wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase ATM (EC 2.7.11.1) (Q9N3Q4)
Organism: Caenorhabditis elegans
Function: Serine/threonine protein kinase which activates checkpoint signaling in the presence of DNA double strand breaks (DSBs) and other forms of DNA damage induced by ionizing radiation and other genotoxic stresses such as UV. Plays a role in maintaining genome stability.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13315}.
Interaction partners:
- Serine/threonine-protein kinase ATR
- Double-strand break repair protein mre-11
- Protein hsr-9
- Telomere length regulation protein clk-2
- Ku domain-containing protein
- ATP-dependent DNA helicase II subunit 2
- PAX-interacting protein 1
- ATP-dependent helicase wrn-1
- DNA repair protein RAD51 homolog
- Serine/threonine-protein kinase chk-2
Sequence:
MSVTQLKNLKHAIAQLLEWDGTKTARKKIVDEVVLLYHALGAEALSEDNQEIYDLYDLSARIFNLAKKEIEEANQQFEKERKKGTRRSEKPVPTPLFELSIQHLKRCCQQGIDHNQVPWIAYCLKLLEFPITITEKSIENEISNVLLLSSNASQLHWAEHAHLSSLWKWIWSRVETADIGALAMRNYMELAANLLENVDYVVFEKSPIDLMAKVMGTLKKSVEMGNPKEYWCHYRKFSVVHILSYIVHRWGLEARDFILREIFELTGSLSNLISVAHKDGEQSKKCIMRLIDDLVKLAMIETVHGHRTMNEVTRGNIQKLVKTGIQESLKSAHRNFSRSSTFSISEECVRYLTRWLLAERRLEQPSAAMNESFELTGDSSSKKKDDATFDSLIDLSFGSTISGKHKLNAWNGVMQILNELLKSRRLELQVTEKIVTILWEKRKSYTTEPLRTVFCSILSTVVCQADVRFGHRKVPTIDSILKYSLSLMPNVASLPSAAALTETIVRFRTVSREGLRNTWDTVSRTSSGSFEVVRLISALISVTEFDENSRFANDERVRSWSFRKDIIEWVLLDPNAHSHKLLYQLCQYHPTYCYESEASSSDDSLLQTLKLCKLACSPAPPSAPKALRPLEASIEEIVRYVHDKLKSILATEITLPAFVLCHEFALKYPDRSYEFNKMYKKLYQIMEDQEEDEFLQSARHFSKWPQNLTLPIQKQTINCMAVFFEANLDNQLVDLCQWSDRRKVLVEMLAELAATRSEIRDKLQKSMPFNKFVKECIMENRGDLYEMTKRFEKYSFLLSIRNLIVTRMIITNEAARLLGDGETISETDIFIIEKRTLSTCIRNVSEGKELSGYTLDPYTVAANVHNVHFDHINVEIYLELLKKSPFFAQNIVRHLLRQNGKEAEEETWHLHATVLKIVMKDEKLLAVCVATIPNMVRYLKVYQIHFSPKSNAAKFLHLDMESISHCQSYLRKPTKSSNLITAANFLTLFGCEKRTWKRPILRFWSIFKQQPAMCCEKLLIFAEECVELGLNHRIACLLRALTTSEFCRKALCDEYLKIAFQLTYRSIFLILSKNECRPEIVELCDDMNLRYDLLQHQIKHVAAHHLEHFERFETKIAFSVEKFLKSGIDGIDFEDLGLVEFYKQLNENLTEDAIRSNEARNIYIVDILSTIWLQLPSIRPQILPILARFKHISPAWTNFPQPPHISTNEKSFLQHLRFHLYLKMMNISKSMTQGEYATCIMMLLTSYDSSHFVADLIEKKQLGKLKLQQRRNVLCILSRLLKDQAVMGDEDETIIDPILFKAITKASAVFEDTAACIVPFLFKICVDFKGKYDKCVINLLGCLKGVNAEDEIVVRCLAECVDSIGLNVIARYERLNIETHSEFGVKWFFKLSRLFLKHGFTTHSFAIANILFDRLSARKRNTMMIDRTSLDRIDRSQELINLLVEIYVAEGNSVALSSLPPAVQNRPDVRQVMNKSSKEWLKLLSSNQMDSWELTIVQWMCGIQFNAITGDKYLNSILRCNFNEYTKKIDSPLKFVYFQLFHLSTSTLEIEEAISSMPLAPTIDQMRLMIIANATASFEPQSVEEHVVRAVRELRETSNRRKSGGNVKGINEKTTRMVKLAEMLTENKAYDAAINLLDTWEHECLQWTSVAAESIDIDLIRICKQHVTCRSGDPRMADINLRTMHPRVPVMSDLAIAEWSLALSKITIEYRNDMEEGIRILEFGCKHLQNKDSVETRLKVLLKLHSVCIGQLSKLEEYRETRTYRMKQQAVTAFEQQIQNSCRTSLARGNSGDEWTKKTVQRVRKEHQFEKNDLEKVDNSLNSAARKAVSSGFDALLCISQLEDDDEAIRASSLIIFPLIDVIYKYETDVGVIALLKEHTKSKLPSKLWISATSHIASKCFSIEKSQITRHLSQILCHLIYDYPYHVLHTILMYDDEKNASKVKGFLKTIFDARADQRDSSKLKEIVITIREAHQAYREIAMLDVRGNVRIQRVEINGKTMYRWPHDLKIFKCKLRQLPIPTISQKIGCPGDYSTTDLITWKRWKDVFTIADGISTPKIWEIEGSDGKWYKTVWKKDDVRQDVLVEQMFDVTNNMLEKAMLRTYNVVPLDTECGVIEFCGGTVSLKEVMCGVTREGGLHREFNSEEVSASKVSSMMRQVQTESTETRRQVFVEICQQYSPVFRHFFYTNFSTAQIWRQKIINYRQSLATWSIVCYIVGLGDRHASNILFDQKLCTFVHIDLGMILEYSKRTLPVPEQVPFRITRDVLDPILIEGIENGQLAEECTQIMEKLKENGKVILGVASALLRETMTNFREAEQAAGRPSYISEMAIGRLREKLRGTDDGVTAQSSNLQIRRLLREATSADNLSRMFCGWMPFL
Protein: Zinc finger MYND domain-containing protein 19 (Melanin-concentrating hormone receptor 1-interacting zinc finger protein) (MCH-R1-interacting zinc finger protein) (Q96E35)
Organism: Homo sapiens (Human)
Function: May be involved as a regulatory molecule in GPR24/MCH-R1 signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12208518}. Cell membrane {ECO:0000269|PubMed:12208518}; Peripheral membrane protein {ECO:0000269|PubMed:12208518}.
Interaction partners:
- E3 ubiquitin-protein transferase RMND5A
- Armadillo repeat-containing protein 8
- Protein FAM170A
- Deformed epidermal autoregulatory factor 1 homolog
- Melanin-concentrating hormone receptor 1
- Tubulin alpha-4A chain
- Tubulin beta chain
Sequence:
MTDFKLGIVRLGRVAGKTKYTLIDEQDIPLVESYSFEARMEVDADGNGAKIFAYAFDKNRGRGSGRLLHELLWERHRGGVAPGFQVVHLNAVTVDNRLDNLQLVPWGWRPKAEETSSKQREQSLYWLAIQQLPTDPIEEQFPVLNVTRYYNANGDVVEEEENSCTYYECHYPPCTVIEKQLREFNICGRCQVARYCGSQCQQKDWPAHKKHCRERKRPFQHELEPER
Protein: Small ribosomal subunit protein bS6m (28S ribosomal protein S6, mitochondrial) (MRP-S6) (S6mt) (P82932)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS10m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS7m
- Large ribosomal subunit protein bL20m
Sequence:
MPRYELALILKAMQRPETAATLKRTIEALMDRGAIVRDLENLGERALPYRISAHSQQHNRGGYFLVDFYAPTAAVESMVEHLSRDIDVIRGNIVKHPLTQELKECEGIVPVPLAEKLYSTKKRKK
Protein: Lysozyme RrrD (EC 3.2.1.17) (Endolysin) (Lysis protein) (Muramidase) (P78285)
Organism: Escherichia coli (strain K12)
Function: Essential for lysis of bacterial cell wall, by showing cell wall hydrolyzing activity. Exhibits lytic activity against E.coli and S.typhi cell wall substrate.
Interaction partners:
- Prophage lysis protein S homolog EssD
- Prophage Rz endopeptidase RzpD
- Prophage outer membrane lipoprotein RzoD
- Prophage outer membrane lipoprotein RzoR
- UPF0299 membrane protein YohJ
- Diaminopimelate decarboxylase
Sequence:
MPPSLRKAVAAAIGGGAIAIASVLITGPSGNDGLEGVSYIPYKDIVGVWTVCHGHTGKDIMLGKTYTKAECKALLNKDLATVARQINPYIKVDIPETTRGALYSFVYNVGAGNFRTSTLLRKINQGDIKGACDQLRRWTYAGGKQWKGLMTRREIEREVCLWGQQ
Protein: Migration and invasion enhancer 1 (HBV X-transactivated gene 4 protein) (HBV XAg-transactivated protein 4) (Protein C35) (Q9BRT3)
Organism: Homo sapiens (Human)
Function: Increases cell migration by inducing filopodia formation at the leading edge of migrating cells. Plays a role in regulation of apoptosis, possibly through control of CASP3. May be involved in a redox-related process.
Subcellular location: Cytoplasm, cytosol. Cell membrane; Lipid-anchor; Cytoplasmic side. Note=Concentrates at the leading edge of migrating cells. Localizes outside membrane raft regions.
Interaction partners:
- Thioredoxin reductase-like selenoprotein T
- GPI-specific phospholipase A2-like PGAP3
- Selenoprotein W
- Receptor tyrosine-protein kinase erbB-2
- StAR-related lipid transfer protein 3
- Growth factor receptor-bound protein 7
- DNA-directed RNA polymerase III subunit RPC6
Sequence:
MSGEPGQTSVAPPPEEVEPGSGVRIVVEYCEPCGFEATYLELASAVKEQYPGIEIESRLGGTGAFEIEINGQLVFSKLENGGFPYEKDLIEAIRRASNGETLEKITNSRPPCVIL
Protein: Putative glutathione-independent glyoxalase hsp3105 (EC 4.2.1.130) (Glyoxalase 3 homolog 5) (Heat shock protein 31 homolog 5) (Q09918)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May catalyze 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}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable hydroxyacylglutathione hydrolase SPCC13B11.03c
- Glutathione-independent glyoxalase DJ-1
- Probable hydroxyacylglutathione hydrolase glo2
- Lactoylglutathione lyase
- 2-hydroxyacid dehydrogenase homolog 2
- Putative D-lactate dehydrogenase C713.03, mitochondrial
- Copper amine oxidase-like protein cao2
- Threonine dehydratase, mitochondrial
- D-serine dehydratase
- Tryptophan synthase
Sequence:
MDERHEAAGETSEKPKVLFLLNSYYGPFYDDGDNTGVNVVDLYEAFKVFEENGFDIVIASDTGDYGFDDKSFRDPAIVDETQSIFSNPDCSLMKKLKNIARLDRLNPSDYVIVYIPGGYGCSFDFPHAKVVQDFLYRFYETKGIICAVAQANIALAYTTNSDGQALCTNRRVTGCTWKDEVQNGVLNVMNRLNFYSFGHIAENIGAIFESPPVYVEDPFIVEDGQLFTGSNTNSAKGVAMEAVRAVLNYDG
Protein: DDB1- and CUL4-associated factor 11 homolog (WD repeat-containing protein 23) (P90794)
Organism: Caenorhabditis elegans
Function: Involved in regulation of lifespan. Required for dopaminergic CEP neuron degeneration in response to Mn(2+). Inhibits the skn-1-mediated up-regulation of tatn-1.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4
- Protein skinhead-1
- F-box domain-containing protein
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- Glycogen synthase kinase-3
- Uncharacterized WD repeat-containing protein F47D12.9
- DDB1- and CUL4-associated factor homolog 1
- RING-box protein 1
Sequence:
MGNWITSTFLRFDLFQRHQPNRFLEYTRVQHSNQSPAYSVRTAAEIVAHQRMKPNHSNDSDTDFSSDDEGCPKMTPHEEQQMFEREQHIAFSGRCHIGDPESCTQLRNEINSRCGPRPSTSNNMEFILNRDLQKRGTSISNPRTVARVLNSHLPNQKRRVDRVATKSFCTQYIQNGTKIVVASQDEKIRFYQRNPDKSKYRSKYMKSDELRVDQCGWSILDTAISLNGDLIAYGTWKDAVFVGKLDFTERQNITWFPIDLNGEPGRDHCAVFCVKFSDSSEQIVCGTSQYSIHVFDVEQRRRIRTIVNAHEDDVNSVCFADLGSNLIYSAGDDGLVKVWDKRAWSDGDVEPVGVFAGHRDGVTHVDSRQDERYLLSNSKDQTIKVWDLRKFSNMSGVEATRACVQSQHWDYRWQPAPPGLCQPVAGDTSVMTLRGHSVLHTLVRANFSPESTGRRYIYTGCARGEVVVYDIMSGTVSRRLKGHTAVVRECDWHPTENEIVSSAWDGVTTVWTWDERQEGVIAPYDHPNISQFGDEDSCDELFQPVKKQCRRQRKTMSSRGHPCSSSSISQN
Protein: Protein transport protein Sec61 subunit gamma (Q19967)
Organism: Caenorhabditis elegans
Function: Required for oocyte development and ovulation. Required for the translocation of secretory and transmembrane proteins into the endoplasmic reticulum in vitro.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Translocon Sec61/SecY plug domain-containing protein
- Protein transport protein Sec61 subunit beta
- J domain-containing protein
- Ubiquitin-like domain-containing protein
- Germinal center kinase 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Translocation protein SEC62
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Large ribosomal subunit protein eL31
Sequence:
MDQFQALIEPARQFSKDSYRLVKRCTKPDRKEYQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGA
Protein: Sterol O-acyltransferase 2 (EC 2.3.1.-) (Sterol-ester synthase 2) (P53629)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sterol O-acyltransferase that catalyzes the formation of stery esters.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10672016}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Sterol O-acyltransferase 1
- Phosphatidic acid phosphohydrolase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Lipid phosphate phosphatase 1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 3
- Sterol esterase 1
- Sterol esterase 2
Sequence:
MDKKKDLLENEQFLRIQKLNAADAGKRQSITVDDEGELYGLDTSGNSPANEHTATTITQNHSVVASNGDVAFIPGTATEGNTEIVTEEVIETDDNMFKTHVKTLSSKEKARYRQGSSNFISYFDDMSFEHRPSILDGSVNEPFKTKFVGPTLEKEIRRREKELMAMRKNLHHRKSSPDAVDSVGKNDGAAPTTVPTAATSETVVTVETTIISSNFSGLYVAFWMAIAFGAVKALIDYYYQHNGSFKDSEILKFMTTNLFTVASVDLLMYLSTYFVVGIQYLCKWGVLKWGTTGWIFTSIYEFLFVIFYMYLTENILKLHWLSKIFLFLHSLVLLMKMHSFAFYNGYLWGIKEELQFSKSALAKYKDSINDPKVIGALEKSCEFCSFELSSQSLSDQTQKFPNNISAKSFFWFTMFPTLIYQIEYPRTKEIRWSYVLEKICAIFGTIFLMMIDAQILMYPVAMRALAVRNSEWTGILDRLLKWVGLLVDIVPGFIVMYILDFYLIWDAILNCVAELTRFGDRYFYGDWWNCVSWADFSRIWNIPVHKFLLRHVYHSSMSSFKLNKSQATLMTFFLSSVVHELAMYVIFKKLRFYLFFFQMLQMPLVALTNTKFMRNRTIIGNVIFWLGICMGPSVMCTLYLTF
Protein: Protein C42 (C42) (P40) (P25695)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Plays a role in host nuclear actin polymerization by recruiting p78/73 protein that is capable of activating an actin-related protein 2/3 complex to initiate nuclear actin polymerization.
Subcellular location: Host nucleus {ECO:0000269|PubMed:11711623}. Virion {ECO:0000269|PubMed:11711623}.
Interaction partners:
Sequence:
MSAIALYLEINKLRLKIDEPMQLAIWPQLFPLLCDEHQSVQLNTDVLINFMMHVARKSQNTILNNNAAIASQYAAGNADVVAAPASAQPTPRPVINLFARANAAAPAQPSEELINMRRYRNAARKLIHHYSLNSTSSTEYKISDVVMTMIFLLRSEKYHSLFKLLETTFDDYTCRPQMTQVQTDTLLDAVRSLLEMPSTTIDLTTVDIMRSSFARCFNSPIMRYAKIVLLQNVALQRDKRTTLEELLIERGEKIQMLQPQQYINSGTEIPFCDDAEFLNRLLKHIDPYPLSRMYYNAANTMFYTTMENYAVSNCKFNIEDYNNIFKVMENIRKHSNKNSNDQDELNIYLGVQSSNAKRKKY
Protein: Regulator of microtubule dynamics protein 3 (Protein FAM82A2) (Protein FAM82C) (H0YMB1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004572}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
XESEDGEDEVSCETVKMGRKDSLDLEEEAASGASSALEAGGSSGLEDVLPLLQQADELHRGDEQGKREGFQLLLNNKLVGVGEGQGPHSPQLRKKGPHPFLSGLQYGSRQDFLWRLARAYSDMCELTEEVSEKKSYALDGKEEAEAALEKGDESADCHLWYAVLCGQLAEHESIQRRIQSGFSFKEHVDKAIALQPENPMAHFLLGRWCYQVSHLSWLEKKTATALLESPLSATVEDALQSFLKAEELQPGFSKAGRVYISKCYRELGKNSEARWWMKLALELPDVTKEDLAIQKDLEELEVILRD
Protein: Focal adhesion kinase 1 (EC 2.7.10.2) (Protein-tyrosine kinase 2) (pp125FAK) (H0YBP1)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000256|ARBA:ARBA00004120}.
Interaction partners:
Sequence:
XYDRYLASSKIMAAAYLDPNLNHTPNSSTKTHLGTGMERSPGAMERVLKVFHYFESNSEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQEIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFTQVQTIQYSNSEDKDRKGMLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQKEGERALPSIPKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSPQHMVQTNHYQDSTVLDLRGIGQVLPTHLMEERLIRQQQEMEEDQRWLEKEERFLKPDVRLSRGSIDREDGSLQGPIGNQHIYQPVGKPDPAAPPKKPPRPGAPGHLGSLASLSSPADSYNEGVKLQPQEISPPPTANLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLGELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKMLGQTRPH
Protein: Synaptophysin (F1N548)
Organism: Bos taurus (Bovine)
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000256|ARBA:ARBA00004644}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004644}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MLLLADMDVVNQLVAGGQFRVVKEPLGFVKVLQWVFAIFAFATCGSYSGEFQLSVDCANKTKSDLNIEVEFEYPFRLHEVYFEAPTCQGDPKKIFLVGNYSSSAEFFVTVAVFAFLYSMGALATYIFLQNKYRENNKGPMLDFLATAVFAFMWLVSSSAWAKGLSDVKMATDPENIIKGMHVCHQPGNTCKELRDPVTSGLNTSVVFGFLNLVLWVGNLWFVFKETGWAAPFLRAPPGAPEKQPAPGDAYGEAGYGQGPGGYGPQDSYGPQGGYQPDYGQPASSGGGGYGPQGDYGQQGYGPQGAPTSFSNQM
Protein: Hypothetical lipoprotein (E7DNA8)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Interaction partners:
Sequence:
MATLKALSTLIVSGAVVHSGSVFSCPEALASSLIERNFAFEIKAAEDGETVETVPQTIESVEEIDEVEQMREEYAAKTVPELVELARANGIDISSISRKSEYIDALIKYELGE
Protein: NCL protein (Q9BQ02)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE
Protein: DEAD-box ATP-dependent RNA helicase 32 (EC 3.6.4.13) (Q9FFT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-rRNA-processing ESF1-like protein
- MIF4G domain-containing protein / MA3 domain-containing protein
- At3g56510 family protein)
- rRNA biogenesis protein RRP36
- Nucleolar protein
- U3 small nucleolar RNA-associated protein 18 homolog
- U3 ribonucleoprotein
- At3g53440
- U3 ribonucleoprotein
- U3 small nucleolar RNA-associated protein
Sequence:
MVKIKKTKGMRKQIRLNEVEEINLLKQWIESQKPDSGFNPLSLRPLPKDSKIGKSEDGKNGTVFSRYAGVRKFAQLPISDKTKRGLKDAKYVDMTDVQSAAIPHALCGRDILGAARTGSGKTLAFVIPILEKLHRERWSPEDGVGCIIISPTRELAAQTFGVLNKVGKFHKFSAGLLIGGREGVDVEKERVHEMNILVCAPGRLLQHMDETPNFECPQLQILILDEADRVLDSAFKGQLDPIISQLPKHRQTLLFSATQTKKVKDLARLSLRDPEYISVHAEAVTATPTSLMQTVMIVPVEKKLDMLWSFIKTHLNSRILVFLSTKKQVKFVHEAFNKLRPGIPLKSLHGKMSQEKRMGVYSQFIERQSVLFCTDVLARGLDFDKAVDWVVQVDCPEDVASYIHRVGRTARFYTQGKSLLFLTPSEEKMIEKLQEAKVPIKLIKANNQKLQEVSRLLAALLVKYPDLQGVAQRAFITYLRSIHKRRDKEIFDVSKLSIENFSASLGLPMTPRIRFTNLKTKKKGVYESSIAMEIENAQEYEAPLVVKKDLLGEDLEEEDFALKPRKEGKVVEKSTKEEEVLIPGNRVLKNKKLKINLHRPFGSRVVLDEEGNSLAPLASVAAEAGTEVALDEERMNDYYKKVGAEMRKADIEDKKVDKERRREKRMKQKIKRKRGAMEDEEEEEEEDHDGSGSSDDETGRNSKRAKKIVSDNEENGGKINTDSLSVADLEEMALKFITQ
Protein: Amyloid-beta A4 precursor protein-binding family B member 3 (Protein Fe65-like 2) (Fe65L2) (O35827)
Organism: Rattus norvegicus (Rat)
Function: May modulate the internalization of amyloid-beta precursor protein.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O95704}. Nucleus {ECO:0000250|UniProtKB:O95704}.
Interaction partners:
- Amyloid-beta precursor protein
- LIM and calponin homology domains 1
- Thymocyte nuclear protein 1
- Plakophilin 4
- Family with sequence similarity 193, member B
- WD repeat-containing protein 55
Sequence:
MLGKDYMLAIILVNCDDDLWGDQNLEGETGLPPGWRKIRDAAGTYYWHVPSGSTQWQRPTWELAEDPGTGKEGIWELRPPKGRSFSSLDSSLNRSNSLTWYNEDSYVRSLEPGAKCFAVRSLGWVEVPEEDLAPGKSSIAVNNCIQQLAQARNRSQPHDGAWGEGQNMLMVLKKDAMSLLNPLDHSLIHCQPLVHIRVWGVGSSKGRDRDFAFVAGDKDSCMLKCHVFRCDVPAKAIASRLQGLCAQILSERVGLSGEAACCSPDPISPEDFPRQVELLDAVSQAAQKYEALYMGILPVTKAMGMDVLNEAIGTLTGRGDRKTWVPAMLSVSDSLMTAHPIQAEAGAEEEPLWQCPVRLVTFIGVGHDPHTFGLIADLGCQSFQCAAFWCQPHAGGLSEAVQAACMVQYQKCLVASAARGKAWGAQARARLRLKRTSSMDSPGGPLPPPLLKGGVGGAGAAPRKRGVFSFLDAFRLKPLFSICPKLILEGWGKRLYTLPVPRVL
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUR1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome M complete sequence
- ABC multidrug transporter SNQ2
Sequence:
MSLADYFTPVPNASVTFEGTTVNLNETATGSAHSHAEDPEFGEKLPLPSVSPCENGQVVDLTFQATAGEMVLVLGAPTSGIFKSLFHAHKHLSYSPQGSIRFKDNEFKAYSSKSPHQIIYNNEQDVHFPFLTVNQTVDFALSCKFDIPKEERENMRNELLREFGLSHVGDTIVGNDYFRGVSGGERKRISIIETFIANGSVYLWDNSTKGLDSSTALDFLTILQKMARTTRSVNLVRISQASDKIVEKFDKILMLSDSYQVFYGTVDECLHHFRDNLGIKKDPNDCIIEYLTSILNFQFRTKSLDITGSSEDLDLKDTDHNEQTFSGIASSLCSEVDLYTQWKKSSYYQDIKEQIGAFNVENKADGNHINPEDVTKTFDIPLKKQILYCTKRAFQRSLGDKAYMISQVISVIIQSLVIGSLFYDIPMTTIGSFSRGSLTFFSILFFTFLSLADMPIAFQRQAVVKKQTLLHFYFNSVETLATTLFDYCFKFCLVVIFTIILYFLAHLQYNAARFFIFLLFLSVYNFCMVSLFSLTTMFTPTISLANLFAGILLLAIAMYASYVIYMKDMHPWFVWIAYLNPAMYAMESILANEMFNLKLDCTESVVPRGPTYQNVPVTNKACAWQGATLGNDYVRGKDYLKNGLSYKYSHVWRNFGILIGFLCFFIAMNLFASEYIKPLFYNDGPEAVQHFINRWFRRSATHSTTSSSSPENIKLKEDVVVKSASLSSTSSLSSSETAKSNPFADKTVQAQKHVISWKNINYTVGGDKRLINNVSGYIGSGLTALMGESGAGKTTLLNVLSQRTESGVVSGEILIDGKPLTNENAFRRSIGFVQQQDIHLELLTVKESLEISSELRGDGDMEYVESISELLKLPLDSLVRELNPTQRKLLSIGVELVTKPSLLLFLDEPTSGLDAEAALTIVQFLKKLSLQGQAIFCTIHQPSKSVISYFDNIYLLKRGGECVYFGPTSEACGYFMSYDKSLTYDPESDNPADFVIDVVGNNESMEEMDDKADFAIREENPWSTRWENSHERKNIDETVVRLEQEAAASGVDFTTAVWEQPSYMKQLIMITKRQYTCTRRDRSYIAAKYLLNGGAGLFIGFSFWKIKHTISGLQDTIFFCFMALCVSSPLINQVQDKALQSKEVFIARESRSNTYHWTCLLLAQFIIELPLAMSSSTLFFVCAFFCCGFDNSGKVAGVFYLNYILFSAYYLTLGLWLIYTAPNLQTAAVFVAFIYSFTASFCGVMQPYALFPGFWKFMYRVSPYTYFVDTFVSTLLHNRKVICNTGEMVPGQPTGGKTCGQFFKAYIDEYGGWLKNPNTFTVCAYCTYDTGDDFLKQQNMSHSHIWRNYGIEWAFVAFNFFAMFAGYYLTYVAKVWPKVFKFIMKLIPTGIKSRASKD
Protein: Ras-related protein Rab-14 (EC 3.6.5.2) (Q91V41)
Organism: Mus musculus (Mouse)
Function: Regulates, together with its guanine nucleotide exchange factor, DENND6A, the specific endocytic transport of ADAM10, N-cadherin/CDH2 shedding and cell-cell adhesion (By similarity). Involved in membrane trafficking between the Golgi complex and endosomes during early embryonic development. Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. May act by modulating the kinesin KIF16B-cargo association to endosomes (By similarity).
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:P61106}. Early endosome membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000250|UniProtKB:P61106}; Cytoplasmic side {ECO:0000250|UniProtKB:P61106}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000250|UniProtKB:P61106}; Cytoplasmic side {ECO:0000250|UniProtKB:P61106}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P61106}; Lipid-anchor {ECO:0000250|UniProtKB:P61106}; Cytoplasmic side {ECO:0000250|UniProtKB:P61106}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P61106}. Note=Recruited to recycling endosomes by DENND6A. {ECO:0000250|UniProtKB:P61106}.
Interaction partners:
- TBC1 domain family member 1
- Solute carrier family 2, facilitated glucose transporter member 4
- Rab GDP dissociation inhibitor beta
- Ras-related protein Rab-5A
Sequence:
MATAPYNYSYIFKYIIIGDMGVGKSCLLHQFTEKKFMADCPHTIGVEFGTRIIEVSGQKIKLQIWDTAGQERFRAVTRSYYRGAAGALMVYDITRRSTYNHLSSWLTDARNLTNPNTVIILIGNKADLEAQRDVTYEEAKQFAEENGLLFLEASAKTGENVEDAFLEAAKKIYQNIQDGSLDLNAAESGVQHKPSAPQGGRLTSEPQPQREGCGC
Protein: Chromosome 17 open reading frame 49 (F8W038)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSASTKVGEIFSAAGAAFTKLGELTMQLHPVADSSPAGAKWTETEIEMLRAAVKRFGDDLNHISCVIKERTVAQIKATVKRKVYEDSGIPLPAESPKKGPKKVASGVLSPPPAAPPPSSSSVPEAGGPPIKKQKADSLTLDSGLLMTSADPPLLSC
Protein: Proteasome subunit alpha type-2-B (20S proteasome alpha subunit B-2) (Q8L4A7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-6
- Proteasome subunit beta type-2-B
- Proteasome subunit beta type-4
- Proteasome subunit beta type-3-A
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-1
- Proteasome subunit beta type-3-B
- Proteasome subunit alpha type-1-A
- Proteasome subunit alpha type-7-A
- Proteasome subunit alpha type-5-B
Sequence:
MGDSQYSFSLTTFSPSGKLVQIEHALTAVGSGQTSLGIKASNGVVIATEKKLPSILVDEASVQKIQHLTPNIGTVYSGMGPDFRVLVRKSRKQAEQYLRLYKEPIPVTQLVRETATVMQEFTQSGGVRPFGVSLLVAGYDDKGPQLYQVDPSGSYFSWKASAMGKNVSNAKTFLEKRYTEDMELDDAIHTAILTLKEGFEGEISSKNIEIGKIGTDKVFRVLTPAEIDDYLAEVE