wanglab/gogpt-training-data huggingface dataset:
Protein: UBX domain-containing protein 6 (UBX domain-containing protein 1) (Q9BZV1)
Organism: Homo sapiens (Human)
Function: May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes. As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation. It may also play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18656546}. Cytoplasm, cytosol {ECO:0000269|PubMed:19275885}. Membrane {ECO:0000269|PubMed:19275885}; Peripheral membrane protein {ECO:0000269|PubMed:19275885}. Nucleus {ECO:0000269|PubMed:18656546}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18656546}. Early endosome membrane {ECO:0000269|PubMed:21822278}; Peripheral membrane protein {ECO:0000305|PubMed:19275885}. Late endosome membrane {ECO:0000269|PubMed:21822278}; Peripheral membrane protein {ECO:0000305|PubMed:19275885}. Lysosome membrane {ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:27753622}; Peripheral membrane protein {ECO:0000305|PubMed:19275885}. Note=Localizes at the centrosome both in interphase and during mitosis (PubMed:18656546). May be recruited to endosomal and lysosomal membranes as part of a ternary complex with CAV1 and VCP (PubMed:21822278). Recruited to damaged lysosomes decorated with K48-linked ubiquitin chains (PubMed:27753622). {ECO:0000269|PubMed:18656546, ECO:0000269|PubMed:21822278, ECO:0000269|PubMed:27753622}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 4
- NSFL1 cofactor p47
- FAS-associated factor 1
- UBX domain-containing protein 10
- Tether containing UBX domain for GLUT4
- UBX domain-containing protein 2A
- Ubiquitin thioesterase OTU1
- UBX domain-containing protein 1
- Phospholipase A-2-activating protein
Sequence:
MKKFFQEFKADIKFKSAGPGQKLKESVGEKAHKEKPNQPAPRPPRQGPTNEAQMAAAAALARLEQKQSRAWGPTSQDTIRNQVRKELQAEATVSGSPEAPGTNVVSEPREEGSAHLAVPGVYFTCPLTGATLRKDQRDACIKEAILLHFSTDPVAASIMKIYTFNKDQDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKLQNKVFQERINCLEGTHEFFEAIGFQKVLLPAQDQEDPEEFYVLSETTLAQPQSLERHKEQLLAAEPVRAKLDRQRRVFQPSPLASQFELPGDFFNLTAEEIKREQRLRSEAVERLSVLRTKAMREKEEQRGLRKYNYTLLRVRLPDGCLLQGTFYARERLGAVYGFVREALQSDWLPFELLASGGQKLSEDENLALNECGLVPSALLTFSWDMAVLEDIKAAGAEPDSILKPELLSAIEKLL
Protein: Latent membrane protein 2A (A8CDV5)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Interaction partners:
Sequence:
MGSLEMVPMGAGPPSPGGDPDGDDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRG
Protein: SRP-independent targeting protein 3 (Inorganic phosphate transport protein PHO88) (Phosphate metabolism protein PHO88) (P38264)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the SND pathway, a SRP (signal recognition particle) and GET (guided entry of tail-anchored proteins) independent pathway for targeting a broad range of substrate proteins to the endoplasmic reticulum. SND functions in parallel to GET in targeting proteins with downstream hydrophobic motifs. Involved in inorganic phosphate uptake. Also involved in telomere length regulation and maintenance.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:27905431}; Single-pass membrane protein {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:8709965}.
Interaction partners:
- SRP-independent targeting protein 2
- Inorganic phosphate transporter PHO86
- SRP-independent targeting protein 1
- Mannan polymerase complexes subunit MNN9
Sequence:
MNPQVSNIIIMLVMMQLSRRIDMEDPTIIMYIRILYCSSIGISWIIYQMARKRIVAKNDMTTMKYVEPGNAMSGEGEKLQVTTVRDYDLKEIDSAIKSIYTGMAMMGFMHLYLKYTNPLFMQSISPVKSALEHNEVKIHLFGKPATGDLKRPFKAPSLFGGMGQTGPKTDKKSIEEAERAGNAGVKAE
Protein: Alcohol dehydrogenase (EC 1.1.1.1) (P10807)
Organism: Drosophila lebanonensis (Fruit fly) (Scaptodrosophila lebanonensis)
Interaction partners:
Sequence:
MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAESKKLLKKIFDQLKTVDILINGAGILDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWLDVEPRVAELLLSHPTQTSEQCGQNFVKAIEANKNGAIWKLDLGTLEAIEWTKHWDSHI
Protein: Arsenite methyltransferase (EC 2.1.1.137) (Methylarsonite methyltransferase) (S-adenosyl-L-methionine:arsenic(III) methyltransferase) (Q9HBK9)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a methyl group from AdoMet to trivalent arsenicals producing methylated and dimethylated arsenicals. It methylates arsenite to form methylarsonate, Me-AsO(3)H(2), which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite is also a substrate and it is converted into the much less toxic compound dimethylarsinate (cacodylate), Me(2)As(O)-OH.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VHT6}.
Interaction partners:
- BLOC-1-related complex subunit 7
- Metal transporter CNNM2
Sequence:
MAALRDAEIQKDVQTYYGQVLKRSADLQTNGCVTTARPVPKHIREALQNVHEEVALRYYGCGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHMEKYGFQASNVTFIHGYIEKLGEAGIKNESHDIVVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFCPPRLVTANLITIQNKELERVIGDCRFVSATFRLFKHSKTGPTKRCQVIYNGGITGHEKELMFDANFTFKEGEIVEVDEETAAILKNSRFAQDFLIRPIGEKLPTSGGCSALELKDIITDPFKLAEESDSMKSRCVPDAAGGCCGTKKSC
Protein: Dihydrouridine synthase 2 (J3QLD5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILNSLSLCYHNKLILAPMVRVGTLPMRLLALDYGADIVYCEELIDLKMIQCKRVVNEVLSTVDFVAPDDRVVFRTCEREQNRVVFQMGTSDAERALAVARLVENDVAGIDVNMGCPKQYSTKGGMGAALLSDPDKIEKILSTLVKGTRRPVTCKIRILPSLEDTLSLVKRIERTGIAAIAVHGRKREERPQHPVSCEVIKAIADTLS
Protein: AT1G76160 protein (SKU5 similar 5) (T23E18.10) (Q9SGR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Thiamine phosphate phosphatase-like protein
- At2g39210/T16B24.15
- non-specific serine/threonine protein kinase
- Receptor homology region, transmembrane domain- and RING domain-containing protein 4
- Receptor homology region, transmembrane domain- and RING domain-containing protein 5
- Receptor homology region, transmembrane domain- and RING domain-containing protein 3
- Protein CHLORORESPIRATORY REDUCTION 42
Sequence:
MAGSASFAAALFIGLSLLFAVTAEDPYRFFEWNITYGDIYPLGVRQQGILINGAFPGPDIHSVTNDNLIINVYNSLDEPFLLSWNGIQQRRNSFVDGVYGTTCPIPPGKNYTYILQMKDQIGSFYYFPSLGFHKAAGGFGGIRILSRPRIPVPFPDPAGDTTVLIGDWYKANHTDLRAQLDNGKKLPLPDGILINGRSSGATLNVEQGKTYRFRISNVGLQDSLNFRIQDHKMKVVEVEGTHTLQTTFSSLDVHVGQSYSVLVTADQTPRDYYVVVSSRFTSNVLTTTGIFRYSNSAGGVSGPIPGGPTIQIDWSLNQARAIRTNLSASGPRPNPQGSYHYGMINTTRTIRLASSAGQVDGKQRYAVNSVSFKPADTPLKIADYFKIDGVYRSGSIQYQPTGGGIYLDTSVMQVDYRTFVEIIFENSEDIVQSWHLDGYSFWVVGMDGGQWSPDSRNEYNLRDAVARCTVQVYPSSWTAILIALDNVGMWNLRSEFWARQYLGQQLYLRVYTPSTSLRDEYPIPKNALLCGRASGRSTRPL
Protein: Nitrite reductase (NADH) small subunit (EC 1.7.1.15) (P0A9I8)
Organism: Escherichia coli (strain K12)
Function: Required for activity of the reductase.
Subcellular location: Cytoplasm.
Interaction partners:
- Nitrite reductase large subunit
- Nitrite transporter NirC
- Respiratory nitrate reductase 1 beta chain
- Respiratory nitrate reductase 1 alpha chain
- Cytochrome c-552
- Nitrate/nitrite antiporter NarK
- Siroheme synthase
- Nitric oxide reductase FlRd-NAD
- Periplasmic nitrate reductase
- Periplasmic nitrate reductase, electron transfer subunit
Sequence:
MSQWKDICKIDDILPETGVCALLGDEQVAIFRPYHSDQVFAISNIDPFFESSVLSRGLIAEHQGELWVASPLKKQRFRLSDGLCMEDEQFSVKHYEARVKDGVVQLRG
Protein: Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 2 (Cytochrome c biogenesis orf203) (Q33884)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a complex with CCMFC, CCMFN1 and CCMH that performs the assembly of heme with c-type apocytochromes in mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18644794}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c-type biogenesis CcmH-like mitochondrial protein
- Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 1
- Cytochrome c biogenesis FN1
- Putative cytochrome c biosynthesis ccmC-like mitochondrial protein
- Putative cytochrome c biosynthesis ccmC-like mitochondrial protein
- Putative cytochrome c biosynthesis ccmC-like mitochondrial protein
- Cytochrome c biogenesis FC.
- Maturase
- Cytochrome c biogenesis CcmF C-terminal-like mitochondrial protein
- NADH-ubiquinone oxidoreductase chain 4
Sequence:
VDTGREQAKRVVRNGKKETTTLPLCWTAGANTVVSDQDQEPIRIWILTCWWFLTVGILLGSWWAYHELGWGGWWFWDPVENASFMPWVLATACIHSVILPLLHSWTLFLNIVTFLCCVLGTFSIRSGLLASVHSFATDDTRGIFLWWFFLLMTGISMILFYQMKQQASVRRTYKKEMVVARSTLVHLRHSARAQPRPVMLWKN
Protein: Cullin-2 (CUL-2) (Cullin-B) (Q9XZJ3)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity). Appears to ensure that the proper number of prestalk cells differentiate at the appropriate time in development. May govern prestalk cell differentiation.
Interaction partners:
- Cullin-associated NEDD8-dissociated protein 1
- Elongin-C
- RING-box protein 1
- Cullin-5
- Cullin-1
- COP9 signalosome complex subunit 5
- UDP-galactose:fucoside alpha-3-galactosyltransferase
- NEDD8-conjugating enzyme Ubc12
- VWFA domain-containing protein
- Bifunctional glycosyltransferase pgtA
Sequence:
MMNGLGRQDIDFNTIWKNIADQVYKILTGSQNVSAMFLYEDVYKLCIAQPQPYCEPLYENIKKFFEQHVDQILLIILDTKSDTISEYLKQWKLFFSGCELCNKVIFRYLNLNWINKKILDKKFGHPPDVYEIQILGLMIWKERLFFKIKDRVLKCVEILIQKDRDGELVQHQFISQFMESLIKLDSVDKDRTLYLIEYEASYLENTRQFYTRESVAFIASSGISSYMKKAETRIDEEEQRSQKYLNSSSHDKMRRLLHSILIEKHKELLQSECINYLKDEKLDEIYNMYKLLSRIEGGLAPVLETVQKYIQHVGIDAIKSIPDRNNPDPKIYVETLLKIYLQFSSIIKKSFNNDVSFITVLDLACHKIFNQNHITRNTTKSPELLAKYCDMLLKKGNKQHEEIELEEKLGQIIVLFKYVDDKDVFQKFYSKMLSRRLINGTSVSDDIEKFMITGLKQACGFEYTSKFQRMFNDITLSAETNEEFKNHLIKNSLSIGKIDFSILVLTSGSWSLHSQTSSFIVPQELTLCISAFQQYYSTQHQGRKLNWLHHLCKAEAKSFFAKKSYDFQVTNFQLGILLIFNTQESVSLEEITKFTNLNENELSRTLQSLIEAKILISKKKDQNSINNNNNNNNNNNNNGEGNNSLVDSANNMQPSSSSSSTQEYTVNSAYSNKRSKVKVSSSLQKETPLQNEETYKGIDEDRKLYLQASIVRIMKARKTMNHVSLIQEVIEHSRLRFQPNIPMIKKCIEQLIEKEYITRAEGESDRYLYAA
Protein: Actin-associated protein FAM107A (Q6IAM1)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cell projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004632}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000256|ARBA:ARBA00004529}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MYSEIQRERADIGGLMARPEYREWNPELIKPKKLLNPVKASRSHQELHRELLMNHRRGLGVDSKPELQRVLEHRRRNQLIKKKKEELEAKRLQCPFEQELLRRQQRLNQLEKPPEKEEDHAPEFIKVRENLRRIATLTSEEREL
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha2 (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa subunit) (PAF-AH subunit beta) (PAFAH subunit beta) (P68401)
Organism: Bos taurus (Bovine)
Function: Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE. May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophosphatidylcholine acyltransferase 1
- Platelet-activating factor acetylhydrolase
- Lysophosphatidylcholine acyltransferase 2
- Choline/ethanolaminephosphotransferase 1
- LPCAT4 protein
- Cholinephosphotransferase 1
- Clathrin heavy chain 1
Sequence:
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDTDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
Protein: Putative RNA polymerase II transcriptional coactivator (P87294)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. Binds single-stranded DNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- mRNA cleavage and polyadenylation specificity factor complex subunit pta1
- Transcription initiation factor IIF subunit beta
- Transcription factor tau subunit sfc7
Sequence:
MAGKRVIASGDKASSKKPKTEKQSDHELHWALNETEKKRITLSEFRGTRYVHIREYYEKDGDMLPGKKGIALNINEWKKLKQLIHEVDDSLGLVDSGSDSEDEIKEKAENNASLKNDEDDLNTKTENKTDDSSVEN
Protein: multidrug resistance regulator 2 (Q59MJ1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that controls the expression of CDR1, the major multidrug efflux pump. Required for yeast cell adherence to silicone substrate and plays a role in virulence.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTKRDRTIYSCDACRSRKIKCNRQTPCASCHKSKRDCVYTVSRQRDAQITNRKLDKKTYHQISAIEKKISALEGKKGLLQVETINFNKSFTDQTPLVELQSLFPYLLLSKQDPGCVLVRHHCHHLLEKDPRYFEYSQLLADLSLTKRHHLTARAKALLGEAYIPSPQEGHTIDQLKHVLSLNPNFRFAGNFADPLTSFFSLIPPAWANKQLVDTFFQHIYPVIPIIDETDFNTSINRVLGPQIDGHYINSFPSIGSADDLPFLALFLLVLRISYMYTPGACPVSYDTLRAAETIMKEFDITKTHSLTALQAEIMLRFYKIVAPESYTQSNYVQVSVGVLIQNCYSLALHRDPEYIGEHNPKQQHLRRKIWHLLLRMEVIDSAIFQTILSSNPDASDTKLPQLIDQAPPMEQSIVKHIWRSTDLFVSLRKLVEINSKTSEDTPLETVLELLVEVETKLQAFLATIDSEASTVFYNDLVIFSVNFLLVYMYYSLYLFKGPTPLGNKYLLKSAQILFVDLARTRSTSLFLAYFNLNYIHLVLMITNFLRMRVDCIIHRHLRAQDSSVQDLQCCRYFLKIIFFSHVKELGNYSSSHKYAWQMRKVYLTLAKIMERSSDVLISNDPELVKSAAVDIPVKEINKLLEQYINFKGFTPTTLFDPTDNELIDEMQHENLWNAMENIEYSEKVYSGWIDAIKNVPSNWDWDYWDFLKIS
Protein: Ras-related protein Rab-6D (EC 3.6.5.2) (Rab6-like protein WTH3DI) (Q53S08)
Organism: Homo sapiens (Human)
Interaction partners:
- Rab GDP dissociation inhibitor beta
Sequence:
MSAGGDFGNPLRKFKLVFLGEQSVAKTSLITRFRYDSFDNTYQAIIGIDFLSKTMYLEDGTIGLRLWDTAGQERLRSLIPRYIRDSAAAVVVYDITNVNSFQQTTKWIDDVRTEGGSDVIITLVGNKTDLADKRQVSIEEGERKAKGLNVTFIETRAKAGYNVKQLFRRVAAALPGMESTQDGSREDMSDIKLEKPQEQTVSEGGCSCYSPMSSSTLPQKPPYSFIDCSVNIGLNLFPSLITFCNSSLLPVSWR
Protein: GSKIP domain-containing protein (Q9XWX6)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTSLPPRNRSASLFEGSPFAPSSTTSPPTSSLAKMLKSEPIPCLRCGNVGSPTGSVPMSLHKVSSINRSAGTNPASRGGESSLELEAIAAVHELSFAVQSISVSEMLPRTPDLIFVNVTTLEAQPYCLELTLKGWRITSLRSDCMVGDFTRLELFTKYYDSLYLLMDDISPGYRERFSEKLVQRLKLIEAGEEDQVAPCASLQSPSLSTDSSSKESQYSSTESLPIVTPVSTPAIDPDFKPKFK
Protein: Lemur tyrosine kinase 2 (D3ZBH5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPGPPASSPLPMPLLLLLLLTVGSARAAPLPQTGAGDAPVVEVPSLFVILSVCSLMVLIVLIANCVSCCKDPEIDFKEFEDNFDDEIDFTPPAEDTPSVQSPAEVFTLSVPNISLPAPSQFQSSVEGLKSQVARHSLNYIQEIGNGWFGKVLLGETYTGTSVTRVIVKELKVSASPKEQDTFLNSGEPYYILQHPNVLQCVGQCVEAIPYLLVFEFCDLGDLKAYLHNEQEHVRSESQTMLLQRMACEIAAGLAAMHKLHFLHSDLALRNCYLTSDLNVKVGDYGIGFSRYKEDYIETDDKKIFPLRWTAPELVTSFQDRLLTADQTKYSNIWSLGVTLWELFNNAAQPYANLSDLDVLNQVIRERDMKLPKPQLELPYSERWYEVLQFCWLSPDKRPAAEDVHRLLTYLRMQSQRDSEVDFEQQWTALKPNANSRDPSSSAAFPILDHFARDRLGREMEEVLTVTETSQGLSFEYVWEAAKHDHFDEQGRGHPDEALSYSSMFFPVEVFENSLSDPGPGKQDGSGQEGPLRAPGVVPVFDAHNLSVGSDYYIQLEEKSSSSLGLEYPPALLTTEVDNPEKGGTDAPHLTAFKTLVSEEPSAEEDFFQSSARPKEANSAEDSHAASIPGSPFNIFSDLDKADDLPSHQKIFDLMELNGVQADFKPAILSPSLDGPKDTCQSEREKPHDQDPLCFPESPVHQDCFDPLSVQELSENFLFLQEKNLLKGSLPGKGRVNDLQTELKDAGFISEMLESPRRGSVSSGLELLEHTLDFPSSQENMSGQNKGTGGTPQGATSPQASPLTEGSPNGPPDSVLKSGETKPFTGVSVPENSVCLDLSPDPVTGPVEIPAADAKAPDGGDGPPEVTCQSKEALNPTKRDPILENEITAQGSMETCLPESGQDLQNQPFSEDPLSGSILEKNSEAVETLNQLNYKAAPKDAALASALSSDSTSQDSLLEDSLSTPIPTSEQSVETPDSLDSVDVHAALLESLGSHTPQKLLPPDKPADSGYETENLESPEWTLHPAPEGTADSDTAAAGDSSHSSLPPNPVIVISDAGDGHRGAEGPPQSFSLGTQSSYRDSAYFSDNDSEPDKKPEEAPGTSASALVLVKDQLPPEPVAPEDSPDDVREGCLEASQSKPEQSPASALQNSCHSELQETLQPTPADQSPASALQNSCHSELQETLQPTPADQSPASALQNSCHSELQEMLQPTPADQSPASALQNSCHSELQETLQPTPADQSPASALQNSCHSELQETLQPTPADQSPASALQNSCHSELQETLQPTPADQSPASALQNSCHSELQETLQPTPAGASRETYPVDDEARGPLGLLNSEFSSCDDLETQEDRPCTLASTGTNTNELLAYTGSTLDKSLPSHFEGPKLKEPDIEGKYLGKLCVSGMLDLSEDGMDADEEDENSDDSDEDLRAFNLHSLSSESEDDMEHPVPIIVSNDDGRHLRSLLKPSAAAAIEQLPDDWKKEKKAVTFFDDVTVYLFDQETPTKELGHCGGEAHGPGPSSPAASTGSPYLSRCMNSESSTDEEGGGFEWDDDFSPDPFMSKTTSLLGSKPSLQTSKYFSPPPPARSSEQSWPHVSPCSRFSISPANIASFSLTHLTDSDIEQGGSSEDGDKD
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380V8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MLANFKALTFVSIALCLPVVTTSAVKTPTKKAKSACDVATQLRQMADSARTKITSTQEAVKTMLTTASKPDVIANGVNTNAGWAAAYLRSIYIQKAAEANDKLAANTPALLKGIEALSRLAGSQEAISRLSQLHLQDLNMATATTSTATATKGQLKPKLDAALKAHCVGQDDSREKDSSTDDHNADHKNAITIVTVTPTPPGSALGTYLTICGSNSVSSGAPNTASCTSTQATNIGFKGGQVFTATVAVAHTTGDSAPLAYNEIGDDATTPNKATIKAELALVLEMVHAATQLGTITPPATIESAFDAASAGHAIAKALGGHEATAEQPNLKEKVKHTTEELFGKERNSIKTQITQLLNTFQPSKAAGSDGAKKLDSINAPEELSKAATYYTIKNFIDEEEQKKKNQENPSCPTKTGKLEEPKKSADECKKHTTEQACKGEKGCDFDEKKDPKCFPNKKVSTTSTGRRSIVINALPLLAVLLLA
Protein: Origin recognition complex subunit 4 (A0A1D8PNC0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Origin recognition complex subunit 1
- DNA replication licensing factor MCM2
- Origin recognition complex subunit 2
- Origin recognition complex subunit 6
- Origin recognition complex subunit 3
- Origin recognition complex subunit 5
- DNA replication factor Cdt1 C-terminal domain-containing protein
- Cell division control protein
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM6
Sequence:
MNSQDHFKDDFEGEFKPIKYLPKRKIDKEESSINSVNPNANIKRIKKASSVIGIDDDNTYLDSPLDKTKHSKTVPDGQYDANDHAITLPEAVEDDIETVKTQILDQLNGNLQIFSSTPSVSEKYSEIYSIFERTIKDKESHSVLMVGPRSSGKTTIVKSALKELNGNYKGEFISIYLNSSVQTDDSSALREIARQLDINVKKDVGGYGSDSMELTNEKIGYANFEKKSINDTFSNILSVLTSNKGDRDERMPLVFVIDEFEKFTVDSRQTLLYNLLDISQSSATPLCVVGLTTKITTKEALEKRVSSRFSQRVISLVHEASLENFWDNCKASLLLQDSTIDKLKNPEYGLSWNKHVEQLYCKKNSLLKGMVVRNYHTAKDYRKFNNACKVPVSKLSLHHTYIEESYFKLRTTGSNGVQDLVTSLSDLELLLVIAAVRWIEKFELQTINFNLAYTEYQEMVKNFNTGNAIVSSTSLDSRIAANIKVDRKVLSRRVSLNSWSTLYKLGILLDPKGDYVEGQSNNYSYHINKNLIIEENQMVLVDITLDELNGFIEDKHVFKRFVRL
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (Vacuolar H(+)-ATPase subunit H) (Vacuolar proton pump subunit H) (Q9LX65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit C
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d2
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit e2
- V-type proton ATPase subunit c''1
Sequence:
MDQAELSIEQVLKRDIPWETYMNTKLVSAKGLQLLRRYDKKPESARAQLLDEDGPAYVHLFVSILRDIFKEETVEYVLALIYEMLSANPTRARLFHDESLANEDTYEPFLRLLWKGNWFIQEKSCKILAWIISARPKAGNAVIGNGIDDVLKGLVEWLCAQLKQPSHPTRGVPIAISCLSSLLKEPVVRSSFVQADGVKLLVPLISPASTQQSIQLLYETCLCIWLLSYYEPAIEYLATSRTMQRLTEVVKHSTKEKVVRVVILTFRNLLPKGTFGAQMVDLGLPHIIHSLKTQAWSDEDLLDALNQLEEGLKDKIKKLSSFDKYKQEVLLGHLDWNPMHKETNFWRENVTCFEENDFQILRVLLTILDTSSDPRSLAVACFDISQFIQYHAAGRVIVADLKAKERVMKLINHENAEVTKNAILCIQRLLLGAKYASFLQA
Protein: [histone H3]-trimethyl-L-lysine(4) demethylase (EC 1.14.11.67) (A0A3B3ISE6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELELVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDERWQRKKTTSVCAVL
Protein: Haloacid dehalogenase-like hydrolase domain-containing protein 3 (Q9BSH5)
Organism: Homo sapiens (Human)
Interaction partners:
- Phosphoserine aminotransferase
- 5'-nucleotidase
Sequence:
MAHRLQIRLLTWDVKDTLLRLRHPLGEAYATKARAHGLEVEPSALEQGFRQAYRAQSHSFPNYGLSHGLTSRQWWLDVVLQTFHLAGVQDAQAVAPIAEQLYKDFSHPCTWQVLDGAEDTLRECRTRGLRLAVISNFDRRLEGILGGLGLREHFDFVLTSEAAGWPKPDPRIFQEALRLAHMEPVVAAHVGDNYLCDYQGPRAVGMHSFLVVGPQALDPVVRDSVPKEHILPSLAHLLPALDCLEGSTPGL