wanglab/gogpt-training-data huggingface dataset:
Protein: Dolichol-phosphate mannosyltransferase subunit 1 (EC 2.4.1.83) (Dol-P-Man synthase1) (Dolichol-phosphate mannose synthase subunit 1) (DPM synthase subunit 1) (Q9LM93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex. Plays a role in plant development and physiology, sensitivity to ammonium stress and endoplasmic reticulum stress response.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21558543}; Peripheral membrane protein {ECO:0000305|PubMed:21558543}. Note=Anchored to the ER membrane by DPMS2 and DPMS3 of the dolichol-phosphate mannose (DPM) synthase complex. {ECO:0000305|PubMed:21558543}.
Interaction partners:
- Dolichol-phosphate mannose synthase subunit 2
- Dol-P-Man:Man
- Dolichol-phosphate mannose synthase subunit 3
- dolichyl-phosphate beta-glucosyltransferase
- UDP-glycosyltransferase TURAN
- Dol-P-Glc:Glc
- Dolichol kinase EVAN
- Mannose-1-phosphate guanylyltransferase 1
- At3g57220
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Sequence:
MADEMETKGEKKYKYSIIIPTYNERLNIAIIVYLIFKHLRDVDFEIIVVDDGSPDGTQEIVKQLQQLYGEDRILLRARAKKLGLGTAYIHGLKHATGDFVVIMDADLSHHPKYLPSFIKKQLETNASIVTGTRYVKGGGVHGWNLMRKLTSRGANVLAQTLLWPGVSDLTGSFRLYKKSALEDVISSCVSKGYVFQMEMIVRATRKGYHIEEVPITFVDRVFGTSKLGGSEIVEYLKGLVYLLLTT
Protein: Flavin-containing monooxygenase 5 (FMO 5) (Dimethylaniline monooxygenase [N-oxide-forming] 5) (EC 1.14.13.8) (Dimethylaniline oxidase 5) (Hepatic flavin-containing monooxygenase 5) (NADPH oxidase) (EC 1.6.3.1) (Q8K4C0)
Organism: Rattus norvegicus (Rat)
Function: Acts as Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity (By similarity). Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects (By similarity).
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:P49326}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49326}.
Interaction partners:
Sequence:
MAKKRIAVIGSGASGLTCIKCCLEEGLEPVCFERSDDIGGLWRYQENPEKGRASIYKSVIINTSKEMMCFSDYPIPDHYPNFMHNSQVLEYFRMYAKEFGLLKYIQFKTTVCSVKKQPDFSTSGQWQVVTEHEGKQQVDVFDGVLVCTGHHTDPHLPLDSFPGIEKFKGKYFHSREYKNPVEFTGKRVIVIGIGNSGGDLAVEISHTAKQVFLSTRRGAWILNRVGKRGYPIDILLSSRITNYLSKICGSALKNRYMEKQLNQRFDHEMFGLKPKHSALGQHPTINDDLPNRIISGLVKVKGNVKEFTETAAIFEDGSREDDIDVVIFATGYSFAFPFLEDSVKVVQNKVSLYKKVFPPNLEKPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKKLPSQSEMMAEINKTREEMAKRYVDSQRHTIQGDYIDTMEEIADLVGVRPNLLSLAFTDPKLAFQLLVGPCTPVQYRLQGPGKWAGARKTILTTEDRIRKPLMTRVVERDSSGTSLVTVRVLMLAVTFLAVILAYF
Protein: Small ribosomal subunit protein uS13 (C3SR52)
Organism: Escherichia coli
Interaction partners:
Sequence:
MARIAGINIPDHKHAVIALTSIYGVGKTRSKAILAAAGIAEDVKISELSEGQIDTLRDEVAKFVVEGDLRREISMSIKRLMDLGCYRGLRHRRGLPVRGQRTKTNARTRKGPRKPIKK
Protein: Uncharacterized membrane protein At4g09580 (Q8L586)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAAPRNLTGDGGARQLVKDEESPAASSAAKGLLNDDSPTGKRTKSERFPLSRWEFAVFFTVFLVFTTGLFCIYLTMPAAEYGKLKVPRTISDLRLLKENLGSYASEYQARFILGYCSTYIFMQTFMIPGTIFMSLLAGALFGVVRGFVLVVLNATAGACSCFFLSKLVGRPLVNWLWPEKLRFFQAEIAKRRDRLLNYMLFLRITPTLPNLFINLSSPIVDIPFHVFFLATLVGLMPASYITVRAGLALGDLRSVKDLYDFKTLSVLFLIGSISIFPALLKRKRVYE
Protein: Nuclear receptor subfamily 4 group A member 1 (NUR77) (Nerve growth factor-induced protein I-B) (NGFI-B) (Orphan nuclear receptor HMR) (P22829)
Organism: Rattus norvegicus (Rat)
Function: Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'. May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation (By similarity). Plays a role in the vascular response to injury (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:8227042}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22736}. Mitochondrion {ECO:0000250|UniProtKB:P22736}. Note=Nuclear export to the cytosol is XPO1-mediated and positively regulated by IFI27. Translocation to the mitochondrion upon interaction with RXRA and upon the presence of 9-cis retinoic acid (By similarity). {ECO:0000250|UniProtKB:P22736}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Retinoic acid receptor RXR-alpha
- RAC-alpha serine/threonine-protein kinase
- Mitogen-activated protein kinase 3
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Mitogen-activated protein kinase 7
- Mitogen-activated protein kinase 1
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
Sequence:
MPCIQAQYGTPATSPGPRDHLTGDPLALEFSKPTMDLASPETAPTAPATLPSFSTFMDGGYTGEFDTFLYQLPGTAQPCSSASSTSSSSSSATSPASASFKFEDFQVYGCYPGTLSGPLDETLSSSGSDYYGSPCSAPSPPTPNFQPSQLSPWDGSFGHFSPSQTYEGLRVWTEQLPKASGPPPPPTFFSFSPPTGPSPSLAQSSLKLFPAPATHQLGEGESYSVPAAFPGLAPTSPNCDTSGILDAPVTSTKARSGSSGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKSAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPTNLLTSLIRAHLDSGPNTAKLDYSKFQELVLPRFGKEDAGDVQQFYDLLSGSLDVIRKWAEKIPGFIELSPGDQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHRLQCARGFGDWIDNILAFSRSLHSLGVDVPAFACLSALVLITDRHGLQDPRRVEELQNRIASCLKEHMAAVAGDPQPASCLSRLLGKLPELRTLCTQGLQRIFCLKLEDLVPPPPIVDKIFMDTLSF
Protein: AKT1 substrate 1 (D3ZH75)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Regulatory-associated protein of mTOR
- DEP domain-containing mTOR-interacting protein
- Target of rapamycin complex subunit LST8
- GTP-binding protein Rheb
- RAC-alpha serine/threonine-protein kinase
- Ribosomal protein S6 kinase beta-1
- RPTOR independent companion of MTOR, complex 2
- TELO2-interacting protein 1 homolog
- RAC-beta serine/threonine-protein kinase
Sequence:
MASGRPEELWEAVVGAAERFRARTGTELVLLTAAPPPPPRPGPCAYAAHGRGALAEAARRCLHDIAQAHRAATATRPPGPPPAPQPPSPAPSSPPRPALAREEDEEDEDEPTETETSGERLGGSDNGGLFMMDEDATLQDLPPFCESDPESTDDGSLSEETPAGPPAYPKLPATSKLSEGQLRFLPSNRSFARTALTRGPRAEPSCGSWLCSASVRRVASFRSRVPLSDWSRPPGSVAKPSLTQNWPEALYFLHY
Protein: DNA polymerase (EC 2.7.7.7) (Q2KNE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000442}.
Interaction partners:
Sequence:
MDFKRRNGGPAMGGASQAKKGKPSTEWEDSPSQFEEELALFDEMDMEVESGEGQAGHDVIPVGDLFSTDLNPRWKRPHASPLHPKSDTLIFQQIDLDYYLGAAVAGMPGQVQGKVPIVRMFGVTDNGNSVCCHIHGFAPYFYVPAPNGFTNAHLAGFQRELNSVVLKDMRSNKDNIAVTVLAVDITKKESMYNYHGNKPHDFLRITMAMPRLVAPAKRLLEQGFKFANFATQSYQAFEANIDFEIRFMVDSNVVGCCWIELPKGKYQLREERREGQTDSKYPGKVSLCQYEVDVAWDSLISHPAEGEWQRIAPLRVLSFDIECAGRKGVFPEPEVDPVIQIASMVQRQGEKEPFIRTVFTLQSCASIVGSQILCFTQEKLMLQSWAEFMRTVDPDIITGYNIQNFDLPYLLNRAATLKVNMFPYLGRVWGCKSVLKDSSFQSKQMGRRENKTINMEGRVQFDLLQVLLRDYKLRSYTLNAVSFHFLQEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAYLPLRLLQKLMCVINYMEMARVTGVPLTYLLSRGQQIKVVSQLLRQAMKQDLVMPVVKTEGGEDYTGATVIEPEKGYYSVPIATLDFSSLYPSIMMAHNLCYTTLLQKSQIEKLGLGPDDFIKTPTGDLFVKSSVRKGLLPEILENLLSARKRAKAELKKETDPFKKQVLDGRQLALKISANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEQTKQLVESRYTLDNGYQADAKVIYGDTDSVMVKLGVATVQEAMNQGKEAAEWVSSHFVPPIKLEFEKVYYPYLLINKKRYAGLYFSSSAEHHDKMDCKGIETVRRDNCPLVANLINTCLQNILIDRDPDGAVTHAKEVISDLLCNRIDISQLVITKELTRTAQEYAGKQAHVELAERMRKRDAGSAPNLGDRVPYVIIKAAKGVAAYMKSEDPIYVLENNIPIDTQYYLEQQLSKPLLRIFEPILGESKAESVLLKGDHTRCKTVLTSRVGGLMAFAQKRSTCIGCRAVLKTDVAVCDFCKKRESELYQKEIAHLSTLEEKFSRLWTQCQRCQGSLHEDVLCTSRDCPIFYMRKKVQKDLDDQEKLVSRFGW
Protein: ELKS/Rab6-interacting/CAST family member 1 (ERC-1) (CAZ-associated structural protein 2) (CAST2) (Rab6-interacting protein 2) (Q811U3)
Organism: Rattus norvegicus (Rat)
Function: Regulatory subunit of the IKK complex. Probably recruits IkappaBalpha/NFKBIA to the complex (By similarity). May be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. May be involved in vesicle trafficking at the CAZ. May be involved in Rab-6 regulated endosomes to Golgi transport.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8IUD2}. Cytoplasm {ECO:0000269|PubMed:12391317}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Presynaptic active zone {ECO:0000269|PubMed:12391317}. Cell projection, podosome {ECO:0000250|UniProtKB:Q99MI1}. Note=Recruited on Golgi membranes by RAB6A in a GTP-dependent manner. Localized to the cortex of myotube podosomes (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q99MI1}.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 1
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B essential modulator
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Regulating synaptic membrane exocytosis protein 2
- Protein unc-13 homolog A
- Liprin-alpha-3
- Ras-related protein Rab-3A
- Ras-related protein Rab-6A
- PTPRF interacting protein alpha 1
Sequence:
MYGSARSVGKVEPSSQSPGRSPRLPRSPRLGHRRTNSTGGSSGNSVGGGSGKTLSMENIQSLNAAYATSGPMYLSDHENVGAETPKSTMTLGRSGGRLPYGVRMTAMGSSPNIASSGVASDTIAFGEHHLPPVSMASTVPHSLRQARDNTIMDLQTQLKEVLRENDLLRKDVEVKESKLSSSMNSIKTFWSPELKKERALRKDEASKITIWKEQYRVVQEENQHMQMTIQALQDELRIQRDLNQLFQQDSSSRTGEPCVAELTEENFQRLHAEHERQAKELFLLRKTLEEMELRIETQKQTLNARDESIKKLLEMLQSKGLSAKATEEDHERTRRLAEAEMHVHHLESLLEQKEKENNMLREEMHRRFENAPDSAKTKALQTVIEMKDSKISSMERGLRDLEEEIQMLKSNGALSTEEREEEMKQMEVYRSHSKFMKNKIGQVKQELSRKDTELLALQTKLETLTNQFSDSKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKETMLNKKTKQIQDMAEEKGTQAGEIHDLKDMLDVKERKVNVLQKKIENLQEQLRDKEKQMSSLKERVKSLQADTTNTDTALTTLEEALADKERTIERLKEQRDRDEREKQEEIDTYKKDLKDLKEKVSLLQGDLSEKEASLLDLKEHASSLASSGLKKDSRLKTLEIALEQKKEECLKMESQLKKAHEATLEARASPEMSDRIQQLEREIARYKDESSKAQTEVDRLLEILKEVENEKNDKDKKIAELESLTSRQVKDQNKKVANLKHKEQVEKKKSAQMLEEARRREDSLSDSSQQLQVEELLMAMEKVKQELESMKAKLSSTQQSLAEKETHLTNLRAERRKHLEEVLEMKQEALLAAISEKDANIALLELSSSKKKTQEEVAALKREKDRLVQQLKQQTQNRMKLMADNYEDDHFRSSRSNQTNHKPSPDQDEEEGIWA
Protein: Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform (PP2A-alpha) (EC 3.1.3.16) (P63331)
Organism: Rattus norvegicus (Rat)
Function: PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (By similarity). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase (By similarity). Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate p53/TP53 (By similarity). Activates RAF1 by dephosphorylating it at 'Ser-259' (By similarity). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (By similarity). Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis: interaction with AMBRA1 enhances interaction between PPP2CA and MYC (By similarity). Mediates dephosphorylation of FOXO3; promoting its stabilization: interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3 (By similarity). Catalyzes dephosphorylation of the pyrin domain of NLRP3, promoting assembly of the NLRP3 inflammasome (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P67775}. Nucleus {ECO:0000250|UniProtKB:P67775}. Chromosome {ECO:0000250|UniProtKB:P67775}. Chromosome, centromere {ECO:0000250|UniProtKB:P67775}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:P67775}. Note=In prometaphase cells, but not in anaphase cells, localizes at centromeres. During mitosis, also found at spindle poles (By similarity). Centromeric localization requires the presence of SGO2 (By similarity). Recruited to chromatin and transcription pause-release checkpoint via its association with the Integrator complex (By similarity). {ECO:0000250|UniProtKB:P63330, ECO:0000250|UniProtKB:P67775}.
Interaction partners:
- Protein phosphatase 2 scaffold subunit A alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Immunoglobulin-binding protein 1
- Immunoglobulin
- Mitogen-activated protein kinase 1
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MDEKLFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL
Protein: Neural cell adhesion molecule 1 (H7BYX6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLQTKDLIWTLFFLGTAVSLQVDIVPSQGEISVGESKFFLCQVAGDAKDKDISWFSPNGEKLTPNQQRISVVWNDDSSSTLTIYNANIDDAGIYKCVVTGEDGSESEATVNVKIFQKLMFKNAPTPQEFREGEDAVIVCDVVSSLPPTIIWKHKGRDVILKKDVRFIVLSNNYLQIRGIKKTDEGTYRCEGRILARGEINFKDIQVIVNVPPTIQARQNIVNATANLGQSVTLVCDAEGFPEPTMSWTKDGEQIEQEEDDEKYIFSDDSSQLTIKKVDKNDEAEYICIAENKAGEQDATIHLKVFAKPKITYVENQTAMELEEQVTLTCEASGDPIPSITWRTSTRNISSEEKTLDGHMVVRSHARVSSLTLKSIQYTDAGEYICTASNTIGQDSQSMYLEVQYAPKLQGPVAVYTWEGNQVNITCEVFAYPSATISWFRDGQLLPSSNYSNIKIYNTPSASYLEVTPDSENDFGNYNCTAVNRIGQESLEFILVQADTPSSPSIDQVEPYSSTAQVQFDEPEATGGVPILKYKAEWRAVGEEVWHSKWYDAKEASMEGIVTIVGLKPETTYAVRLAALNGKGLGEISAASEFKTQPVREPSAPKLEGQMGEDGNSIKVNLIKQDDGGSPIRHYLVRYRALSSEWKPEIRLPSGSDHVMLKSLDWNAEYEVYVVAENQQGKSKAAHFVFRTSAQPTAIPATLGGNSASYTFVSLLFSAVTLLLLC
Protein: Endoglucanase Cel12A (EC 3.2.1.4) (Cellulase) (Endo-1,4-beta-glucanase) (P84196)
Organism: Gloeophyllum trabeum (Brown rot fungus) (Agaricus trabeus)
Function: Has carboxymethylcellulase activity.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:15870328}.
Interaction partners:
Sequence:
GVQISQISSFPTTADVSYDFNITNALGGIQPVGSLK
Protein: Elongation factor Tu, mitochondrial (EF-Tu) (EC 3.6.5.3) (P43) (P49411)
Organism: Homo sapiens (Human)
Function: Promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Also plays a role in the regulation of autophagy and innate immunity. Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway. In turn, inhibits RLR-mediated type I interferon while promoting autophagy.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22749352}.
Interaction partners:
- Small ribosomal subunit protein uS7m
- Elongation factor Ts, mitochondrial
- Large ribosomal subunit protein bL9m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
Sequence:
MTTMAAATLLRATPHFSGLAAGRTFLLQGLLRLLKAPALPLLCRGLAVEAKKTYVRDKPHVNVGTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAARHYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYVNKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLLDAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIRTVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILSKEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQRFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG
Protein: Cytochrome P450 71A20 (EC 1.14.-.-) (Q9T0K2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEMILITLCLTTLLALLLKSILKRTATKNFNLPPSPWRLPVIGNLHQLSLHTHRSLRSLSLRYGPLMLLHFGRTPVLIVSSADVAHDVMKTHDLVCANRPKTKVVDKILSGGRDVAFAPYGEYWRQMKSICIQNLLNNKMVRSYEKIREEEIKRMIEKLEKASCSSSPSPVNLSQILMTLTNDIICRVALGRKYSGKKDGIDVENIVRTFAALLGEFPVGEYIPSLSWIDRIRGLDHKMEVVDKRFDEFLERVVKEHEEADKETRSDLVDKLLTIQSDKTGQFELEKSALKLIIWDMFLAGTATTLSFLEWAMTELMRNPKVMKKLQEEIRSSSPQDLFVTEKEAEKMNYLQAVIKEALRLRPPAPLLVPRVLSEDVKLKGYNIPAGTQVIVNAWAIQRDTTTWGTDAEEFKPERHLDTNLDFQGQDFKFIPFGSGKRICPGIGFTSALIGVTLANIVKRFNWRMDVEPQRVQHDLTEATGLVVFRKFPLIAIPSSA
Protein: Heterogeneous nuclear ribonucleoprotein U like 1 (cDNA FLJ56481, highly similar to Heterogeneous nuclear ribonucleoprotein U-like protein 1) (B7Z4B8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRSWAFSYLDAMDNITRQNQFYDTQVIKQENESGYERRPLEMEQQQAYRPEMKTEMKQGAPTSFLPPEASQLKPDRQQFQSRKRPYEENRGRGYFEHREDRRGRSPQPPAEEDEDDFDDTLVAIDTYNCDLHFKVARDRSSGYPLTIEGFAYLWSGARASYGVRRGRVCFEMKINEEISVKHLPSTEPDPHVVRIGWSLDSCSTQLGEEPFSYGYGGTGKKSTNSRFENYGDKFAENDVIGCFADFECGNDVELSFTKNGKWMGIAFRIQKEALGGQALYPHVLVKNCAVEFNFGQRAEPYCSVLPGFTFIQHLPLSERIRGTVGPKSKAECEILMMVGLPAAGKTTWAIKHAASNPSKKYNILGTNAIMDKMRVMGLRRQRNYAGRWDVLIQQATQCLNRLIQIAARKKRNYILDQTNVYGSAQRRKMRPFEGFQRKAIVICPTDEDLKDRTIKRTDEEGKDVPDHAVLEMKANFTLPDVGDFLDEVLFIELQREEADKLVRQYNEEGRKAGPPPEKRFDNRGGGGFRGRGGGGGFQRYENRGPPGGNRGGFQNRGGGSGGGGNYRGGFNRSGGGGYSQNRWGNNNRDNNNSNNRGSYNRAPQQQPPPQQPPPPQPPPQQPPPPPSYSPARNPPGASTYNKNSNIPGSSANTSTPTVSSYSPPQPSYSQPPYNQGGYSQGYTAPPPPPPPPPAYNYGSYGGYNPAPYTPPPPPTAQTYPQPSYNQYQQYAQQWNQYYQNQGQWPPYYGNYDYGSYSGNTQGGTSTQ
Protein: Uncharacterized protein (G3XD37)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type III secretion chaperone SycN
- Uncharacterized protein
- Type III secretion outer membrane protein PopN
- Type III secretory apparatus protein PcrD
- Type III secretion system effector delivery regulator TyeA domain-containing protein
- Regulator in type III secretion
- Regulatory protein PcrH
- Type III secretion protein PcrV
- Translocation protein in type III secretion
- Translocation protein in type III secretion
Sequence:
MSRVGAWHIGIERLDLAHAEPFAPPLPERHLLAPDGRPVETHVASLYPAQQAQQRLFDYARPQLEFHGLLRPGDFRQALRDLRLALTLPRQPALQAAACLLGERDEDERLLQMALNLLHKV
Protein: Protein MON2 (P48563)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for traffic between late Golgi and early endosomes. Required for endocytosis and maintenance of vacuolar structure.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:16219684, ECO:0000269|PubMed:16301316}; Peripheral membrane protein {ECO:0000269|PubMed:12052896, ECO:0000269|PubMed:16219684, ECO:0000269|PubMed:16301316}. Note=Late Golgi.
Interaction partners:
- Protein DOP1
- Phospholipid-transporting ATPase NEO1
- ADP-ribosylation factor-like protein 1
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- Scramblase ANY1
- ADP-ribosylation factor-like protein 3
- Guanine nucleotide exchange factor subunit RIC1
- Phospholipid-transporting ATPase accessory subunit CDC50
- Sorting nexin-3
Sequence:
MAMNTGGFDSMQRQLEAELRSLSSESKRRNSTIRHASDKSIEILKRVHSFEELERHPDFALPFVLACQSRNAKMTTLAMQCLQGLSTVPSIPRSRLSEILDAFIEATHLAMEIQLKVLQVVPIFFKTYGKFIYGPLCKKLLLCCSNLLHVPNKAPVVVGTASATLQQLIDEIFDRLSIESVVDDKQYEVLISNSESIKVNVYRYDANKLFDNICSLNEISSNGAVSDEEMLLDIGDIPIDYGLEILESILKNSQKNLLECQDLQYLLRVKAIPLLLRCISSSRHFSTAVRSCRCLKLLIRKEYLSILELELEVILSLLIHGISVESNLSGWQRVLSLELFKDLSQDPEIVNTLYMDYDNYPDKKHVFKYLLKECIVLLNSPEYITFLAPSKVVEKMDSPLITTENSTVKTKFMHLLDKSNAPSINITYIISLILTICNHLCEGLNKSALESSPLEKKIEDKEREEGTGNDSTVVKVYSGLFSGLFELNKLFLYSTSLETSIFHLVVRAFQKLAHSAGVLSLKDKLRACMKLFSILITNNVTSSNQYSFNDTSKSAKNQHTRNISTSSVTTSPVESTKNPSRSIADSAQNKEMKRRLHPRNISSRQVSLLRALISLSISLGPIFDSESWRYTFLTWQWITYYIYGPSADFKESFYSEDIPPPPILTKSDVTSIESSLTKFFESTSSYSCSTFHLVLTRLILDSKNTLTLEQTNLNLNNDIGYHPLDAKDEIIPCIYNKAFFVNKIGELATYNCKKFLFGKNGKELWSLISTYMIKLISNREMDNDSLRLYTVRVFTDIIKKATNEVGNSDEQDNKVKQFGTLENLVIDSLMATINSIKQLDIGKQEIYNGTINVESDILFQLLLTLKEILNEFGELLMNSWTNIFNIINSPFEWTVEDTDFSVNEDIDDSSLFEGIVQKHKNMIQVSYDVFKLISDDFLQSLPMSVIKFVIDTLVNFVSQKRNLNISFSSISQFWLVGDYLRVRFNPETLNLSDEKRRSLSEKINNQKLIEIITSSSSHDWELYNGLWIYLLKNLINCTNDDRVEVKNGAVQTFFRIIDSHSVCFPPWDLIFLEVIEPLLTKEWSTEELENETDFINVTLQGLIKLYPEHFKDFKNNTTCAKEWSMLLDFLKRLLSSTSNNTKNAVILNYQTLLKEIITIEDVPSDILKKCCEIFTDYNITYSDLSTNASSKTEYDCIYELITGFPPLYQLISKYDAMTDEFVEKVLLLFNSAIKYPLLPEFVQDKTKPSSMQKAILSGLDIFMTNDSKDTEILILLQLSTISILAFDTREKITKKLGPKLPKASLNRLPTFEAISYMSCSNLRNRIAKIDQFGISTLKAKHILRILKNLAEIIKRKSLITGSESDEIPIWVLASNCFCDLSNKIFKSLQEDAENPLKDNFCDLFINVIVVTLQRINPELDNLTEIDDLNEYSKYREILLENRIIDLFNERQLDTFIYAVWDCSFLYEFDELENALMQDCGTFSELSQKLSSFDFSCIFGSTTNPRFQTKYKCSLECLQDLVNFMLNTNEKLRKLTAPYLSARIALALRRYISDEYLIGRAPIPKLRKTELATLLNGLCVILRGVLDQNSTLGNKQIGVENLQTLSPLILRTIPVSHKMDGLQDKVLELSLGFTKLD
Protein: UDP-glucose 4-epimerase (EC 5.1.3.2) (UDP-galactose 4-epimerase) (E8MF10)
Organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)
Function: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. Can also epimerize UDP-GalNAc to UDP-GlcNAc. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria.
Interaction partners:
Sequence:
MTTVLVTGGAGFIATHTDIELLNKGYDVISVDNYGNSSPVALERVEQITGKPVKRYDGDVRDEALMERVFAENNIDWVIHFAGLKAVGESVAKPIEYYDNNLYSTLVLLKVMKKHNVKKIIFSSSATVYGTPKELPITEETPTGGTTNPYGTSKLFQEQILRDVHVADPSWTIVLLRYFNPVGAHESGLLGEDPKGIPANLTPYVAKVAVGELKEVQVYGDDYDTPDGTGVRDYIHVVDLAKGHVAVIDHIDKEGVFVYNLGTGHGYSVLEVIKAYEKAAGHPIPYAIKPRRPGDIAACYADASKAEKELGWKAELTIDDMAASSLNWQTKNPNGFRDAE
Protein: Negative elongation factor complex member E (A0A0A0MT02)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDP
Protein: Creatine kinase S-type, mitochondrial (EC 2.7.3.2) (Basic-type mitochondrial creatine kinase) (Mib-CK) (Sarcomeric mitochondrial creatine kinase) (S-MtCK) (P17540)
Organism: Homo sapiens (Human)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Interaction partners:
- Guanidinoacetate N-methyltransferase
- Creatine kinase M-type
- Creatine kinase U-type, mitochondrial
- Non-selective voltage-gated ion channel VDAC1
- Myoglobin
- Non-selective voltage-gated ion channel VDAC2
- Non-selective voltage-gated ion channel VDAC3
- L-lactate dehydrogenase A-like 6A
- L-lactate dehydrogenase A-like 6B
- Myozenin-2
Sequence:
MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKHNNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPACTRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHVRIPKLSKDPRFSKILENLRLQKRGTGGVDTAAVADVYDISNIDRIGRSEVELVQIVIDGVNYLVDCEKKLERGQDIKVPPPLPQFGKK