wanglab/gogpt-training-data huggingface dataset:
Protein: Structure-specific endonuclease subunit SLX4 (Synthetic lethal of unknown function protein 4) (Q12098)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit that interacts with and increases the activity of different structure-specific endonucleases. Has several distinct roles in protecting genome stability by resolving diverse forms of deleterious DNA structures. Component of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for simple Y, 5'-flap and replication fork-like structures. It cleaves the strand bearing the 5'-non-homologous arm at the branch site junction and generates ligatable, nicked products from the 5'-flap or replication fork substrates. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. Has Holliday junction resolvase activity in vitro. Interacts with the structure-specific RAD1-RAD10 endonuclease and promotes RAD1-RAD10-dependent 3'-non-homologous tail removal (NHTR) during repair of double-strand breaks by single-strand annealing. SLX4 also promotes recovery from DNA-alkylation-induced replisome stalling during DNA replication by facilitating the error-free mode of lesion bypass. This does not require SLX1 or RAD1-RAD10, but probably RTT107.
Subcellular location: Nucleus. Cytoplasm.
Interaction partners:
- Structure-specific endonuclease subunit SLX1
- Regulator of Ty1 transposition protein 107
- ATP-dependent helicase SGS1
- DNA repair protein RAD1
- Crossover junction endonuclease MMS4
- Crossover junction endonuclease MUS81
- DNA replication regulator DPB11
- RecQ-mediated genome instability protein 1
- Holliday junction resolvase YEN1
- DNA repair protein RAD9
Sequence:
MELQRAQRNLKFLQNEDYVNVTDQTNLNGESQNAYSLGMETQVPEMQFSLSSDDDSIGTQVKSVTAQKSPMTQETTKNDTERNKDVDKSCNPVSTSHPDLGGSNIEENIFINTQIQSRLDDAEEETNLKLKLEKFKYSFKSSNADDTHSNANVTAKRRPAIRKANSKLKTKPKTKRDPKIIKNITDFNINNYERSRTASLLKQLSGKHKKVLDIIKTQNEGNSDKPPRARNNKGEKATFDTYSEQEWKDIMKLLLQKFPQSEETDLNEVQKFLYGSEKSSNSLDNQESSQQRLWTASQLPPELPDEAIQPEQEERIRDTQSAVNFLSLSQVMDDKSEIMKDEESIIISRGDSTSSQEYGNGLEPQQPVGNVVGEDIELAVGTRINAFSLTDYKACKPMSVEVSRRCENSTDNDYDNISIVSDTTDETSTLFPLDQYRYVFIENDERPPLATDTIGSTQFFTPNTSPLDGIIDLTQESFKAVRSLISPLKVENNKTGVTSQASNQVQVPATRTPTIIPQKNLTTTLKTEEEKNNIGSSIRVKLLQESVVKLNPKLVKHNFYRVEANDSEEEETEFDDQFCIADIQLVDSSKISTKDSTQNPTTSNDIIDTSAASSIASPEKFCEIMMSQSMKELRQSLKTVGLKPMRTKVEIIQSLQTASQILSTANPDNKGEHGGVANFSKIEIFDHLTELIEAFPDFLERIYTFEPIPLNELIEKLFSAEPFVSQIDEMTIREWADVQGICLRNDKK
Protein: PDZ domain-containing protein 8 (Sarcoma antigen NY-SAR-84/NY-SAR-104) (Q8NEN9)
Organism: Homo sapiens (Human)
Function: Molecular tethering protein that connects endoplasmic reticulum and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for endoplasmic reticulum-mitochondria Ca(2+) transfer. In neurons, involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. Plays an indirect role in the regulation of cell morphology and cytoskeletal organization. May inhibit herpes simplex virus 1 infection at an early stage.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29097544}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at mitochondria-endoplasmic reticulum contact sites. {ECO:0000269|PubMed:29097544}.
Interaction partners:
- Ras-related protein Rab-7a
- Protrudin
Sequence:
MGLLLMILASAVLGSFLTLLAQFFLLYRRQPEPPADEAARAGEGFRYIKPVPGLLLREYLYGGGRDEEPSGAAPEGGATPTAAPETPAPPTRETCYFLNATILFLFRELRDTALTRRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPSATGEPDGPEGEALPAACPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRLVFTRVPFTHWFFSFVEDPLIDFEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPNYKIRFKPFFPYQTLQGFEEDEEHIHIQQWALTEGRLKVTLLECSRLLIFGSYDREANVHCTLELSSSVWEEKQRSSIKTVELIKGNLQSVGLTLRLVQSTDGYAGHVIIETVAPNSPAAIADLQRGDRLIAIGGVKITSTLQVLKLIKQAGDRVLVYYERPVGQSNQGAVLQDNFGQLEENFLSSSCQSGYEEEAAGLTVDTESRELDSEFEDLASDVRAQNEFKDEAQSLSHSPKRVPTTLSIKPLGAISPVLNRKLAVGSHPLPPKIQSKDGNKPPPLKTSEITDPAQVSKPTQGSAFKPPVPPRPQAKVPLPSADAPNQAEPDVLVEKPEKVVPPPLVDKSAEKQAKNVDAIDDAAAPKQFLAKQEVAKDVTSETSCPTKDSSDDRQTWESSEILYRNKLGKWTRTRASCLFDIEACHRYLNIALWCRDPFKLGGLICLGHVSLKLEDVALGCLATSNTEYLSKLRLEAPSPKAIVTRTALRNLSMQKGFNDKFCYGDITIHFKYLKEGESDHHVVTNVEKEKEPHLVEEVSVLPKEEQFVGQMGLTENKHSFQDTQFQNPTWCDYCKKKVWTKAASQCMFCAYVCHKKCQEKCLAETSVCGATDRRIDRTLKNLRLEGQETLLGLPPRVDAEASKSVNKTTGLTRHIINTSSRLLNLRQVSKTRLSEPGTDLVEPSPKHTPNTSDNEGSDTEVCGPNSPSKRGNSTGIKLVRKEGGLDDSVFIAVKEIGRDLYRGLPTEERIQKLEFMLDKLQNEIDQELEHNNSLVREEKETTDTRKKSLLSAALAKSGERLQALTLLMIHYRAGIEDIETLESLSLDQHSKKISKYTDDTEEDLDNEISQLIDSQPFSSISDDLFGPSESV
Protein: Protein crumbs homolog 1 (Q8VHS2)
Organism: Mus musculus (Mouse)
Function: Plays a role in photoreceptor morphogenesis in the retina. May maintain cell polarization and adhesion.
Subcellular location: [Isoform 1]: Apical cell membrane {ECO:0000269|PubMed:11850625}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:11850625}. Photoreceptor inner segment {ECO:0000269|PubMed:11850625}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000269|PubMed:14684155}. Cytoplasm {ECO:0000269|PubMed:14684155}. Cell junction, focal adhesion {ECO:0000269|PubMed:14684155}. Note=Found in the cytoplasmic area of undifferentiated keratinocytes and associated with the plasma membrane at the site of cell-cell contacts and focal adhesion upon keratinocytes differentiation. {ECO:0000269|PubMed:14684155}.
Interaction partners:
- InaD-like protein
- Protein PALS1
- Protein crumbs homolog 3
- Multiple PDZ domain protein
- Protein crumbs homolog 2
- Carbonyl reductase 1])
Sequence:
MKLKRTAYLLFLYLSSSLLICIKNSFCNKNNTRCLSGPCQNNSTCKHFPQDNNCCLDTANNLDKDCEDLKDPCFSSPCQGIATCVKIPGEGNFLCQCPPGYSGLNCETATNSCGGNLCQHGGTCRKDPEHPVCICPPGYAGRFCETDHNECASSPCHNGAMCQDGINGYSCFCVPGYQGRHCDLEVDECVSDPCKNEAVCLNEIGRYTCVCPQEFSGVNCELEIDECRSQPCLHGATCQDAPGGYSCDCAPGFLGEHCELSVNECESQPCLHGGLCVDGRNSYHCDCTGSGFTGMHCESLIPLCWSKPCHNDATCEDTVDSYICHCRPGYTGALCETDINECSSNPCQFWGECVELSSEGLYGNTAGLPSSFSYVGASGYVCICQPGFTGIHCEEDVDECLLHPCLNGGTCENLPGNYACHCPFDDTSRTFYGGENCSEILLGCTHHQCLNNGKCIPHFQNGQHGFTCQCLSGYAGPLCETVTTLSFGSNGFLWVTSGSHTGIGPECNISLRFHTVQPNALLLIRGNKDVSMKLELLNGCVHLSIEVWNQLKVLLSISHNTSDGEWHFVEVTIAETLTLALVGGSCKEKCTTKSSVPVENHQSICALQDSFLGGLPMGTANNSVSVLNIYNVPSTPSFVGCLQDIRFDLNHITLENVSSGLSSNVKAGCLGKDWCESQPCQNRGRCINLWQGYQCECDRPYTGSNCLKEYVAGRFGQDDSTGYAAFSVNDNYGQNFSLSMFVRTRQPLGLLLALENSTYQYVSVWLEHGSLALQTPGSPKFMVNFFLSDGNVHLISLRIKPNEIELYQSSQNLGFISVPTWTIRRGDVIFIGGLPDREKTEVYGGFFKGCVQDVRLNSQTLEFFPNSTNNAYDDPILVNVTQGCPGDNTCKSNPCHNGGVCHSLWDDFSCSCPTNTAGRACEQVQWCQLSPCPPTAECQLLPQGFECIANAVFSGLSREILFRSNGNITRELTNITFAFRTHDTNVMILHAEKEPEFLNISIQDARLFFQLRSGNSFYTLHLMGSQLVNDGTWHQVTFSMIDPVAQTSRWQMEVNDQTPFVISEVATGSLNFLKDNTDIYVGDQSVDNPKGLQGCLSTIEIGGIYLSYFENLHGFPGKPQEEQFLKVSTNMVLTGCLPSNACHSSPCLHGGNCEDSYSSYRCACLSGWSGTHCEINIDECFSSPCIHGNCSDGVAAYHCRCEPGYTGVNCEVDVDNCKSHQCANGATCVPEAHGYSCLCFGNFTGRFCRHSRLPSTVCGNEKRNFTCYNGGSCSMFQEDWQCMCWPGFTGEWCEEDINECASDPCINGGLCRDLVNRFLCICDVAFAGERCELDLADDRLLGIFTAVGSGTLALFFILLLAGVASLIASNKRATQGTYSPSGQEKAGPRVEMWIRMPPPALERLI
Protein: Ubiquinone biosynthesis accessory factor UbiT (P64599)
Organism: Escherichia coli (strain K12)
Function: Required for O(2)-independent ubiquinone (coenzyme Q) biosynthesis. Likely functions as an accessory factor.
Interaction partners:
- Ubiquinone biosynthesis protein UbiV
- Ubiquinone biosynthesis protein UbiU
- Uncharacterized N-acetyltransferase YhbS
Sequence:
MLDKLRSRIVHLGPSLLSVPVKLTPFALKRQVLEQVLSWQFRQALDDGELEFLEGRWLSIHVRDIDLQWFTSVVNGKLVVSQNAQADVSFSADASDLLMIAARKQDPDTLFFQRRLVIEGDTELGLYVKNLMDAIELEQMPKALRMMLLQLADFVEAGMKTAPETKQTSVGEPC
Protein: Precursor of CEP7 (PCEP7) [Cleaved into: C-terminally encoded peptide 7 (CEP7)] (P0DN96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signaling peptide that may regulate primary root growth rate and systemic nitrogen (N)-demand signaling (By similarity). Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular location: [C-terminally encoded peptide 7]: Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:O80460}. Note=Accumulates in xylem sap. {ECO:0000250|UniProtKB:O80460}.
Interaction partners:
- Precursor of CEP15
- Precursor of CEP8
- Precursor of CEP14
- Precursor of CEP4
- Precursor of CEP6
- Precursor of CEP13
- Protein IDA-LIKE 5
- Precursor of CEP11
- Precursor of CEP9
- Protein IDA-LIKE 4
Sequence:
MAKCTLTSLILLLIVLVLIQESHIVEGRPLKSSRISNVSKKFAAGNSNLSSKLTTEDHSLDAFRPTNPGNSPGIGH
Protein: Neurotransmitter-gated ion-channel ligand-binding domain-containing protein (Q8IFY7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MWHYRLTTILLIISIIHSIRAKRKLKEQEIIQRILKDYDWRVRPRGMNATWPDTGGPVLVTVNIYLRSISKIDDVNMEYSAQFTFREEWTDQRLAYERYEESGDTEVPPFVVLATSENADQSQQIWMPDTFFQNEKEARRHLIDKPNVLIRIHKNGQILYSVRLSLVLSCPMSLEFYPLDRQNCLIDLASYAYTTQDIKYEWKEKKPIQQKDGLRQSLPSFELQDVVTDYCTSLTNTGI
Protein: Actin-related protein 3C (Actin-related protein 11) (Q9C0K3)
Organism: Homo sapiens (Human)
Function: May play a role in the suppression of metastatic potential in lung adenoma carcinoma cells.
Interaction partners:
- Actin-related protein 2
- Actin nucleation-promoting factor WAS
- Actin, cytoplasmic 1
- Actin nucleation-promoting factor WASL
- Hematopoietic lineage cell-specific protein
- Dynactin subunit 2
- Actin, cytoplasmic 2
- Actin-related protein 2/3 complex subunit 3
- Actin-binding protein WASF2
- WASP homolog-associated protein with actin, membranes and microtubules
Sequence:
MFESFNVPGLYIAVQAVLALAASWTSRQVGERTLTGIVIDSGDGVTHVIPVAEGYVIGSCIKHIPIAGRDITYFIQQLLREREVGIPPEQSLETAKAIKEKYCYICPDIVKEFAKYDVDPQKWIKQYTGINAINQKKFVIDVGYERFLGPEIFFHPEFANPDSMESISDVVDEVIQNCPIDVRRPLYKMEQIPLSYPQGHGFHPLSPPFH
Protein: DSki protein (A0PDV2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEYVTPMISTVLKKYQTSATKSLQGPGHALTTAGVLDIVTNGRSESPGLNGKCQASPPVVALIKKEILSSPEPQDLHHHECSTRGTPPQIYSPATLPRELSQPILSAADAGCGELYETKLEGKTIGCFSVGGEMRLCL
Protein: Mating-type switching protein swi10 (Q06182)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in termination of copy-synthesis during mating-type switching. Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Along with RAD16 forms an endonuclease that specifically degrades single-stranded DNA.
Subcellular location: Nucleus.
Interaction partners:
- DNA repair protein rad16
- DNA repair protein rad14
- DNA repair protein rad13
- Crossover junction endonuclease mus81
- DNA mismatch repair protein msh2
- Uncharacterized protein C1322.02
- Probable tyrosyl-DNA phosphodiesterase
- DNA repair protein rhp7
- DNA mismatch repair protein pms1
- DNA repair protein rhp41
Sequence:
MSDIDDEEFEQLAVSALEEVEKKAGFAQQPTPQKVSRVTAHSILVNPRQKGNPLLPHVRNVPWEYTDIVPDFVMGTGICSLFLSLKYHHLHPEYIYSRISKLGKSYNLRILLILVDVENHQASIQELVKTSIVNQYTLILAWSSEEAARYLETYKAYENMSPALIMEKPSTDYLSQVQSFLTSIRGINKSDSLSLLSKFGSLERALVASRDELEQLEGWGPTKVNRFLEAVQQPFMSHSTIKRPEAINLKQT
Protein: Cadherin-9 (T1-cadherin) (P70407)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cadherin-13
- Cadherin-12
- Cadherin-8
Sequence:
MRTYSCLQLVIWTCIFHMVDNSTLQGKDSSHFLRRIVNLKKDEGKMLHRAKRGWMWNQFFLLEEYTGTDTQYVGKLHTDQDKGDGNLKYILTGDGAGNLFVIDENTGDIHAAKRLDREEKSLYILRAKAIDRKTGRQVEPESEFIIKIHDINDNEPKFTKDLYTASVPEMSGVGTSVIQVTATDADDANYGNSAKVVYSILQGQPYFSVDPESGIIKTALPDMSRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNNNPPRFPQSTYQFNSLESAPLGTHLGRIKANDPDMGENAELEYSIAEGEGSDMFDVITDKDTQEGIITVKQNLDFEKKMLYTLRVDASNTHPDPRFLHLGPFKDSAMVKISVEDVDEPPVFSKLSYLMEVDEDVKEGSIIGQVTAYDPDAMNNIIKYSVDRHTDMDRVFSIHSENGSIFTLKPLDRESSPWHNITITATEINNPKQSSQIPVFIRILDINDHAPEFATYYETFVCENAKSGQLIQTISVMDKDDPPRGHKFFFEPVPEFPLNPNFTIVDNKDNTAGIVTRKDGYSRNKMNTYLLPVLIFDNDYPIQSSTGTLTIRVCACDNLGNMQSCNAEALMLAAGLSTGALIAILLCVVILLTLIVLFAALKRQRKKEPLIISKDDVRDNIVTYNDEGGGEEDTQAFDIGTLRNPEAREDSKLRRDVMPETIFQIRRTVPLWENIDVQDFIHRRLKENDSDPSAPPYDSLATYAYEGNDSVANSLSSLESLTADCNQDYDYLSDWGPRFKKLAEMYGGNDSD
Protein: V-type proton ATPase subunit (Q8SZ31)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|PIRNR:PIRNR038097}; Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR038097}.
Interaction partners:
Sequence:
MVSEWVAPIVITSIWAFIGIICPFFARGPNRGVTQCCLILTAATCWLFWLCCYMTQLNPLIGPKLSMNEIMIMAREWGNEIKDTMAVTV
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q582Q1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
- Atg6 BARA domain-containing protein
- Ubiquitin-like protein, putative
- Ubiquitin/ribosomal protein S27a, putative
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase, putative
- Ubiquitin fusion degradation protein, putative
Sequence:
MPPPFSITQEACAHCWDESAVTTPHHQSAVHKEECAYCCRTCMHNGGVLVCMCCHIALCEVHVRKHVSLRSNHAMYVWLKECPQKEDDAPRDVNKLGVVLPKEYESAICCALCSLTFSSPPELLEGCYQSILNATSTGAQGAIDANEEQFTRPQCPHLVCLEQQPSPFSPAPSHMETCVVAGCGCQTDNWMCVTCGAVGCPRPEVGGRGHALEHHNTTQHPVVVKLGTITPSGADFYCYSCDDEVSDVHFEAHMKHFGIDVKTSKKTAKTFGEIQYDYWSQFDFNRITESGETLVPVFGPGRTGMRNFGNTCYMNCVLQCLMSLEVFKEAFYAGRDTRHQNACRENPYKCRSCQVERVASGLLSGEFSISDNDEPNGITAREFKQVFAEGHPEFSTSEQQDAQEYFLYLLEEMRRYVKPSCVDAKQNRHPVDIFKMKLENRVECSSCRKVRYTYESDCCLSLPIPLGTAERRSACNRKLTEEEIEASRPRTSLEACITSLMKTIEVDCSCSACGNQVTYNETVRVATFPDVLAVYLRRAHFDAETMTVTKRDVFVEVPEEVDLEYLRGKGLQSGEVEMPSNERELRHKPVSAALTPVDEMALATLLSMGVDEKIAKYALQQTGMNVERALDYVFSRNDIEGEIARAEGSEGQLVSRGNVTAPEVDGPASYRLHAMISHMGASAKTGHYVCHIRDEETGKWLLFNDEKVAESKQPPFALASLYFYKRKRVSN
Protein: G10 protein (Q38AU1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- PRP8 protein homologue
- PHD finger-like domain-containing protein 5A
- Small nuclear ribonucleoprotein Sm D2
- U2 small nuclear ribonucleoprotein B, putative
- Small nuclear ribonucleoprotein E
- Pre-mRNA-splicing factor SYF1
- Sm protein F
- Sm protein G
- Sm protein B
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
Sequence:
MPKIRPGMKRPPPGFEKINDKLDEYDAEMRLALSEDPSQAELPVPSKRKDKQNKVEATKDKHAQSVQRGDGGVAGHSDGELDKPEPPLWRVARINRERTRYVFNACFRERIIAEEVLDYCCEMNFIDAGLVRRWSLAGYERLCCNTCCLPGAASEAARMVNKFANRDKKDRRTNGNDDTGGTCICRVPDEKRLAKAFTRCMVCGCSGCGSGGKRKHDTEEKDSVSDMKKVRTDDYEVKSGK
Protein: Colicin-E1 (P02978)
Organism: Escherichia coli
Function: This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
METAVAYYKDGVPYDDKGQVIITLLNGTPDGSGSGGGGGKGGSKSESSAAIHATAKWSTAQLKKTQAEQAARAKAAAEAQAKAKANRDALTQRLKDIVNEALRHNASRTPSATELAHANNAAMQAEDERLRLAKAEEKARKEAEAAEKAFQEAEQRRKEIEREKAETERQLKLAEAEEKRLAALSEEAKAVEIAQKKLSAAQSEVVKMDGEIKTLNSRLSSSIHARDAEMKTLAGKRNELAQASAKYKELDELVKKLSPRANDPLQNRPFFEATRRRVGAGKIREEKQKQVTASETRINRINADITQIQKAISQVSNNRNAGIARVHEAEENLKKAQNNLLNSQIKDAVDATVSFYQTLTEKYGEKYSKMAQELADKSKGKKIGNVNEALAAFEKYKDVLNKKFSKADRDAIFNALASVKYDDWAKHLDQFAKYLKITGHVSFGYDVVSDILKIKDTGDWKPLFLTLEKKAADAGVSYVVALLFSLLAGTTLGIWGIAIVTGILCSYIDKNKLNTINEVLGI
Protein: Transcription cofactor vestigial-like protein 1 (Vgl-1) (Vestigial-related factor) (Q99NC0)
Organism: Mus musculus (Mouse)
Function: May act as a specific coactivator for the mammalian TEFs.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional enhancer factor TEF-3
- Transcriptional enhancer factor TEF-1
- Transcription cofactor vestigial-like protein 4
Sequence:
MEEMKKNGVWIPESSQKPVKTEWNAGSVIFTYFEGDINSMVDEHFSRALRNLKRPHKCSSSSHSDNLTLKNGVNKTRTDTSHTDRERKVESSQTENSGELKDVPVEEKGTNKSMPPNQRHLSSWTIAQPAASPENGARSSSLDEYGLKAMDQHSLSMPKTPSALPLEPWHFSSLARPGFIAPAYFPVFPDRHLTPEVYRVFPDRHLTPEVYHVFPDRHLTPEVYPDGRCGPLQHLVQQDRYQNHPLEPAARENCSPAKIAGSTGSLMNLPPYPVHYKKKICARGAASASLDDERSPSPKRRRDAYYY
Protein: V-type proton ATPase subunit F 2 (V-ATPase subunit F 2) (Vacuolar H+ ATPase subunit 14-2) (Vacuolar proton pump subunit F 2) (Q9VNL3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit G
- V-type proton ATPase subunit H
- H
- Probable V-type proton ATPase subunit d 2
- V-type proton ATPase subunit d 1
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MSTPTHNLPRTRVSAFCWVALERSTRIERPTSWSWKELSHYSLIVFHCIPDTTPKQIEECFKKFLRRPDIVIILINQVYADMIRPTVDAHNLAVPTVLEIPSKQHPYDSSRDSILKRAQRVITPPERHY
Protein: Tubulin alpha chain (C9JQ00)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTL
Protein: T3SS secreted effector NleC (Q8X834)
Organism: Escherichia coli O157:H7
Interaction partners:
- Protein-arginine N-acetylglucosaminyltransferase NleB2
- T3SS secreted effector NleD
- Protein-arginine N-acetylglucosaminyltransferase NleB1
- T3SS secreted effector NleA/EspI
- T3SS secreted effector EspJ
- Cysteine S-methyltransferase NleE
- Secreted effector protein EspF
- Translocated intimin receptor Tir
- EspB
Sequence:
MICRVLDINMKIPSLQSNFNFSAPAGYSAPIAPNRAENAYADYVLDIGKRIPLSAADLSNVYESVIRAVHDSRSRLIDQHTVDMIGNTVLDALSRSQTFRDAVSYGIHNEKVHIGCIKYRNEYELNEESSVKIDDIQSLTCNELYEYDVGQEPIFPICEAGENDNEEPYVSFSVAPDTDSYEMPSWQEGLIHEIIHHVTGSSDPSGDSNIELGPTEILARRVAQELGWSVPDFKGYAEPEREAHLRLRNLNALRQAAMRHEENERAFFERLGTISDRYEASPDFTEYSAVSNIGYGFIQQHDFPGLAINDNLQDANQIQLYHGAPYIFTFGDVDKHNQQ
Protein: Superoxide dismutase [Fe] 3, chloroplastic (EC 1.15.1.1) (Protein FE SUPEROXIDE DISMUTASE 3) (Q9FMX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD2.
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000269|PubMed:18996978}.
Interaction partners:
- Superoxide dismutase 3
- Superoxide dismutase 1
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 2, chloroplastic
- Superoxide dismutase 1, chloroplastic
- Superoxide dismutase 1, mitochondrial
- Superoxide dismutase 2, mitochondrial
- Thioredoxin-like protein CITRX, chloroplastic
- Thioredoxin-like fold domain-containing protein MRL7, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
Sequence:
MSSCVVTTSCFYTISDSSIRLKSPKLLNLSNQQRRRSLRSRGGLKVEAYYGLKTPPYPLDALEPYMSRRTLEVHWGKHHRGYVDNLNKQLGKDDRLYGYTMEELIKATYNNGNPLPEFNNAAQVYNHDFFWESMQPGGGDTPQKGVLEQIDKDFGSFTNFREKFTNAALTQFGSGWVWLVLKREERRLEVVKTSNAINPLVWDDIPIICVDVWEHSYYLDYKNDRAKYINTFLNHLVSWNAAMSRMARAEAFVNLGEPNIPIA
Protein: Actin depolymerizing factor 1 (A8MR09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MVSSIFHLLSRSANAASGMAVHDDCKLRFLELKAKRTHRFIVYKIEEKQKQVVVEKVGQPIQTYEEFAACLPADECRYAIYDFDFVTAENCQKSKIFFIAWCPDIAKVRSKMIYASSKDRFKRELDGIQVELQATDPTEMDLDVFRSRAN
Protein: Uncharacterized ATP-dependent helicase C29A10.10c (EC 3.6.4.-) (O94387)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Rpb7-binding protein seb1
- Ribonuclease H
- Uncharacterized RNA-binding protein C3H8.09c
- DNA-directed RNA polymerase II subunit rpb1
- 5'-3' exoribonuclease 2
Sequence:
MENDEAFDRLIRKIQENQKHPSFEGSNKVLHLALSYLNTNRQNPHWVCDPKLQVAVRECLFLFSFQNDNEYLVWFKKHLNERLQLCPKCIVKYHQSLDDFKSLCLNIFHFDPNTLEIVMEKIYSWDIFRLQEVLKTVPKIDTSSASKPILCAFYEILYSPRILHNKEIFPLFRNRFLESGFLRLSKNLVPGVISLLFSRDDELRRWACSILSDVKTISDNEFKILEGPLLQEIRSLDQKKENENEMQIFLKGLSLLLKHVDHLYFRGLTGKNFNVADFILSGLQSDHTNLCPSFLVCLHSLLYCYGRNFWTPEISPSEVIDKIFNGNAYKRWTEENTSNFSNDQKAENPFEWATSLLKTISIIDEVELINKILINYTMQYKKELEVGFKNVQLLQSLADIFSVLFSEYFMIFPHSDQSLQNKVFELHSTLAIKFDELFRLLNLENEESVEWRLIKKVFEYRLNLDLYILKQFYCHYLDRNRKPPLNIKSVSESFKNFWVYLQNVFREEKFFMVRIVFRACSTVCLIDKLPPKKVDIPFKSDFENALNGFVATFSEMLIQTQCWHLSAQTQLVSNPLTFRGIFSLVFSPILEISTGSISIIKSISLSDSVVDTIGELLRSQFSNTLNSSCYVLLQWLKVRNFGGAKHIVYFNKLIINTIFDSVDGLTSKDATFAKQVEKKESLKNFWESLWKFFTHFFIVLPTWPVHDKDNLVDLMRDTLDFCDMLINIFEEVNGFIFGLSDNDIKIVSANDKGSALAMCIADSLVTVSYWLKLTDSSLLTSVVKVICKMLKICKKLECPISQNVIDIIHRASITSDEQTILTFTEREDLFISLTPYLSEDVLNHSPFNDTNTLETKLQSDDRGLLSKDQTIGIAKKLPESNISTSNHFLLPPKAISASKAINRNAQKSQNLNFLKSKQETTQRIRESAKVPRTSAGNHLSEKLNSDNHIPKALQKLDSADPIRKPSLLHTSKSYSNPDDKNTSTSDEDTSESEEESSNGLFSLAREANSHASKSLPQRRQIQFLDFDSLKTKNVVHPTQLRRNTQQSAQLARLRLNPDVQEFYKVILGWNPLADSFSASNVEMQCVQAKFTYNDSNAYEKVFKPMLFHECWAQVKSAVEEKQYPPIDLILNTRSTVDNFVDIYFTSCSPTEVSFLSDTDICLLSKSQSSGDTNNPKSFQLCKIQSISRKKESLELCLRMNIESIDLQEYAPNIRFTAQKLFNATTSLREFAALKSLRHLPLSQRILDANVTRLPSNFTDDKKQKIMKSYGVNEPQAYAIYASSVNDGFTLIQGPPGTGKTKTILGMIGAVLTSSSQGLQFNVPGQTRKTSKNKILICAPSNAAIDEILLRIKAGVYDHEGIKFFPKVIRVGFGDSISVHAKEFTLEEQMIKQMELTNLKKDQEANNSSDTRKKYDSIIKKRDSLREDLEKFRSTGKNSSILEAQLREITKQKNMLEQSLDDMRERQRSTNRNLDVLKKQIQNQLLQEADIVCATLSASGHELLLNAGLTFRTVIIDEAAQAVELSSIIPLKYGCESCVMVGDPNQLPPTVLSKTSAKFGYSQSLYVRMFKQHNESACLLSIQYRMNPEISRFPSKFFYNSKLLDGPNMSAVTSRPWHEDPQLGIYRFFNVHGTEAFSNSKSLYNVEEASFILLLYERLIQCYLNIDFEGKIGVVTPYRSQVQQLRSQFQRKYGSIIFKHLDIHTVDGFQGQEKDIIIFSCVRSSMSGGIGFLQDLRRLNVALTRAKSSLYIVGNSKPLMQEDIFYSLIEDAKTRGVWRDLSANQFKNSKSISNVSTHLASNNLNLASRDTPIKSPSVGICEEKQEAHKVKKRHNIDSANLSRGTERDEDIPNKRAKNKVSTDQTAADNKVTKPRLDESSSSKQDVLNKIDESEIEQASSKKPGYVEKNKDKGHMKKSKKPKSKLALAAMAHGFAPPKVEHFKRK
Protein: Hemocyanin A chain (P83173)
Organism: Cherax destructor (Common yabby crayfish)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
GVPGDVHDEQKQHDINFLLFKVYEVLXDIXLKXVA