wanglab/gogpt-training-data huggingface dataset:
Protein: Zcf14p (A0A1D8PNN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Dilute domain-containing protein
Sequence:
MPITKNNNTPINSSRGEHQFKQTKKRNRLSLNCFNCKRKKIKCNRQQPCLSCIKSNLESKCEYQQQKWLATPNNENNGIFQIQRLNDDKINESCQNKKDEIVIPLLRNQEKQEKNVGDGDGLSQLKLLNNILKEPINNNERNKFHEFEHENIGNIESEKYLSGLFENFIKYHEHLLENLELILGIRNKIEKISQLEPLLFKFEIYLDEKYPNIKHHELINTSENEVSFSSSSLSPNKIRNYINMKMILHMIYFYYYLYYERKQLQSLSYTYLKKTLVSHINGIIPHLFKLLSHDNDSNDFRFLITPIIIMINFPILIKLNYCVYKSRYLNSNHNEDLRDDFQYKLKFAKLNKLTQIYKKITEISLSIIISKLNQKHSSEYRQEIIIKIKSYRYILERICNDNEFLSNQTKYYNTIDELSKNNEELSEIIKILEIGMKRYTELKNKKEINTNFENYEKFNEPISKQNLISEIELVSLIPSYSHSQQQQQQQEQEKQRQELLFTDWEQGFNIMSNLDIDKFWSILAQLKK
Protein: Non-structural protein ORF4b (ORF4b) (K9N643)
Organism: Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1)
Function: Plays a role in the inhibition of host innate immunity by inhibiting the interaction between host IKBKE and MAVS. In turn, this inhibition prevents the production of host interferon beta. Additionally, inhibits host NF-kappa-B by interacting with host KPNA4 and thereby preventing the translocation of the NF-kappa-B complex into the nucleus by this importin.
Subcellular location: Host nucleus {ECO:0000269|PubMed:24318862, ECO:0000269|PubMed:24443473, ECO:0000269|PubMed:26631542, ECO:0000269|PubMed:29370303}. Host nucleus, host nucleolus {ECO:0000269|PubMed:26631542}. Host cytoplasm {ECO:0000269|PubMed:26631542}. Note=Mainly localized in the host nucleus. {ECO:0000269|PubMed:24318862, ECO:0000269|PubMed:24443473, ECO:0000269|PubMed:26631542}.
Interaction partners:
Sequence:
MEESLMDVPSTSGTQVYSRKARKRSHSPTKKLRYVKRRFSLLRPEDLSVIVQPTHYVRVTFSDPNMWYLRSGHHLHSVHNWLKPYGGQPVSEYHITLALLNLTDEDLARDFSPIALFLRNVRFELHEFALLRKTLVLNASEIYCANIHRFKPVYRVNTAIPTIKDWLLVQGFSLYHSGLPLHMSISKLHALDDVTRNYIITMPCFRTYPQQMFVTPLAVDVVSIRSSNQGNKQIVHSYPILHHPGF
Protein: Organic solute carrier partner 1 (Q582B3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDSSLVFLILNYGAEMIFILEARLSAQNVSEKTARMVLHDVIKHMYSSEFMDELFRPQMLYSFAATREVFKSLSQTSVMQLSPASMAKLFELMTTGLKYKIFSLRHPLELLELTWAHLEEVKRIASHETQCFVDPIFSRVNDLFQQLNVGMLAEVRKDLLNFLVGRCTPVSLLLESGVQAQSGYFYLKEDKTLPPLVECEPPGTIRYYGNGNLLATCTFKHRDAHLRHPLAFPVGRWDPRSSTAPRFTKRNVNMYTSKDLETKTQKLAQPSQKSDVIAAHPVGTKPEAVKAVQQEMSQLLRLVRGESEKPQHLFKLALCYEFEAEHGTRTPTTAEDATLSCSGTGPPSPRASDTAPSLPVNQMSKADVRKENEKLFSLMGELNLEEVSRKGGHNSVVTGANLLDIMDEE
Protein: Glutathione S-transferase 1 (EC 2.5.1.18) (GST-I) (Q9Y7Q2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the oxidative stress response and detoxification.
Interaction partners:
- Glutathione S-transferase 3
- Glutathione S-transferase 2
- Glutathione synthetase large chain
- Glutathione hydrolase proenzyme 2
- Glutathione hydrolase proenzyme 1
- Glutathione reductase
- Glutathione-specific gamma-glutamylcyclotransferase
- Uncharacterized protein C11D3.14c
- mRNA export factor elf1
Sequence:
MAQFTLWSHAHGPNPWKVVQALKELDLTYETRYVNFSKNEQKSPEHLALNPNGRVPTLIDHHNNDYTIWESDAILIYLADKYDTERKISLPRDHPEYYKVIQYLFFQASGQGIIWGQAGWFSVYHQELVISAITRYRNEIKRVLGVLEDILKDRDYLVANRFTIADLSFISWNNFLEIIFAEGKFSIEEEVPQLDFEKEFPRTYSWHQRLLARPASKATFEERSKALDN
Protein: Hephaestin (Hp) (EC 1.16.3.1) (Q9BQS7)
Organism: Homo sapiens (Human)
Function: May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:17486601, ECO:0000269|PubMed:20019163}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Ferroportin
- Ferrochelatase, mitochondrial
- Frataxin, mitochondrial
- Heme oxygenase 1
- Heme oxygenase 2
- Ceruloplasmin
- Natural resistance-associated macrophage protein 2
- Plasma membrane ascorbate-dependent reductase CYBRD1
- Hepcidin
- Transferrin receptor protein 2
Sequence:
MESGHLLWALLFMQSLWPQLTDGATRVYYLGIRDVQWNYAPKGRNVITNQPLDSDIVASSFLKSDKNRIGGTYKKTIYKEYKDDSYTDEVAQPAWLGFLGPVLQAEVGDVILIHLKNFATRPYTIHPHGVFYEKDSEGSLYPDGSSGPLKADDSVPPGGSHIYNWTIPEGHAPTDADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGALDGNSPPQRQDVDHDFFLLFSVVDENLSWHLNENIATYCSDPASVDKEDETFQESNRMHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISCQVNSHFRDGMQALYKVKSCSMAPPVDLLTGKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHLEEDRHLGILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACLTWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQKGVDKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQCPGHQATPRQRYQAARIYYIMAEEVEWDYCPDRSWEREWHNQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDMYSGLVGPLAICQKGILEPHGGRSDMDREFALLFLIFDENKSWYLEENVATHGSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDLHTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVFSRTEHLSPLTVITKETEKAVPPRDIEEGNVKMLGMQIPIKNVEMLASVLVAISVTLLLVVLALGGVVWYQHRQRKLRRNRRSILDDSFKLLSFKQ
Protein: Ribonuclease MRP protein subunit SNM1 (RNA-processing protein SNM1) (RNase MRP 22.5 kDa subunit) (P40993)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the MRP ribonucleoprotein endoribonuclease that cleaves mitochondrial primer RNA sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease P/MRP protein subunit RPP1
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP7
- Ribonuclease MRP protein subunit RMP1
- Ribonucleases P/MRP protein subunit POP6
- Ribonucleases P/MRP protein subunit POP3
- Ribonucleases P/MRP protein subunit POP8
- Ribonuclease P/MRP protein subunit POP5
- Uncharacterized protein YDR476C
Sequence:
MNKDQAEKYQERSLRQKYNLLHVLPTLNSRALSGLYYKNFHNSVKRYQIMLPEQLKSGKFCSHCGCVYVPNFNASLQLTTNTEQGDSDELGGESMEGPKKCIQVNCLNCEKSKLFEWKSEFVVPTFGQDVSPMINSTSSGKVSYAVKKPQKSKTSTGKERSKKRKLNSLTNLLSKRNQEKKMEKKKSSSLSLESFMKS
Protein: AT09333p (Q7JQU5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Stromalin-2
- FI03418p
- Something that sticks like glue, isoform A
Sequence:
MPALTHQILTMQRAPPLNLSFKIQLLSGQNVILVECSGYESELFLPQIVGERITMQNVIQDRRCCAESMLLRDPPMGDLGSETRTAKSPPRRFFAAANPPTPLAKSTPTNTSSLRARAGKENAVPQLTPEGLRCRPFHLPAPVEMDVDQLCCQEQTPERRASSKSISSANTNNSFFENEVSQPVISSKNVYANESARNNITPSSIYETGISPPVLPRENLTEQNHQAMELAINKTKPKLTAVRTYTRKRVETASKAKATPVWSPLQKKKKSSWVSSTKVPSPTMKVEVRNRKLIVDTKKTLAVHDPRKLSSGSITMKKIIRKQVTGKTRKQFEALKVTAFDLLTNLCVANISDDLTKQFQKACANRVCTTLPNYAEIAVVPPLEMDREVNALMARQKRMERETHRRWSAVPPEGNPV
Protein: Uncharacterized protein (Q38AV8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVDKLTPPFVPPFQHTKMPAVPCRASKGHHQVQLQHSVITFGSPNVEDGSRFFRQVVEGVRTGSERVLPKDESRRCLSGESDGATSRRLQQLNTDLQQALQKLRQRDREETKLRRRLSVVQLKLEEAAERHSATIEHVLGLMDVYGSRMEEQRMELQRLRAKVNNCDKTSEGLRNEGVISAPVGVRGLKASAVQAENESLKNRVKSLTDEREELRKMTQRLQDEKEENLQTFSNIRNKLTADIMDKQEQIHQANKKLKELSDEAAARDILVQQVRLFVQMVCQPDFHVVKDTSLQPVDRSRTEPTGFVLVPLTLMLQGYSLLSNEDRDDLVELYRQRLT
Protein: Protein O-glucosyltransferase 1 (EC 2.4.1.376) (CAP10-like 46 kDa protein) (hCLP46) (KTEL motif-containing protein 1) (Myelodysplastic syndromes relative protein) (O-glucosyltransferase Rumi homolog) (hRumi) (Protein O-xylosyltransferase POGLUT1) (EC 2.4.2.63) (Q8NBL1)
Organism: Homo sapiens (Human)
Function: Dual specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-glucose and UDP-xylose, respectively, to a serine residue found in the consensus sequence of C-X-S-X-P-C. Specifically targets extracellular EGF repeats of protein such as CRB2, F7, F9 and NOTCH2. Acts as a positive regulator of Notch signaling by mediating O-glucosylation of Notch, leading to regulate muscle development. Notch glucosylation does not affect Notch ligand binding. Required during early development to promote gastrulation: acts by mediating O-glucosylation of CRB2, which is required for CRB2 localization to the cell membrane (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16524674, ECO:0000269|PubMed:24387993, ECO:0000269|PubMed:27807076}.
Interaction partners:
- Coagulation factor VII
- GDP-fucose protein O-fucosyltransferase 1
- Xyloside xylosyltransferase 1
- EGF domain-specific O-linked N-acetylglucosamine transferase
- Neurogenic locus notch homolog protein 1
- Glucoside xylosyltransferase 1
- Glucoside xylosyltransferase 2
Sequence:
MEWWASSPLRLWLLLFLLPSAQGRQKESGSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTHYQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLVDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWLEFFYPQLKPWVHYIPVKTDLSNVQELLQFVKANDDVAQEIAERGSQFIRNHLQMDDITCYWENLLSEYSKFLSYNVTRRKGYDQIIPKMLKTEL
Protein: FAS-associated factor 1 (hFAF1) (UBX domain-containing protein 12) (UBX domain-containing protein 3A) (Q9UNN5)
Organism: Homo sapiens (Human)
Function: Ubiquitin-binding protein. Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation. Potentiates but cannot initiate FAS-induced apoptosis (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:26842564}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 1
- UBX domain-containing protein 7
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 6
- NSFL1 cofactor p47
- UBX domain-containing protein 2B
- Tether containing UBX domain for GLUT4
- BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2
Sequence:
MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSEYGGETIPGPAFNPASHPASAPTSSSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLAESGLSYPCHRLTVGRRSSPAQTREQSEEQITDVHMVSDSDGDDFEDATEFGVDDGEVFGMASSALRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAKE
Protein: Protein FAM181A (Q8N9Y4)
Organism: Homo sapiens (Human)
Interaction partners:
- Transcriptional enhancer factor TEF-3
Sequence:
MPLEERRSSGERNDAAPTNHRRPGEKRASTAKQVSSVPFLGAAGHQQSLPSSWKASCSGPLVMASDSDVKMLLNFVNLASSDIKAALDKSAPCRRSVDHRKYLQKQLKRFSQKYSRLPRGLPGRAAEPYLKRGSEDRPRRLLLDLGPDSSPGGGGGCKEKVLRNPYREECLAKEQLPQRQHPEAAQPGQVPMRKRQLPASFWEEPRPTHSYHVGLEGGLGPREGPPYEGKKNCKGLEPLGPETTLVSMSPRALAEKEPLKMPGVSLVGRVNAWSCCPFQYHGQPIYPGPLGALPQSPVPSLGLWRKSPAFPGELAHLCKDVDGLGQKVCRPVVLKPIPTKPAVPPPIFNVFGYL
Protein: Proteasome subunit alpha type-2 (Q54DM7)
Organism: Dictyostelium discoideum (Social amoeba)
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 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-2
- Proteasome subunit beta type-6
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-7
- 26S proteasome regulatory subunit 7
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3
- 26S proteasome non-ATPase regulatory subunit 11
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-1
Sequence:
MDSDYSFSLTTFSPSGKLVQIEHALQAAASGGSAIGIKAKNGVVLITEKKLHSLVDVTSVQKISMITENIGLVYAGMGPDSRVLIKKARKESEKYYKQYKEKIPVLQLVRELASIMQEFTQSGGVRPFGVSLLVAGFDEKGPHLYQVDPSGSYFAWKATAIGKNMVSSKTFLEKRYSDDLEIEDAIQTALITIKEGFETQLTEFNMELAIIGKNQEFKILTPAQIKDYLLNL
Protein: Brummer, isoform A (EC 3.1.1.3) (LD21785p) (Q9VUH7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLSFAGCGFLGIYHVGVAVCFKKYAPHLLLEKIGGASAGSLAACCLLCDLPLGSMTSDFFRVVNEARRYSLGPFSPSFNIQTCLLEGLQKHLPDDAHKRVNGRLHISLTRVYDGKNVIISEFESREEVLQALLCACFIPGFSGILPPRFRGVRYMDGAFSDNLPILDENTITVSPFCGESDICPRDQSSQLFHLNWANTSIEISRQNINRFVRILFPPRPEFLSKFCQQGFDDALQFLHRNNLINCRRCVAVQSTFVVSETVAQPQEFDPECRECKKHRKDALSSNMPQTVLDVIQDYIEQANKGLANWIFKHRGIKLLSLPATVPMDFLLATISKISALTPKLTKQARVMVEDLILQLNHAMRIRLLNKFTLYDQPHFDATGLLHSSRLYGPRVSILVDECGATPLEDDVDNFEHVLKMTTHNDALYAYYYTDSNTNKVKVTEIFDFDEITEHDKLATDLQIYEGSVEDHPNPHQHSHNTVVSEWNGVESVQVMPTTPELHDVAF
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FSJ1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MKLSNALAAVALAVSGVNAIEPTTTLAPTDFRVNMIELQAYLADIKGHMMQYLSFQGANPNQPYPSQMLGAVMFGNTGPLSEIAPETITMMITGVPWYSERLVGAIAARLADAGIVTAWPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPSPKSPSPSPSSSSSSSSMPSSSSSSSSMPSSSSSSSSMPSSSSSSSSMPSSSSSSSSMPSSSSSMTPSQKASIIPSSAAPSSSSSIVTTSSISSADASPVLPSSVVSSSSTEPSSANPRSISSVSNSTTIISMSSQTGSLNNISSTVFGNTTVSMPSPTTVVVTNTVGEVITEVITYCPETDHHGNVGTSTSSYIIGTSRVSQDTMTTKIVEDNITKTAIVYCETTTDSKGQASTKTVTVCPECTSINSKSGSKSTETVTATTKPVVNVSNGVTSTTFITEYVTVKSGIPTTSSTPGGKSDVQQAKIATTTTTLTSKQQQDSSIKIQSQSGTVKPQVEQQVSASAAKQQHSSVVVSQYAGSAASLNGLGSIGTLVTLLVLMLIN
Protein: Protein PER1 homolog (Q9P6N9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchors proteins. Required for phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for efficient transport of GPI-anchor proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MRVLRNFTIFFLFTALSLFRQISASAGDLHPVYVSCVNRCIENKCHGNPSDTSKLPLDLKLFRWDCGSNCGYECEITAENYFAAHNLPSQQYHGKWYFIRVFGIQELFSVFFSMLNFMIHYNGYHIMRRCIPDEHPAKRLCLSWAIVGMNAWVWSSVFHIRDTPITEKLDYFSAGAFVLFGSYCTLILMLRLDQLPGGKLLCWIIGVIFIAAFIAHVSYLSFYSFDYGYNMKANVAVGLVQNILWYYYSWSNRNSGLYWTRWPAYIVTSLMLATSLELFDFSPIANLIDAHALWHLSTVPITHYLYGFVVRKCSYDLTKGTFKIKAYDSSR
Protein: Adenosine 3'-phospho 5'-phosphosulfate transporter 1 (Q6P101)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Exostosin glycosyltransferase 2
- UDP-glucuronic acid decarboxylase 1
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
- Exostosin-like 3
- Protein-tyrosine sulfotransferase
- 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- Ribosomal protein L15
- Heparan sulfate 2-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- Xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7
Sequence:
MPLFPWSVCVCAALCFLPAVNADAVDASLLGGWQDVWLFRLFLNVLGYATIIIPGYFLISYFKRVNYLETGRGLCFPLIKTCVFGNESKTGLLDDASPAGRNESESSSSARQAFKLIFCAAGLQVSYLTWGVLQERVMTRSYGSSEAEGSGERFRDSQFLVFMNRILALTVSGLWCVLFKQPRHGAPMYKYSFASLSNILSSWCQYEALKFISFPTQVLAKASKVIPVMLMGKIVSRKSYEYWEYLTAVLISLGVSMFLLSSSTDKHPSTVTTFSGVLILAGYIVFDSFTSNWQDNLFKYKMSSVQMMFGVNLFSCLFTVGSLLEQGAFFNSLAFMTRHSEFAFHAVLLSVCSAFGQLFIFFTIAQFGAAVFTIIMTLRQALAILLSCFLYGHPVSLTGGLGVGVVFLALFLRIYARSRVKKSTKRPAQTPVQKV
Protein: SET domain-containing protein (Q57V49)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEVVPTRCVDWSLNTDSESGKLFLWHNIYNISVWSNTLGLSEPYDGLDDTSVWEAFLQFQISTVYKLCGVCRKPEGNEDLKVCCYCGQAVHKLCSTKAASDQIEWKDANKKFVSHMRVCGSCDGVEVPAAFTPPVREAPDARRVVRRALVVRDEYPEEVVRELESLEKKACRPHSKEEDDRLLGMVCRAVTRFFQPRNSLHLFAKVRQESKGGVGVVALKNIPALTIVGVYPGYCDALSGEHAKLGRPTAKYALMDLNCADYFNVVFEEFQSTFTPFINEPGEDERSNCGWIQETKNKDGRLSVMTCRGIRKGEELLIGYGPVYPRSYPYTYDAFTFHQVESKNCAVCFALWHWPTTDAEDAVLECHVGYDSATDSYHLVDIEDDSKRS
Protein: Amyloid-beta A4 precursor protein-binding family A member 1 (Adapter protein X11alpha) (Neuron-specific X11 protein) (Neuronal Munc18-1-interacting protein 1) (Mint-1) (Q02410)
Organism: Homo sapiens (Human)
Function: Putative function in synaptic vesicle exocytosis by binding to Munc18-1, an essential component of the synaptic vesicle exocytotic machinery. May modulate processing of the amyloid-beta precursor protein (APP) and hence formation of APP-beta. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20531236}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20531236}. Nucleus {ECO:0000269|PubMed:20531236}. Note=Only about 5% of the protein is located in the nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus {ECO:0000269|PubMed:23737971}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- Amyloid-beta precursor protein
- Syntaxin-binding protein 1
- Protein lin-7 homolog A
- Protein lin-7 homolog C
- Kinesin-like protein KIF17
- Protein lin-7 homolog B
- Neurexin-1
- Syntaxin-1A
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MNHLEGSAEVEVTDEAAGGEVNESVEADLEHPEVEEEQQQPPQQQHYVGRHQRGRALEDLRAQLGQEEEERGECLARSASTESGFHNHTDTAEGDVIAAARDGYDAERAQDPEDESAYAVQYRPEAEEYTEQAEAEHAEATHRRALPNHLHFHSLEHEEAMNAAYSGYVYTHRLFHRGEDEPYSEPYADYGGLQEHVYEEIGDAPELDARDGLRLYEQERDEAAAYRQEALGARLHHYDERSDGESDSPEKEAEFAPYPRMDSYEQEEDIDQIVAEVKQSMSSQSLDKAAEDMPEAEQDLERPPTPAGGRPDSPGLQAPAGQQRAVGPAGGGEAGQRYSKEKRDAISLAIKDIKEAIEEVKTRTIRSPYTPDEPKEPIWVMRQDISPTRDCDDQRPMDGDSPSPGSSSPLGAESSSTSLHPSDPVEASTNKESRKSLASFPTYVEVPGPCDPEDLIDGIIFAANYLGSTQLLSDKTPSKNVRMMQAQEAVSRIKMAQKLAKSRKKAPEGESQPMTEVDLFISTQRIKVLNADTQETMMDHPLRTISYIADIGNIVVLMARRRMPRSNSQENVEASHPSQDGKRQYKMICHVFESEDAQLIAQSIGQAFSVAYQEFLRANGINPEDLSQKEYSDLLNTQDMYNDDLIHFSKSENCKDVFIEKQKGEILGVVIVESGWGSILPTVIIANMMHGGPAEKSGKLNIGDQIMSINGTSLVGLPLSTCQSIIKGLKNQSRVKLNIVRCPPVTTVLIRRPDLRYQLGFSVQNGIICSLMRGGIAERGGVRVGHRIIEINGQSVVATPHEKIVHILSNAVGEIHMKTMPAAMYRLLTAQEQPVYI
Protein: Protein TRI1 (Q05024)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in transcription regulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA topoisomerase 1
- SWI/SNF chromatin-remodeling complex subunit SNF5
- Chromatin structure-remodeling complex subunit SFH1
Sequence:
MADINKYIPMVDAILSVSNPDEISPKRVRKALQILYSVNLDSQRKLINELILERFGDIQENPRVLIPKNDLISRDQELSLRLQKEEERPLRSTRKRKGKSESKSKRKKKKNDSPDSNSISVRKVLLSAPLQKFLGSEELPRTQVVKMIWQYIKEHDLQNPKDRREILCDEKMEPIFGKKMTMFSMNKLLTKHLFNPDEIVKHEEEQKQTPEKEIKLENESLPNLSG
Protein: Methionine aminopeptidase (MAP) (MetAP) (EC 3.4.11.18) (Peptidase M) (P0AE18)
Organism: Escherichia coli (strain K12)
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
Interaction partners:
- Peptide deformylase
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS8
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL2
- Elongation factor G
- Large ribosomal subunit protein uL6
Sequence:
MAISIKTPEDIEKMRVAGRLAAEVLEMIEPYVKPGVSTGELDRICNDYIVNEQHAVSACLGYHGYPKSVCISINEVVCHGIPDDAKLLKDGDIVNIDVTVIKDGFHGDTSKMFIVGKPTIMGERLCRITQESLYLALRMVKPGINLREIGAAIQKFVEAEGFSVVREYCGHGIGRGFHEEPQVLHYDSRETNVVLKPGMTFTIEPMVNAGKKEIRTMKDGWTVKTKDRSLSAQYEHTIVVTDNGCEILTLRKDDTIPAIISHDE
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (Immunoglobulin heavy chain-binding protein homolog) (BiP) (P59769)
Organism: Aspergillus awamori (Black koji mold)
Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P16474, ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MARISHQGAAKPFTAWTTIFYLLLVFIAPLAFFGTAHAQDETSPQESYGTVIGIDLGTTYSCVGVMQNGKVEILVNDQGNRITPSYVAFTDEERLVGDAAKNQYAANPRRTIFDIKRLIGRKFDDKDVQKDAKHFPYKVVNKDGKPHVKVDVNQTPKTLTPEEVSAMVLGKMKEIAEGYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRVVNEPTAAAIAYGLDKTGDERQVIVYDLGGGTFDVSLLSIDNGVFEVLATAGDTHLGGEDFDQRVMDHFVKLYNKKNNVDVTKDLKAMGKLKREVEKAKRTLSSQMSTRIEIEAFHNGEDFSETLTRAKFEELNMDLFKKTLKPVEQVLKDAKVKKSEVDDIVLVGGSTRIPKVQALLEEFFGGKKASKGINPDEAVAFGAAVQGGVLSGEEGTGDVVLMDVNPLTLGIETTGGVMTKLIPRNTVIPTRKSQIFSTAADNQPTVLIQVYEGERSLTKDNNLLGKFELTGIPPAPRGVPQIEVSFDLDANGILKVHASDKGTGKAESITITNDKGRLSQEEIDRMVAEAEEFAEEDKAIKAKIEARNTLENYAFSLKNQVNDENGLGGQIDEDDKQTILDAVKEVTEWLEDNAATATTEDFEEQKEQLSNVAYPITSKLYGSAPADEDDEPSGHDEL
Protein: Vacuolar protein sorting-associated protein 4 (E9AEB2)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Vta1/callose synthase N-terminal domain-containing protein
- Putative vesicular protein trafficking mediator
- Snf7
- Conserved SNF-7-like protein
- Snf7-like protein
- Charged multivesicular body protein 6
- Snf7-like protein
- Regulator of Vps4 activity in the MVB pathway protein
- SNF7-like protein
- ATPase-like protein
Sequence:
MSVDFTAKAVELFKKAATLDENKEYEQAYRWYMETIDVFLTAIKYENKNPTKREYMRSKVSDIIARAEKIKEFLDRSKDGDGANQGGSGATAQKTASASRKAKEDDEDKQRMRSSLGSAIVKVKPNVHWDQIAGLEAAKQALKESVILPMKFPQLFTGKRKPWRGILLYGPPGTGKSYLAKAVATEADGTFLSVSSSDLLSRWLGDSEKLVRSLFEMAREAYKTGGKPSIIFVDEIDSLVSARSDSENDASRRVKTEFLVQMQGVGYDDEGVLVLAATNIPWSLDSAIRRRFERRIYIPLPELQARVQMFKIHLGDTPNTLVDEDWLELGRRTEMYSGSDIENVVRNALMECIRTLQVATHFKRVVGPDPHDPTRMVKNRLLPCSPGDPDAFPMSAVEITEPELLMPMPVTKEDFIKALRTSKPSVNDEDIERHVKFTADFGQEG