wanglab/gogpt-training-data huggingface dataset:
Protein: Histone H3.v1 (Q54F38)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Histone H3.v2
- Small ribosomal subunit protein eS30
- Histone H2B.v3
Sequence:
MANKPKPSEHLRDLIRSGQRTSPEADLQLKQQQQPRQTQPSRPSSSLTQSYEPPGTTRVPVSPVISTSESSGSSRSPASSGSSRSSGSSGSSRLSGSSRASVNTIMNLSNIEFNDTPSVTDDSYYTNVMTESPIRKAASQRLPTGVMDSIRGSLENINVSHNLTPTTPLSKPNTLMYKKGAPAPPRLTPILPSYKTNLKPVVQTPKIQRKTSQIEEESDDDSSSQNNSSDQEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEEVREAPKRSGGKPLPSPSLSSIFSNYDESSSVASSESSKQSRVKVSKKPSPLIKKKPAPIKKVTTPTRSKQQQQSPLPPTRRSPLPSEAKKPAASKKVSKNVLSSSSSSPSSSSSSSSSLTPTKSRRETIVTTPTKTPPSTRSKSITPLSTPTRTPPSTRSKTSSTPSSTPSSLSISTPSSTSISSPVSSRTSTSILTPPSTPTSTHSSTSASITTPTTPRIRVQRTTTTPTTPTTPRKKRRRRLVASVIRRLRNSVDFMIPRLPLSRLVREIMCLFDDGLRITPGALLAIQTTTEAYLTRLMEDSGLLASHAGRKTIRSVDMYAWKRARHFLF
Protein: DNA-binding protein eta2 (O14108)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MMLAIDMTINENQGTRSNLESPTLSCSSKGAMQERDVMFTDHNTFNITNNKSRPGSLMKSMKRKDVYEFDEDNEFEFEMGSLIHKPSRAHSLGGTSEPVSDDHKDCMEATRQLLENSPLSSVVVKTCSDHASKRKIARSSSDDSESKVESTNSFNAKKRKDAWTEEHEKWFQARIDELLTIRSISREQMIEILEDEHAGSRLQGFLESVASFLNRKENSLLKYMRAFFQVAGYEKIDIGSLAAEEDSQLNFSLEDAQVIQKVVLSYCNNEGVDLQEFGFRMSSSSLRHTNINFLYNELRELLPTSISRKGIIRYLKEIYKPLDPKDRNAWEESELKKLYTLVEQEGTRWNSIANKLGTSPAACMSQWRFVVGTSTQETIDRRKLWTNEEEAKLLDLVKSSYRSSFHTKKMTSLFTHNNHTTSNIQREIPASDSIAWHSISKKLGTKSPESCRKQYEKTIASYSSNQRQEEDQGKKRKKRKKKKSKGKRKFYVADSLKLLEHVQRQCGEAISINAIDWKGIVKQMPKWSEEELRAQATNLVASVRGWKKTRLSESVRIAITDLKSLPPDV
Protein: N-acetyltransferase aca1 (EC 2.3.1.271) ((S)-1-pyrroline-5-carboxylate acetyltransferase) (L-azetidine-2-carboxylate acetyltransferase) (AZC acetyltransferase) (Q09927)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: N-acetyltransferase involved in oxidative stress resistance. Acetylates the toxic proline metabolism intermediate (S)-1-pyrroline-5-carboxylate (P5C), or more likely its spontaneously forming tautomer glutamate-5-semialdehyde (GSA) into N-acetyl-GSA for arginine synthesis in the mitochondria. P5C has been shown to increase the levels of reactive oxigen species (ROS) in the cell by inhibiting the function of the respiratory chain in the mitochondria. The enzyme is able to reduce intracellular ROS levels under P5C-induced oxidative stress and protects cells from damage by oxidative stress (By similarity). Also acetylates and thereby detoxifies the proline analog azetidine-2-carboxylate (AZC), however it is unlikely that AZC is a natural substrate as it occurs only in plants belonging to the Lilaceae family.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000250|UniProtKB:E9P8D2}.
Interaction partners:
- Multistep phosphorelay regulator 1
Sequence:
MKDPNTIPPWRCTDFNAWCIAVDKSTNVKNKEELLSTLTYFINYEIEMGQTYPIDIKMTRNEAEDFFFKFCTVICVPVESETSPAPDLATASIDWKTSLLGAFYIKPNYPGRCSHICNGGFLVSPSHRSKGIGRNLANAYLYFAPRIGFKSSVFNLVFATNIKSIRLWERLNFTRAGIIKDAGRLKGHEGYVDAYIYQYHFPSLEDALK
Protein: Structural maintenance of chromosomes protein (Q8AWB7)
Organism: Gallus gallus (Chicken)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR005719}.
Interaction partners:
Sequence:
MGYLKLIEIENFKSYKGRQIIGPFRRFTAIIVPNGSGKSNLMDAISFVLGEKTSNLRVKALRDLIHGAPVGKPASNRACVSMVYAQDCGTERTFARLIVGSSSEYKINNRVVQLSEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEAEIEKLNKELGLKNREIDKDKKRMDRVEDELKDRKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTAHKIKKVEAARKALQNAQKQYKKRKADMDELEKEMGAVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQERLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYIATSKQSLEEQKRLEGELTAEVESAKRRIDEINQELNQVMEQLGDARIDRQESSRQQRKAEIMDSIKRLYPGSVYGRLIELCQPTQKKYQIAVTKVLGKNLDAFIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNMQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDYEKNQLKEDQDKVHMWEQTVKKDEAEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMDEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEEGSGGGEEGVSGSQRSSSLYAREALIEIDYSDLPEELKAAAPAEEEIKQEMNTLQQKLNERQSILQRISAPNMKAVEKLESVRDKFQETSEDFEAARKEAKKAKQAFEQVKKERFDRFNACFESVATNIDEIYKALSRNSSAQAFLGPENPEEPYLDGINYNCVAPGKRFRPMDNLSGGEKTVAALALLFAIHSYKPAPFFVLDEIDAALDNTNIGKVANYIKEQSTQNFQAIVISLKEEFYTKAESLIGVYPEQGDCVISKVLTFDLTKYPDANPNPNEQ
Protein: ImpB/MucB/SamB family protein (A0A0H2WVY6)
Organism: Staphylococcus aureus (strain COL)
Interaction partners:
Sequence:
MYNYHLLEDRDVLCIDQKSFFASVSCIEKGLDPLETKLAVVADTKRQGSVILAATPKLKELGIKTGSRLFEIPHRNDIYIINPSMRKYLNVSVAISKIALRYIPPEDLHQYSIDEFFMDVTDSYHRFSSTVHAFCERLKREIYEETGIYCTVGIGSNMLLSKIAMDVEAKHSQNGIAEWRYQDVPTKLWPIQPLRDFWGINRRTEAKLNKRGIFTIGDLAKYPYKFLKKEFGILGVDMHLHANGIDQSKVREKHKISNPSICKSQILMRDYHFDEAKVVMQELIEDVASRVRARKKVARTIHFAFGYSDEGGVHKQYTLKDPTNLEKDIYKVVMHFADKLCNKQALYRTLSISLSQFINEDERQLSLFEDEYQRKRDECLAKTIDQLHLKYGKGIVSKAVSFTEAGTKHGRLGLMAGHKM
Protein: Zn(2+) transporter (A0A1D8PGL8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Low-affinity Zn
- Zinc-regulated transporter 1
- Zn
- Cation efflux protein cytoplasmic domain-containing protein
- Mitochondrial metal transporter
- Cu
Sequence:
MNSKEIRIVALLILDTVFFLLEAIIGYTVHSLALIADSFHMLNDIISLIIALWAVRVKNTKPADGKYTYGWQRAEILGALINAVFLLALCFTIIMDSIQRFFEPQEISNPKLILIVGIAGLVSNGVGLVLFHEHGHSHSHGGGGGGGSDHSGDSKSHSHSHSHSHGEATTFSQGDEEEHIGTEENEHTPLLYNITHTTMKSTPSEVFDYLPDNVVERYSNYQPSFSGQSPLNGTSANSSDANTVVNNNNTSDHSGTNNNTPQSALQKIKQKSMNMEGVFLHVLGDALGNIGVIITALVIWKTDYSWRFLADPITSLFITLIILNSALPLVRKASRILLQSAPPYIDSNLIVNQIKQLPLIKNIHDFHVWNLNEDILIASLHIELNPNCEVNLPLPLPSNGGDNNNNNTKNGSNGDSSIDEEQDQDQELELEEAPSQIDRKLFLAAVGQVREVLHIYGINSVTIQPEFSNSKKVCRSIF
Protein: Carboxypeptidase B2 (EC 3.4.17.20) (Carboxypeptidase U) (CPU) (Plasma carboxypeptidase B) (pCPB) (Thrombin-activable fibrinolysis inhibitor) (TAFI) (Q96IY4)
Organism: Homo sapiens (Human)
Function: Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin.
Subcellular location: Secreted.
Interaction partners:
- Prothrombin
- Plasminogen
- Thrombomodulin
- Carboxypeptidase B
- Tissue-type plasminogen activator
- Alpha-2-antiplasmin
- Complement C5
- Carboxypeptidase E
- Pigment epithelium-derived factor
- Carboxypeptidase N catalytic chain
Sequence:
MKLCSLAVLVPIVLFCEQHVFAFQSGQVLAALPRTSRQVQVLQNLTTTYEIVLWQPVTADLIVKKKQVHFFVNASDVDNVKAHLNVSGIPCSVLLADVEDLIQQQISNDTVSPRASASYYEQYHSLNEIYSWIEFITERHPDMLTKIHIGSSFEKYPLYVLKVSGKEQAAKNAIWIDCGIHAREWISPAFCLWFIGHITQFYGIIGQYTNLLRLVDFYVMPVVNVDGYDYSWKKNRMWRKNRSFYANNHCIGTDLNRNFASKHWCEEGASSSSCSETYCGLYPESEPEVKAVASFLRRNINQIKAYISMHSYSQHIVFPYSYTRSKSKDHEELSLVASEAVRAIEKISKNTRYTHGHGSETLYLAPGGGDDWIYDLGIKYSFTIELRDTGTYGFLLPERYIKPTCREAFAAVSKIAWHVIRNV
Protein: Supercoiling factor variant B (Supercoiling factor, isoform B) (Q8IRH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQTVYGFMDDLSPDEKEQEENGVSYKSLLKRDRYRWSVADQDLDDNLTKDEFTAFLHPEDHPSMKGVVLRETITDLDKDHDGKISVDEYIGDMYRSTGAEDEEPEWVANEREAFSTHRDLDKDGYLNEEEVKQWIAPHDFDHSEAEAKHLLFEADADHDDKLTKEEILDKYDVFVGSQATDFGEALARHDEF
Protein: Apoptotic chromatin condensation inducer in the nucleus (Acinus) (Q9UKV3)
Organism: Homo sapiens (Human)
Function: Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells.
Subcellular location: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.
Interaction partners:
- Histone deacetylase complex subunit SAP18
- RNA-binding protein with serine-rich domain 1
- Pinin
- Eukaryotic initiation factor 4A-III
- Protein mago nashi homolog
- Serine/arginine repetitive matrix protein 2
- THO complex subunit 4
- Serine/arginine repetitive matrix protein 1
- Caspase-3
- Pre-mRNA-processing factor 40 homolog A
Sequence:
MWRRKHPRTSGGTRGVLSGNRGVEYGSGRGHLGTFEGRWRKLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEEASAESEDEMIHPEGVASLLPPDFQSSLERPELELSRHSPRKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEASSPPPHPQLHSEEEIEPMEGPAPAVLIQLSPPNTDADTRELLVSQHTVQLVGGLSPLSSPSDTKAESPAEKVPEESVLPLVQKSTLADYSAQKDLEPESDRSAQPLPLKIEELALAKGITEECLKQPSLEQKEGRRASHTLLPSHRLKQSADSSSSRSSSSSSSSSRSRSRSPDSSGSRSHSPLRSKQRDVAQARTHANPRGRPKMGSRSTSESRSRSRSRSRSASSNSRKSLSPGVSRDSSTSYTETKDPSSGQEVATPPVPQLQVCEPKERTSTSSSSVQARRLSQPESAEKHVTQRLQPERGSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTVEEKEEVTMDTSENRPENDVPEPPMPIADQVSNDDRPEGSVEDEEKKESSLPKSFKRKISVVSATKGVPAGNSDTEGGQPGRKRRWGASTATTQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISEDETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEEKEPEAEPPVPPQVSVEVALPPPAEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQDELDYHRGLLVDRPSETKTEEQGIPRPLHPPPPPPVQPPQHPRAEQREQERAVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKEKAQEEPPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQKEAERAERAKEREKRRKEQEEEEQKEREKEAERERNRQLEREKRREHSRERDRERERERERDRGDRDRDRERDRERGRERDRRDTKRHSRSRSRSTPVRDRGGRR
Protein: Prefoldin subunit 4 (ABI3-interacting protein 3) (Gene involved in microtubule biogenesis 3) (Q9M4B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8, especially in cold conditions. Required for microtubules (MTs) (MTs) organization and dynamicity. Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus. Prevents cold acclimation (e.g. 7 days at 4 degrees Celsius) in a DELLA proteins-dependent manner by promoting nuclear proteasome-mediated HY5 degradation, thus modulating the expression of several genes and reducing anthocyanin biosynthesis, but seems not involved in constitutive freezing tolerance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:28412546}. Nucleus {ECO:0000269|PubMed:28412546}. Note=In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (PubMed:28412546). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (PubMed:28412546). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity). {ECO:0000250|UniProtKB:P57742, ECO:0000269|PubMed:28412546}.
Interaction partners:
- Prefoldin subunit 2
- Prefoldin subunit 6
- Prefoldin subunit 1
- Prefoldin subunit 5
- Prefoldin subunit 3
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
Sequence:
MQQQGSKSGSEMEVTWEDQQNINIFSRLNNRVHDLDDDIKSAKEKCENLEDAGNELILADEEMVRFQIGEVFAHVPRDDVETKIEEMKEATCKSLEKLEQEKESIVTQMAALKKVLYAKFKDSINLEED
Protein: Nucleolar MIF4G domain-containing protein 1 (SGD1 homolog) (Q5C9Z4)
Organism: Homo sapiens (Human)
Function: Plays a role in targeting PPP1CA to the nucleolus.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15715967, ECO:0000269|PubMed:17965019}.
Interaction partners:
- Eukaryotic initiation factor 4A-III
- Probable ATP-dependent RNA helicase DDX10
- Something about silencing protein 10
- WD repeat-containing protein 3
- KRR1 small subunit processome component homolog
- Neuroguidin
- Ribosomal RNA processing protein 36 homolog
- RNA cytidine acetyltransferase
- ESF1 homolog
- U3 small nucleolar RNA-interacting protein 2
Sequence:
MAASRSAGEAGPGGSQGRVVRMKRRGGRGPRRGPAGGGEKALKRLKLAVEEFVHATSEGEAPGGCEGRGAPVSFRPGGRKSRKELRKEKRHLRKARRLQRTAGPEQGPGLGGRSGAEEASGHRQDTEERARPAPSRDPSPPRKPRPSRVKAKATAATAKTRPSAAATAAARKRALLAANEEEDREIRKLERCLGLNKRKKKDGSSSVPLSFARDGLDYILGALESGKNSGLYDSSGEEEEDAGQTLPESDLESDSQDESEEEEEGDVEKEKKAQEAEAQSEDDDEDTEEEQGEEKEKGAQEKRRGKRVRFAEDEEKSENSSEDGDITDKSLCGSGEKYIPPHVRQAEETVDFKKKEELERLKKHVKGLLNRLSEPNMASISGQLEELYMAHSRKDMNDTLTSALMGACVTASAMPSRLMMEHVLLVSILHHTVGIEVGAHFLEAVVRKFDAIYKYGSEGKECDNLFTVIAHLYNFHVVQSLLIFDILKKLIGTFTEKDIELILLMLKNVGFSLRKDDALSLKELITEAQTKASGAGSEFQDQTRIRFMLETMLALKNNDMRKIPGYDPEPVEKLRKLQRALVRNAGSGSETQLRVSWDSVLSAEQTGRWWIVGSAWSGAPMIDNSHHTHLQKQLVGTVSSKILELARKQRMNTDIRRNIFCTIMTSEDFLDAFEKLLKLGLKDQQEREIIHVLMDCCLQEKTYNPFYAFLASKFCEYERRFQMTFQFSIWDKFRDLENLPATNFSNLVHLVAHLLKTKSLSLSILKVVEFSELDKPRVRFLRKVLSILLMETEVEDLSLIFTRVSDNPKLGVLREGLKLFISHFLLKNAQAHRSADEANVLREKADLATKCLQGKASLRM
Protein: Stress-activated protein kinase JNK (EC 2.7.11.24) (A0A286YFD7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
Interaction partners:
Sequence:
MSKSKVDNQFYSVEVGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDMWSVGCIMGEMIKGAVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLQPTVRNYVENRPKYAGLTFPKLFPDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDDALQHPYINVWYDPAEVEAPPPQIYDKQLDEREHTIEEWKELIYKEVMNSEEKTKNGVVKGQPSPSGAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR
Protein: Protection of telomeres protein tpz1 (Meiotically up-regulated gene 169 protein) (O14246)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Telomeric DNA-binding protein that is required to protect the 3'-end telomeric overhang and involved in telomere length regulation. recruits poz1 and ccq1 to telomeres, regulating telomere length negatively and positively respectively.
Subcellular location: Chromosome, telomere {ECO:0000269|PubMed:18535244}. Nucleus {ECO:0000269|PubMed:18535244}.
Interaction partners:
- Protection of telomeres protein poz1
- DNA-binding protein rap1
- Coiled-coil quantitatively-enriched protein 1
- Protection of telomeres protein 1
- Telomerase reverse transcriptase
- Telomere length regulator taz1
- Protein stn1
- Protein ten1
- Trehalose-phosphatase
- Telomeric DNA-binding factor trf1
Sequence:
MSNCLKHPWLENGLLNLIKNADVLPIRVFKCQPLQIFEYIRYEHPIRCKLSDTEFYIEAEFSSQSISDLNNFTEKRITSLRGGIVTLGNFLIHLIPSQSGIIPWIQVESFNFQGCEGAVFGNPKAITTSALFNALLQSPYLAALANEFNRSIKEGSSYQEASLSQQEKPNDNTSNSRDIKNNIQFHWKNMTSLSIEECIIPKGQQLILEKESEENTTHGIYLEERKMAQGLHNSVSETPEVKQEDNDEDLDAYSWSSSTDSAGEIPSLPTNRKILEKIAEKPPPFESPLEDDETPDQTNEHEANQVNVSQLPLNPRGSGISGRPVESTEQLNSSLTIERSQSIQSTDSKQRVETQSHRRSKIEIFDAQDELFDRSICTTIDDSTGKLLNAEETPIKTGDLHSTSASSVISCTPPAINFTSDICNEQIELEYKRKPIPDYDFMKGLETTLQELYVEHQSKKRRLELFQLTNNHQKNSEACEMCRLGLPHGSFFELLRDWKKIEEFRNKS
Protein: Sodium/calcium exchanger NCL (Na(+)/Ca(2+)-exchange protein NCL) (Protein NCX-like) (AtNCL) (Q8L636)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses sodium/calcium exchanger (NCX) activity when expressed in a heterologous mammalian CHO-K1 cell system. Does not possess cation/proton exchanger (CAX) or sodium/proton (NHX) activity when expressed in a heterologous yeast cell system. Has the ability to bind calcium in vitro. Participates in the maintenance of calcium homeostasis. May play a role in auxin response, diurnal rhythm and flowering time. Involved in salt stress response.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23148213}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:26296956}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Magnesium/proton exchanger
- Cation/calcium exchanger 3
- Cation/calcium exchanger 5
- Cation/calcium exchanger 4
- Vacuolar cation/proton exchanger 5
- Cation/calcium exchanger 1
- Putative vacuolar cation/proton exchanger 6
- Cation/calcium exchanger 2
- Probable ion channel POLLUX
- Vacuolar cation/proton exchanger 4
Sequence:
MRFRSLISLLFLLFFTSSAYARFVSLNPSSTSLISDGIDGGSNLAGSGSVIKSVVSAPAEEKEEACEQTYGFMPCTKTALGNVFLILVYGFLMFTAATYLSAGSELLLEILGPGIVGGLFLPMLGALPDAMLIMVSGLSGDAATAQSQVSVGMGLLAGSTVMLLTVIWGTCTVVGKCDLRDSIAVNNQDTKGFHLKDSGVTVDIWTSYAARIMAISVIPFVIVQLPQMLGSTSGRQLSVLIALILSVLMLISYCVYQVFQPWIQRRRLAFAKHKHVISGILRHLKQHALGRLLDDEGQPDEHVIRKLFLTIDANNDGHLSAAELKALIIGISFEDIDFDKDDAVGKVLQDFDKTLDEQVDQEEFVRGIKQWLIQAMGGAPSGPEAGPRTMKFLDNFHVQTKREHALLGDNENGENDEEGGEVADPKWITIKAALLLLLGAAIAAAFADPLVDTVNNFSAATGIPSFFISFIALPLATNSSEAVSAIIFASRKKIRTASLTFSELCGGVTMNNILCLSVFLAIVYVRGLTWNFSSEVLVILIVCLVMGGFASFRTTYPLWTCFIAYLLYPFSLGLVYILDYWFGWS
Protein: Chaperone protein DnaJ (HSP40) (Heat shock protein J) (P08622)
Organism: Escherichia coli (strain K12)
Function: Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein GrpE
- Chaperone protein DnaK
- Chaperone protein HtpG
- Chaperone protein ClpB
- ATP-dependent protease ATPase subunit HslU
- Chaperonin GroEL
- Co-chaperonin GroES
- Chaperone protein HscA
- RNA polymerase sigma factor RpoH
- Chaperone protein HscC
Sequence:
MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGDLLCRVVVETPVGLNERQKQLLQELQESFGGPTGEHNSPRSKSFFDGVKKFFDDLTR
Protein: Envelope glycoprotein H (gH) (F5HAK9)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis (By similarity). Targets host EPHA2 to promote KSHV entry.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04033}.
Interaction partners:
Sequence:
MQGLAFLAALACWRCISLTCGATGALPTTATTITRSATQLINGRTNLSIELEFNGTSFFLNWQNLLNVITEPALTELWTSAEVAEDLRVTLKKRQSLFFPNKTVVISGDGHRYTCEVPTSSQTYNITKGFNYSALPGHLGGFGINARLVLGDIFASKWSLFARDTPEYRVFYPMNVMAVKFSISIGNNESGVALYGVVSEDFVVVTLHNRSKEANETASHLLFGLPDSLPSLKGHATYDELTFARNAKYALVAILPKDSYQTLLTENYTRIFLNMTESTPLEFTRTIQTRIVSIEARRACAAQEAAPDIFLVLFQMLVAHFLVARGIAEHRFVEVDCVCRQYAELYFLRRISRLCMPTFTTVGYNHTTLGAVAATQIARVSATKLASLPRSSQETVLAMVQLGARDGAVPSSILEGIAMVVEHMYTAYTYVYTLGDTERKLMLDIHTVLTDSCPPKDSGVSEKLLRTYLMFTSMCTNIELGEMIARFSKPDSLNIYRAFSPCFLGLRYDLHPAKLRAEAPQSSALTRTAVARGTSGFAELLHALHLDSLNLIPAINCSKITADKIIATVPLPHVTYIISSEALSNAVVYEVSEIFLKSAMFISAIKPDCSGFNFSQIDRHIPIVYNISTPRRGCPLCDSVIMSYDESDGLQSLMYVTNERVQTNLFLDKSPFFDNNNLHIHYLWLRDNGTVVEIRGMYRRRAASALFLILSFIGFSGVIYFLYRLFSILY
Protein: LOW protein: UPF0503-like protein, putative (DUF740) (F4IRZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVMNNPANNNPVAASSASAVALAPPPHPPQPHRPSTSCDRHPDERFTGFCPSCLFDRLSVLDITGKNNNAVASSSKKPPSSSAALKAIFKPSSSSGSFFPELRRTKSFSASKAEAFSLGAFEPQRRSCDVRVRNTLWSLFHEDAEHNSQTKEGLSVNCSEIDLERINSIVKSPVFEEETEIESEQDNEKDIKFETFKEPRSVIDEIVEEEEEEETKKVEDFTMEFNPQTTAKKTNRDFKEIAGSFWSAASVFSKKLQKWRQKQKLKKHRTGNLGAGSSALPVEKAIGRQLRDTQSEIAEYGYGRRSCDTDPRFSIDAGRFSLDAGRVSVDDPRYSFEEPRASWDGYLIGRAAAPMRMPSMLSVVEDSPVRNHVHRSDTHIPVEKSPQVSEAVIDEIVPGGSAQTREYYLDSSSSRRRKSLDRSSSTRKLSASVMAEIDELKLTQDREAKDLVSHSNSLRDDCCSVENNYEMGVRENVGTIECNKKRTKKSRWSWNIFGLLHRKNGNKYEEEERRSGVDRTFSGSWNVEPRNGFDPKMIRSNSSVSWRSSGTTGGGLQRNSVDGYISGKKKVSKAENGMLKFYLTPGKGRRRGSGNSTAPTSRPVPASQPFGSRNVMNFY
Protein: Tubulin alpha chain (Q6ZLZ9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Tubulin beta chain
- Dynein heavy chain, putative.
- Cytoplasmic dynein intermediate chain, putative
- Thioredoxin-like protein
- Tubulin epsilon chain, putative
- Ras-related protein RAB7
- Tubulin alpha chain
- Dynein intermediate light chain, putative
- Microtubule-associated protein RP/EB family, putative
- Kinesin-5
Sequence:
MREVISIHVGQAGIQVGNACWELFCLEHGIQPDGQMPSDKASRANDDAFNTFFSETGAGKHVPRCVFVDLEPTVVDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEVIDVCLDRIRKLADNCTGLQGFLMFSAVGGGTGSGFGCLMLERLSVDYGKKSKLNFCCWPSPQVSTAVVEPYNSVLSTHSLLEHTDVAIMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVVSAEKAYHEQLSVSEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRMDQKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIESNEAEGEDEGYEADY