wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoplasmic linker associated protein 1 (A0A1B0GWS3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}.
Interaction partners:
Sequence:
MTTGKDKNFDDEDSVDGNRPSSASSSSSKAPSSSRRNVSMGTTRRLMASSLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNALKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTIFNLIPNSAKIMATSGVVAVRLIIRHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTASRGSTVSTKSMSTTGSLQRSRSDIDVNAAASAKSKVSSSSGSTAFSSAAALPPGSYASLDGTATKAEGRIRTRRQSSGSTTNVASTSSDSRGRSRAKVVSQSQRSRSANPAGAGSRSSSPGKLLGSGYGGLAGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLDRFGLGQSGRIPGSVSAMRVLSTSTDLEAAVADALLLGDARSKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNAGVGSPSNTIGRTPSRHPSSRTSPLTSPTNCSHGGLSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKDCDIVSRDGGAASPATEGRGGSEVEGGRMALDNKTSLLNTQPPRAFPGPRAREYNPYPYSDTINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERITKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS
Protein: Homoserine dehydrogenase (HDH) (HSD) (EC 1.1.1.3) (P9WPX1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Threonine synthase
- Homoserine kinase
- Aspartate-semialdehyde dehydrogenase
- Aspartokinase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Methionine synthase
- Homoserine O-acetyltransferase
- Diaminopimelate decarboxylase
- Cystathionine gamma-synthase
- Branched-chain-amino-acid aminotransferase
Sequence:
MPGDEKPVGVAVLGLGNVGSEVVRIIENSAEDLAARVGAPLVLRGIGVRRVTTDRGVPIELLTDDIEELVAREDVDIVVEVMGPVEPSRKAILGALERGKSVVTANKALLATSTGELAQAAESAHVDLYFEAAVAGAIPVIRPLTQSLAGDTVLRVAGIVNGTTNYILSAMDSTGADYASALADASALGYAEADPTADVEGYDAAAKAAILASIAFHTRVTADDVYREGITKVTPADFGSAHALGCTIKLLSICERITTDEGSQRVSARVYPALVPLSHPLAAVNGAFNAVVVEAEAAGRLMFYGQGAGGAPTASAVTGDLVMAARNRVLGSRGPRESKYAQLPVAPMGFIETRYYVSMNVADKPGVLSAVAAEFAKREVSIAEVRQEGVVDEGGRRVGARIVVVTHLATDAALSETVDALDDLDVVQGVSSVIRLEGTGL
Protein: DNA repair protein RAD50 (EC 3.6.-.-) (Q9W252)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the MRN complex, a complex that possesses single-stranded DNA endonuclease and 3' to 5' exonuclease activities, and plays a central role in double-strand break (DSB) repair. The complex participates in processes such as DNA recombination, DNA repair, genome stability, telomere integrity and meiosis. The MRN complex may protect telomeres by facilitating recruitment of HOAP and HP1 at chromosome ends. In the complex, it mediates the ATP-binding and is probably required to bind DNA ends and hold them in close proximity.
Subcellular location: Nucleus {ECO:0000269|PubMed:15296753}. Chromosome {ECO:0000269|PubMed:15296753}. Chromosome, telomere {ECO:0000269|PubMed:15296753}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}.
Interaction partners:
- Nibrin
- Double-strand break repair protein
- Serine/threonine-protein kinase ATM
- ATP-dependent DNA helicase 2 subunit 1
- Flap endonuclease 1
- Serine/threonine-protein kinase ATR
- Microcephalin, isoform D
- ATP-dependent DNA helicase PIF1
- Exonuclease 1
- DNA repair protein Rad51 homolog
Sequence:
MSSIESLSIQGIRSFGTYADDLQSIKFSSPVTLILGENGCGKTTVVECLKYALTGECPPGSDRGKSFVHDPKIFGLNEVLAQIKMQVRDRRGAQVSICRTMKVSKKRNKMSFETMDSTINFLTGAGQSKREKQDSLSGRSVDIDVAISDFMGVSKAIINNVLFCHQEDSSWPLDESKKLKEKFDAIFGITEYNKALDKIIKLRKEAMEELKIKEANIKHVAYLKQEMEVKTLNLQKAQRKCDAIKAQCSECEEEMKPIEARLVEIRNVEFEIGKYQAQKVEMDTKHKNCKDQISTLTLKIKKPFRGTLDELDQEISNFDQRMLEMRQKRTEVEGDLSQIKRSSVAEQEKLGTQDRKHCLAKQRHQSELACRAQLLKRVKEFCRELHIPIDCDLVEQPEKMGEVLRDIEAMIITKHCEITEIVEQNEKADRSRQVKIDELRIELTKSEQSVTAQEKQRESSKRESETLGVEIKKIETSMQDLKKLEKEINEVNELYESATKNIDQQAIKDAIARKKASIAENQIQFKKLDEQLTFLGSMAKLVAECSLKQKELDKKNQEVHRVRSRHSDHFGKLFKEPITCNYRRSMQVVYEKLRREIQELNEKANTQKLKEQSYEIKRKNLISDISRMEKELKDSEELIYQKCRSTPYDDLLERSKTTISKLQFDHGALKSSEALYKKYIQKMDEEPSCPLCHHNMTSDEACDLTSELTDEIQKLPDNITRAEKALKAEQIKYENLLQLKPTILKVKELKDSLPQKKEELKKVEELLGDSVSEYETLIALIGEPTHNMELANSMMGDMSLLDEALKDSARLTKDLDLQKGQLPASYDSSVSMDDLQAEKSKVSKELETERKELESAQNAVQQQMDALNRLREKKNSLKDRQIHLREGLQSLPQLKERLEKLNSFLTTVASEISELKAKIQPLKLNLRAAIEEKERLKKSESEKLAQLNSKYNSYKSTDHDIQRLNKEAEDYAKLDLRNEIKKLDEIIMASKDKLRKLEAEISLKTDELETIKTECSNQQTVERDLKDNRELKQLEDKEAKLRESCQVLDKQLGNLDFHSVSKEKVNLTKQRDKATVRKGELLGQLGEIHSQVNKLQREIDEPRFKESLKNFRKANYEIEVTRLCIEDLGQYRLALEWALIQFHSEKMEMINRLIREYWRKIYRGNDIDYIQVKTDEVSSDASADRRKTYNYRVVQSKNYSEIEMRGRCSAGQRVLASLIIRLALAETFSSNCGVLALDEPTTNLDRANINSLCEALNCIVEERQSQSNFMLIIITHDENFVSSLGKITSYHRVFRNEECKSVIRRVEAGPSKKALIDQ
Protein: LIM/homeobox protein lim-6 (Q21192)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Required for the terminal differentiation of sensory- and motor-neurons, especially GABAergic neurons, and for morphological aspects of uterine development. Plays a role in the cell-type-specific regulation of glutamic acid decarboxylase unc-25. Involved in promoting sleep-like behavioral quiescence, acting by modulating expression of transcription factor aptf-1 in the single sleep-active ring interneuron RIS. Plays a role in regulation of RIS differentiation. Required for the functional asymmetry of the ASER and ASEL chemosensory neuron pair, conferring the ability to discriminate sodium from chloride, perhaps by modulating expression of receptor-type guanylate cyclases, such as gcy-5. Involved in regulating postembryonic axon maintenance in the ventral nerve cord, acting in concert with LIM homeobox protein ceh-14, via modulation of expression of immunoglobulin domain zig genes in the interneuron PVT. May play a role in the functions of the excretory gland cell.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|RuleBase:RU000682}.
Interaction partners:
- COG-1A
- Transcription factor che-1
- High-affinity choline transporter 1
- Formin-homology and zinc finger domains protein 1
- Receptor-type guanylate cyclase gcy-5
- C2H2-type domain-containing protein
Sequence:
MERDCDIVDLDQPSLGTVISIKDGSTPTDISTTSSTTEDKLCSGCGCLIKDRYIYRVMEDSYHESCLRCSCCQLSLSSFKKCFSRHGNIYCEHDHQMLYGKRCRRCMTLLLPTDIVHRVHFMYYHAQCFSCCSCQRPFNLGDEYHVFDGEVFCRNDYQSICNFQTISNPDPLMEEVVRSEIHRKTPKRPRTILNAQQRRQFKTAFERSSKPSRKVREQLANETGLSVRVVQVWFQNQRAKIKKLNKKDSDSGDTFKHGPGSEGRSTEDIRSSDDEEESVINLDADEVETSETSSYTDPIQKLYNMTSSQIYFPYHS
Protein: Ribosomal protein uL24-like (60S ribosomal protein L26-like 1) (Large ribosomal subunit protein uL24-like 1) (Q9UNX3)
Organism: Homo sapiens (Human)
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL20
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL2
Sequence:
MKFNPFVTSDRSKNRKRHFNAPSHVRRKIMSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIHPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEELIEKMQE
Protein: L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L) (P30836)
Organism: Rattus norvegicus (Rat)
Function: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1378303}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Glycosylation-dependent cell adhesion molecule 1
- CD34 molecule
- Selectin P ligand
- P-selectin
- E-selectin
- CD44 antigen
- T-cell surface glycoprotein CD4
- Mucosal addressin cell adhesion molecule 1
- Vascular cell adhesion protein 1
- Intercellular adhesion molecule 1
Sequence:
MVFPWRCQSAQRGSWSFLKLWIRTLLCCDLLPHHGTHCWTYHYSERSMNWENARKFCKHNYTDLVAIQNKREIEYLEKTLPKNPTYYWIGIRKIGKTWTWVGTNKTLTKEAENWGTGEPNNKKSKEDCVEIYIKRERDSGKWNDDACHKRKAALCYTASCQPESCNRHGECVETINNNTCICDPGYYGPQCQYVIQCEPLKAPELGTMNCIHPLGDFSFQSQCAFNCSEGSELLGNAKTECGASGNWTYLEPICQVIQCMPLAAPDLGTMECSHPLANFSFTSACTFTCSEETDLIGERKTVCRSSGSWSSPSPICQKTKRSFSKIKEGDYNPLFIPVAVMVTAFSGLAFIIWLARRLKKGKKSQERMDDPY
Protein: AFG2-interacting ribosome maturation factor (Ribosome biogenesis protein C1orf109) (Q9NX04)
Organism: Homo sapiens (Human)
Function: Involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles. Acts together with SPATA5, SPATA5L1 and CINP.
Subcellular location: Nucleus {ECO:0000269|PubMed:22548824}. Cytoplasm {ECO:0000269|PubMed:22548824}.
Interaction partners:
- Cyclin-dependent kinase 2-interacting protein
- ATPase family gene 2 protein homolog B
- Solute carrier organic anion transporter family member 1A2
- Protein limb expression 1 homolog
- Pre-mRNA-splicing factor CWC25 homolog
- Protein associated with UVRAG as autophagy enhancer
- Phosphopentomutase
Sequence:
MTQDRPLLAVQEALKKCFPVVEEQQGLWQSALRDCQPLLSSLSNLAEQLQAAQNLRFEDVPALRAFPDLKERLRRKQLVAGDIVLDKLGERLAILLKVRDMVSSHVERVFQIYEQHADTVGIDAVLQPSAVSPSVADMLEWLQDIERHYRKSYLKRKYLLSSIQWGDLANIQALPKAWDRISKDEHQDLVQDILLNVSFFLEE
Protein: Extracellular signal-regulated kinase 1 (ERK1) (EC 2.7.11.24) (MAP kinase 1) (P42525)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Kinase involved in a signal transduction pathway.
Interaction partners:
- non-specific serine/threonine protein kinase
- Heat shock factor-type DNA-binding domain-containing protein
- Dual specificity mitogen-activated protein kinase kinase 1
- Tyrosine-protein phosphatase 2
- Exportin-1
- Patatin family protein
- Cyclin N-terminal domain-containing protein
- Uncharacterized protein
- Ras-like protein rasD
Sequence:
MEPEFDHFQSQMDSDNTHQSTMFNVQDNNAILMSGMENVLQSPRQLQAAAQAQQQAAAQAQQQQVQAQQVQAQQAQQQQQQQQNQQQQQQQQNQQNQQQQQNQQQQSQQMTQQQLQQLMPPPPTSDTSNFNDNISYFVYGSQFTVPRRYSIVKCIGHGAYGVVCSAKDNLTGEKVAIKKISKAFDNLKDTKRTLREIHLLRHFKHENLISIKDILKPNSKEQFEDVYIVSELMDTDLHQIITSPQPLSDDHCQYFVYQMLRGLKHIHSANVLHRDLKPSNLLINEDCLLKICDLGLARVEDATHQGFMTEYVATRWYRAPEVILSWNKYTKAIDIWSVGCIFAELLGRKPLFQGKDYIHQITLIIETIGSPSEEDICNIANEQARQFIRNMGNQPKVNFANMFPKANPDAIDLLERMLYFDPSKRLTVEEALAHPYFQSLHDPSDEPICLHKFSLNFEAWDLNRDLLKELIYNEMLAYHPEDPQAPYYTDLNNPNFNLSRIQSSSELFNLLQQQKQQIHQQVNQQSIKN
Protein: Catechol O-methyltransferase (EC 2.1.1.6) (P22734)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
Subcellular location: [Isoform Soluble]: Cytoplasm {ECO:0000269|PubMed:1765063}.; SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane {ECO:0000269|PubMed:1765063}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:1765063}.
Interaction partners:
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- UDP-glucuronosyltransferase
- Aromatic-L-amino-acid decarboxylase
- Cytochrome P450 1A1
- Dopamine beta-hydroxylase
- UDP-glucuronosyltransferase 1A1
- Phenylethanolamine N-methyltransferase
- Cytochrome P450 1B1
- UDP-glucuronosyltransferase 2B15
Sequence:
MPLAAVSLGLLLLALLLLLRHLGWGLVTIFWFEYVLQPVHNLIMGDTKEQRILRYVQQNAKPGDPQSVLEAIDTYCTQKEWAMNVGDAKGQIMDAVIREYSPSLVLELGAYCGYSAVRMARLLQPGARLLTMEMNPDYAAITQQMLNFAGLQDKVTILNGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEKCGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKVVDGLEKAIYQGPSSPDKS
Protein: Autophagy-related protein 8d (Autophagy-related ubiquitin-like modifier ATG8d) (AtAPG8d) (Protein autophagy 8d) (Q9SL04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8LEM4}.
Interaction partners:
- Protein NBR1 homolog
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy-related protein 3
- Cysteine protease ATG4b
- Cysteine protease ATG4a
- Autophagy-related protein 18b
- Serine/threonine-protein kinase ATG1a
- Serine/threonine-protein kinase ATG1b
- Ubiquitin-like protein ATG12A
- Autophagy-related protein 18h
Sequence:
MAISSFKHEHPLEKRQAEAARIREKYPDRIPVIVERAEKSDVPDIDRKKYLVPADLTVGQFVYVVRKRIKLSPEKAIFIFVKNILPPTAAIMSAIYEEHKDEDGFLYMSYSGENTFGIFF
Protein: NADH-ubiquinone oxidoreductase chain 3 (EC 7.1.1.2) (Q2F984)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion membrane {ECO:0000256|RuleBase:RU003640}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003640}.
Interaction partners:
Sequence:
MDNIFFGVYNARNGYESATVLQGIRIDLAINGYESAFLSEFAPICIYLVISPLVSLIPLGVPFPFASNSSTYPEKLSAYECGFDPSGDARSRFDIRFYPVPILFIIPDLEVTFFFPWAVPPNKIDLFGSWSMMAFLLILTIGFLYEWKRGASDRE
Protein: NADH dehydrogenase [ubiquinone] 1 subunit C2 (Complex I-B14.5b) (CI-B14.5b) (NADH-ubiquinone oxidoreductase subunit B14.5b) (Q9CQ54)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 beta subcomplex subunit 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MMNGRPGHEPLKFLPDEARSLPPPKLNDPRLVYMGLLGYCTGLMDNMLRMRPVMRAGLHRQLLFVTSFVFAGYFYLKRQNYLYAVKDHDMFGYIKLHPEDFPEKEKKTYAEILEPFHPVR
Protein: RS1 (Transcription regulator/activator ICP4) (Transcriptional regulator ICP4) (I1UYM4)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MASENKQRPGSPGPTDGPPPTPSPDRDERGALGWGAETEEGGDDPDHDPDHPHDLDDARRDGRAPAAGTDAGEDAGDAVSPRQLALLASMVEEAVRTIPTPDPAASPPRTPAFLADDDDGDEYDDAADAAGDRAPARGREREAPLRGAYPDPTDRLSPRPPAQPPRRRRHGRRRPSASSTSSDSGSSSSSSASSSSSSSDEDEDDDGNDAADHAREARAVGRGPSSAAPEAPGRTPPPPGPPPLSEAAPKPRAAARTPAASAGRIERRRARAAVAGRDATGRFTAGQPRRVELDADAASGAFYARYRDGYVSGEPWPGAGPPPPGRVLYGGLGDSRPGLWGAPEAEEARRRFEASGAPAAVWAPELGDAAQQYALITRLLYTPDAEAMGWLQNPRVVPGDVALDQACFRISGAARNSSSFITGSVARAVPHLGYAMAAGRFGWGLAHAAAAVAMSRRYDRAQKGFLLTSLRRAYAPLLARENAALTGAAGSPGAGADDEGVAAVAAAAPGERAVPAGYGAAGILAALGRLSAAPASPVGGDDPDAARHADADAGRRAQAGRVAVECLAACRGILEALAEGFDGDLAAVPGLAGARPASPPRPEGPAGPASPPPPHADAPRLRAWLRELRFVRDALVLMRLRGDLRVAGGSEAAVAAVRAVSLVAGALGPALPRDPRLPSSAAAAAADLLFENQSLRPLLAAAASAPDAADALAAAAASAAPREGRKRKSPGPARPPGGGGPRPPKTKKSGADAPGSDARAPLPAPPSTPPGPEPTPAQPAAARGAAAQARPRPVALSRRPAEGPDPLGGWRRQPRGPSHTAAPAAAALEAYCSPRAVAELTDHPLFPVPWRPALMFDPRALASIAARCAGPAPAAQAACGGDDDENPHPHGAAGGRLFGPLRASGPLRRMAAWMRQIPDPEDVRVVVLYSPLPGEDLAGGGASGGPPEWSAERGGLSCLLAALANRLCGPDTAAWAGNWTGAPDVSALGAQGVLLLSTRDLAFAGAVEFLGLLASAGDRRLIVVNTVRACDWPADGPAVSRQHAYLACDLLPAVQCAVRWPAARDLRRTVLASGRVFGPGVFARVEAAHARLYPDAPPLRLCRGGNVRYRVRTRFGPDTPVPMSPREYRRAVLPALDGRAAASGTTDAMAPGAPDFCEEEAHSHRACARWGLGAPLRPVYVALGREAVRAGPARWRGPRRDFCARALLEPDDDAPPLVLRGDDDDGPGALPPAPPGIRWASATGRSGTVLAAAGAVEVLGAEAGLATPPRRDVVDWEGAWDEDDGGAFEGDGVL
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (O77313)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
- Alpha-soluble NSF attachment protein, putative
- Thioredoxin-like protein, putative
- Sec1 family protein, putative
- SNARE protein, putative
- Syntaxin, Qa-SNARE family
- Syntaxin, Qa-SNARE family
- Syntaxin, Qa-SNARE family
- Protein transport protein SEC22
- SNARE protein, putative
- Syntaxin, Qa-SNARE family
Sequence:
MRTNLQCCKLQSQELALTNCGFINIGLYNNLKKSVKSNDVYSEVGNMVLILRGDGNIGREEIALNTCQREFSRIQLKELVEINILDKENKNDLVNFIPIDSIELEVNLFVKPDRLIEMEDEKLEDVFKKYFLNHILTKGQILALKYNDILLKCIVKDLKTADFDEIKRLNNSNNNNNNRNSSGFSGYFNKWSPGFNNADNQNLSYNRYERGILFENTECIFTSISDGGKLCIESKKVLKQNIIKNNFNFEELGIGALDEEFKTIFRRTFASRIYPNYIIKQLSIKHVKGMILYGPPGTGKTLIARQIGKTLNAREPKIINGPEILNKYVGQSEENIRNLFKDAEMEYKQSGENSLLHIIILDEIDAICRQRGNVGSSSTGVNDSVVNQLLSKIDGVNSLNNILLIGMTNRIDLIDEALLRPGRFELHIEISLPNKEGRIQILNIHTKNMRMSNKLSSDVNILELAERTPNFSGAEIEGLVRNTVSYAFERHINFNDLTKPINADDIMITKNDFMKALKETKPAFGAEEDIIGNLLCNGIINYGKEYENIENTCKLLIKQIVDNENTKLMSILLYGENGSGKTTISAYIAKCANFHFTKFITPENLIGYSEIGRINYINKIFEDAYKTPLSLVILDNIERLIDYTRIGPRFSNSILQAIMVLIKKKPKKENQKILIICTTSEYQFMKDVGLTKNFFVNIHVPLLSTSSSIKNVLQHRNQTYHDFPNNEIEKVISSNIIKNIAIKNLLMIIDMASEASDDKNITSDVFLKIFNDCGLLLDDDTDY
Protein: 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic (AtSBE II-2) (EC 2.4.1.18) (Branching enzyme 2) (AtBE2) (Starch-branching enzyme 2-2) (Q9LZS3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}. Plastid, amyloplast {ECO:0000250}.
Interaction partners:
- 4-alpha-glucanotransferase DPE2
- Starch synthase 3, chloroplastic/amyloplastic
- Alpha-glucan phosphorylase 2, cytosolic
- Alpha-glucan phosphorylase 1
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Starch synthase 1, chloroplastic/amyloplastic
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Probable starch synthase 4, chloroplastic/amyloplastic
- Alpha-amylase 3, chloroplastic
- Starch synthase 2, chloroplastic/amyloplastic
Sequence:
MVVIHGVSLTPRFTLPSRPLNTGFNAGNSTLSFFFKKHPLSRKIFAGKQSAEFDSSSQAISASEKVLVPDNLDDDPRGFSQIFDLESQTMEYTEAVRTEDQTMNVVKERGVKPRIVPPPGDGKKIYEIDPMLRTYNNHLDYRYGQYKRLREEIDKYEGGLEAFSRGYEKLGFSRSDAGITYREWAPGAKAASLIGDFNNWNSNADIMTRNEFGVWEIFLPNNTDGSPAIPHGSRVKIRMDTPSGIKDSIPAWIKFSVQAPGEIPFNGIYYDPPEEEKYVFKHPQPKRPKSLRIYEAHVGMSSTEPMVNTYANFRDDVLPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRCGTPEELKSLIDRAHELGLVVLMDIVHSHASKNTLDGLNMFDGTDAHYFHSGPRGYHWMWDSRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLSVGFTGNYTEYFGLETDVDAVNYLMLVNDMIHGLYPEAITVGEDVSGMPTFCIPVQDGGVGFDYRLHMAIADKWIEMLKKRDEDWQMGDIIYTLTNRRWSEKCISYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRPSTPLIDRGIALHKMIRLITMGLGGEGYLNFMGNEFGHPEWIDFPRGEQRLSDGSVIPGNNFSYDKCRRRFDLGDADYLRYRGLQEFDQAMQHLEENYGFMTSEHQFISRKDEADRVIVFERGDLVFVFNFHWTSSYFDYRIGCSKPGKYKIVLDSDDPLFGGFNRLDRKAEYFTYDGLYDERPCSFMVYAPCRTAVVYALANHD
Protein: Beta-galactoside alpha-2,6-sialyltransferase 2 (Alpha 2,6-ST 2) (EC 2.4.3.1) (CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2) (ST6Gal II) (ST6GalII) (hST6Gal II) (Sialyltransferase 2) (Q96JF0)
Organism: Homo sapiens (Human)
Function: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. Has alpha-2,6-sialyltransferase activity toward oligosaccharides that have the Gal-beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate groups, but it has weak or no activities toward glycoproteins and glycolipids.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 3
- Beta-galactoside alpha-2,6-sialyltransferase 1
Sequence:
MKPHLKQWRQRMLFGIFAWGLLFLLIFIYFTDSNPAEPVPSSLSFLETRRLLPVQGKQRAIMGAAHEPSPPGGLDARQALPRAHPAGSFHAGPGDLQKWAQSQDGFEHKEFFSSQVGRKSQSAFYPEDDDYFFAAGQPGWHSHTQGTLGFPSPGEPGPREGAFPAAQVQRRRVKKRHRRQRRSHVLEEGDDGDRLYSSMSRAFLYRLWKGNVSSKMLNPRLQKAMKDYLTANKHGVRFRGKREAGLSRAQLLCQLRSRARVRTLDGTEAPFSALGWRRLVPAVPLSQLHPRGLRSCAVVMSAGAILNSSLGEEIDSHDAVLRFNSAPTRGYEKDVGNKTTIRIINSQILTNPSHHFIDSSLYKDVILVAWDPAPYSANLNLWYKKPDYNLFTPYIQHRQRNPNQPFYILHPKFIWQLWDIIQENTKEKIQPNPPSSGFIGILIMMSMCREVHVYEYIPSVRQTELCHYHELYYDAACTLGAYHPLLYEKLLVQRLNMGTQGDLHRKGKVVLPGFQAVHCPAPSPVIPHS
Protein: FI03239p (FI04819p) (LD45662p) (MIP35121p1) (Uncharacterized protein CG1677) (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Q9W3R9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- sn-1-specific diacylglycerol lipase ABHD11
- GH24548p
Sequence:
MVLDMESDDSHASSASNSSESRSNSPTNDKDEVVADHGGESPGGGGDPILDRSDRAPSTSSSSSNSSSSSNRSDLSKKQKKSSSSSSGSGSGSGSSSSSGSSSEDEGDQEPEQEVQRLSEQQREQQQHSPINERESESAAGTPVNADQPGSPNAKSQPSSFLSSVRSRSVSPQLYNQAAVDLNISHDDLSDVSDIEGEEKRTSSKNSMRPADENEDGAISNDSLPTLGEEDEVEQKQSTPNGKASSGDEKEPFAKETHTDDASNGLAPATALQEDLVKTHDDDALDFEAEEGECPEQAKEPSPMESTANETNQTKSTTKVSQDEGDDDGEVDKDGDDKDGDDKDTRKDGAGNGCLEDGAGNDSRKDDAGNGCLEEGEEEKDIVSVSTSSSQEKVEEGELEEGEVSDEDEKRPEETEPKPVCRFYTRGQCTWGMSCRFLHPGVTDKGNYTMFDNVIRPVPMQGGSTGASAPAAPSSTAAPRAGGSAYSSHASATADYHDYRTERPLHHRPPLLHAPSIYGAPVHDARTLLPDGAPVVVENAWERGLRTAKEMMRKANKRKEQDMDFEDKKMNLTLSPDEMEKDSYYLKDRGGSSARSPPPPSANVREQPLNPLSMPLSMHPHAVAHANPRALLPLQYSVYGPPPDRYGRPQYMPPQYDDVDAYGRMTRYRELPPHRMPHYEDDRRSRPTREVIVQRVEAAGRGDEWSDPWMRSKSVGRGSYEREDRRRRDRRSYSSNSSYSTSNSSQSDSSSDSSRSSSPSDHKRRYGSHKLATATATSRRHGGRAARSPSQIPRRPRRTSKGSLSPSYKRPAVDKRGVGHSPSSKRKKLSSPAPKKFDKLRRRRSSSSSDSDSSDTSYSDSESGSSSSDSSSGSRETPQKRVRATDKALNERKLISKPAEQSTKKRSPISIEIKKTSNMVGVSALASASNSADSDAEKDHDNGKDKEKDHVKEKDKDCKEKDKDKDGMKDKEGKKSRREELLKQLRAVEDAIAKKRSKLN
Protein: Antizyme inhibitor 1 (AZI) (AZI1) (Ornithine decarboxylase antizyme inhibitor) (O14977)
Organism: Homo sapiens (Human)
Function: Antizyme inhibitor (AZI) protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake. AZI is an enzymatically inactive ODC homolog that counteracts the negative effect of ODC antizymes (AZs) OAZ1, OAZ2 and OAZ3 on ODC activity by competing with ODC for antizyme-binding. Inhibits antizyme-dependent ODC degradation and releases ODC monomers from their inactive complex with antizymes, leading to formation of the catalytically active ODC homodimer and restoring polyamine production.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35484}.
Interaction partners:
- Ornithine decarboxylase antizyme 1
- Ornithine decarboxylase antizyme 3
- Ornithine decarboxylase antizyme 2
- Alpha-aminoadipic semialdehyde synthase, mitochondrial
- Spermine synthase
- Spermidine synthase
- Kinesin light chain 1
- Guanidino acid hydrolase, mitochondrial
- Phenazine biosynthesis-like domain-containing protein
Sequence:
MKGFIDDANYSVGLLDEGTNLGNVIDNYVYEHTLTGKNAFFVGDLGKIVKKHSQWQNVVAQIKPFYTVKCNSAPAVLEILAALGTGFACSSKNEMALVQELGVPPENIIYISPCKQVSQIKYAAKVGVNILTCDNEIELKKIARNHPNAKVLLHIATEDNIGGEEGNMKFGTTLKNCRHLLECAKELDVQIIGVKFHVSSACKESQVYVHALSDARCVFDMAGEIGFTMNMLDIGGGFTGTEFQLEEVNHVISPLLDIYFPEGSGVKIISEPGSYYVSSAFTLAVNIIAKKVVENDKFPSGVEKTGSDEPAFMYYMNDGVYGSFASKLSEDLNTIPEVHKKYKEDEPLFTSSLWGPSCDELDQIVESCLLPELNVGDWLIFDNMGADSFHEPSAFNDFQRPAIYYMMSFSDWYEMQDAGITSDSMMKNFFFVPSCIQLSQEDSFSAEA