) (EC 3.4.-.-) (Jun activation domain-binding protein 1) (Q92905)
Organism: Homo sapiens (Human)
Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. In the complex, it probably acts as the catalytic center that mediates the cleavage of Nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex. Interacts directly with a large number of proteins that are regulated by the CSN complex, confirming a key role in the complex. Promotes the proteasomal degradation of BRSK2.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399, ECO:0000269|PubMed:9535219}. Nucleus {ECO:0000269|PubMed:17050680, ECO:0000269|PubMed:20978819, ECO:0000269|PubMed:22609399}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9535219}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:21102408}. Note=Nuclear localization is diminished in the presence of IFIT3. {ECO:0000269|PubMed:17050680}.
Interaction partners:
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1
- Ubiquitin-like protein NEDD8
- COP9 signalosome complex subunit 7b
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 8
- Transcription factor Jun
Sequence:
MAASGSGMAQKTWELANNMQEAQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKISALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQSEAQLGRGSFMLGLETHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQINIS
Protein: DNA-binding protein HU, beta subunit, putative (Q72AX6)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Viral histone-like protein
- Integration host factor subunit alpha
- DNA-binding protein HU
- Uncharacterized protein
- Large ribosomal subunit protein bL21
Sequence:
MNKSELIRTLSEETNIPIEEATIVVNTFIDNMKDSLLAGDRVEIRGFGSFKIKDYGGYSGRNPKTGKMVDVEPKRLPFFRAGKELKEFLNEQQ