wanglab/gogpt-training-data huggingface dataset:
Protein: Vacuolar protein sorting-associated protein 26A (Vesicle protein sorting 26A) (hVPS26) (O75436)
Organism: Homo sapiens (Human)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins (Probable). The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Required for the endosomal localization of WASHC2A (indicative for the WASH complex). Required for the endosomal localization of TBC1D5. Mediates retromer cargo recognition of SORL1 and is involved in trafficking of SORL1 implicated in sorting and processing of APP. Involved in retromer-independent lysosomal sorting of F2R. Involved in recycling of ADRB2. Enhances the affinity of SNX27 for PDZ-binding motifs in cargo proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15078903}. Endosome membrane {ECO:0000269|PubMed:22431521}; Peripheral membrane protein {ECO:0000250|UniProtKB:P40336}. Early endosome {ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:16732284, ECO:0000269|PubMed:20682791}. Note=Localizes to tubular profiles adjacent to endosomes (PubMed:15078903). Predominantly found in early not late endosomes (By similarity). {ECO:0000250|UniProtKB:P40336}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-2
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- Sorting nexin-3
- Sorting nexin-5
- TBC1 domain family member 5
- Sorting nexin-27
- Sorting nexin-6
- Vacuolar protein sorting-associated protein 26B
Sequence:
MSFLGGFFGPICEIDIVLNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPGKRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYESYIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAPVKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPEKLRKQRTNFHQRFESPESQASAEQPEM
Protein: Akr1c1 protein (Q5I0L1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
NSKQQTVRLSDGHFIPVLGFGTYAPREVPKSKALEATKIAIDAGFRHIDSAAVYQNEKEVGLAIRSKIADGTVKREDIFYTSKVWCTFNHPERVQVCLEQSLKQLQLEYVDLYLIHFPMALKPEEDLKAKDENEKLLFDVVDICDTWKAMEKCKDAGLAKSIGVSNFNRRQLEKILNKPGLKHRPVCNQVECHPYLNQRKLLDFCKSKDIVLVAYSALGSHRETRCVDKSLPVLLADPVLCAIAKKYNWTPALIALRYQLERGVVVLAKSFTEKRIKENMQVFEFQLTSEDMKVLDGLNKNIRYMSGSRFQGHPDFPFLDEY
Protein: Potassium voltage-gated channel subfamily A member 6 (Voltage-gated potassium channel HBK2) (Voltage-gated potassium channel subunit Kv1.6) (P17658)
Organism: Homo sapiens (Human)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (By similarity). Homotetrameric channels display rapid activation and slow inactivation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14575698, ECO:0000269|PubMed:2347305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily A member 1
- Voltage-gated potassium channel subunit beta-2
- Ubiquitin-like protein FUBI
- Voltage-gated potassium channel subunit beta-1
- Potassium voltage-gated channel subfamily A member 3
- Voltage-gated potassium channel subunit beta-3
- Triosephosphate isomerase
- Sedoheptulokinase
Sequence:
MRSEKSLTLAAPGEVRGPEGEQQDAGDFPEAGGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRVDGRGGNNGGVSRVSPVSRGSQEEEEDEDDSYTFHHGITPGEMGTGGSSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGTELVQQQEQQPASGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADDDDSLFPSIPDAFWWAVVTMTTVGYGDMYPMTVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEQEEQGQYTHVTCGQPAPDLRATDNGLGKPDFPEANRERRPSYLPTPHRAYAEKRMLTEV
Protein: Bacterial dynamin-like protein (BDLP) (EC 3.6.5.5) (B2IZD3)
Organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Function: Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer; this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:17122778}; Peripheral membrane protein {ECO:0000305|PubMed:17122778}. Note=Probably inserts into the outer leaflet of the membrane only (Probable). Forms foci localized in the cell periphery, and occasionally in the cell interior. {ECO:0000305|PubMed:20064379}.
Interaction partners:
- DUF3040 domain-containing protein
- Cell division protein FtsZ
- Small ribosomal subunit protein uS15
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Cell division protein SepF
Sequence:
MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWAMGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGPIGFALLGLGVGFLQADQARRELVKTAKKELVKHLPQVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS
Protein: B3 domain-containing protein At4g05630 (Protein AUXIN RESPONSE FACTOR 46) (Q9M0U1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 1
- Auxin response factor 9
Sequence:
MANFPDKQYDSNNPYNIMITLSPFDVDRSTTIMMPKALLETNLFPFMEISTLVQLLQVQDKPKMIGVYDIDTQITTYVIIRQDGNNFKFHGWNDILKRKHYKAGDTIAFWWDLRHTRLNFKHVA
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11 (Complex I-B14.7) (NADH-ubiquinone oxidoreductase subunit B14.7) (K7EQ77)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004292}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004292}; Matrix side {ECO:0000256|ARBA:ARBA00004292}.
Interaction partners:
Sequence:
MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYTFTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARSEWPPPHPHPPPSLAE
Protein: GCS light chain (Gamma-ECS regulatory subunit) (Gamma-glutamylcysteine synthetase regulatory subunit) (Glutamate--cysteine ligase modifier subunit) (Q9VCW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutamate--cysteine ligase
- Uncharacterized protein, isoform C
- Gamma-glutamyl transpeptidase, isoform A
- Branched-chain-amino-acid aminotransferase
- Dipeptidase B, isoform A
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- RE13973p
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
Sequence:
MIPTITKKYQNVVISTGNIIATELGQRKSNEELYDGLKITLHTDSTAERVVVEKEIDELHGRVQRATQELTTRLTENGRNEISIGAKIFLNRHSTESVNQAVEELLHILSVTHVDNVVLAYHPNAVATATPVATTKPPCSEDSNVSRATNWSQRNGKEGVAELKELYKTLEQYALKQQITQLGIADLDAAALEELHNSAQVVPTIAQVNLSTCCVVPPELQEFCTAHDIQLNTHSDPELLLPVEQFDGLVPGYTIDWTLRYQVHVRCRGVLTAKGYIVGASRSSV
Protein: Pre-mRNA-splicing factor 38 (X2JF51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367025}.
Interaction partners:
Sequence:
MDEDYSASSSAGGGKKAGKQHNTLPFWGNESSMNLNALILANIQSSSYFKVHLFKLKTYHEVVDEIYYQVKHMEPWERGSRKTSGQTGMCGGVRGVGAGGIVSTAYCLLYKLYTLRLTRKQINGLLNHTDSAYIRALGRCW
Protein: Transcription factor AP-2-alpha (AP-2 transcription factor) (Activating enhancer-binding protein 2-alpha) (Activator protein 2) (A0A6E1XE14)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKMLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEFLNRQHSDPNEQVTRKNMLLATKQICKEFTDLLAQDRSPLGNSRPNPILEPGIQSCLTHFNLISHGFGSPAVCAAVTALQNYLTEALKAMDKMYLSNNPNSHTDNNAKSSDKEEKHRK
Protein: Collagen alpha-4(IV) chain (P53420)
Organism: Homo sapiens (Human)
Function: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}. Note=Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250}.
Interaction partners:
- Collagen alpha-3
- Collagen alpha-1
- CD44 antigen
- Collagen alpha-5
- Platelet glycoprotein VI
- Immunoglobulin-binding protein 1
- Integrin alpha-V
- Integrin alpha-3
- Collagen alpha-1
- Nephrin
Sequence:
MWSLHIVLMRCSFRLTKSLATGPWSLILILFSVQYVYGSGKKYIGPCGGRDCSVCHCVPEKGSRGPPGPPGPQGPIGPLGAPGPIGLSGEKGMRGDRGPPGAAGDKGDKGPTGVPGFPGLDGIPGHPGPPGPRGKPGMSGHNGSRGDPGFPGGRGALGPGGPLGHPGEKGEKGNSVFILGAVKGIQGDRGDPGLPGLPGSWGAGGPAGPTGYPGEPGLVGPPGQPGRPGLKGNPGVGVKGQMGDPGEVGQQGSPGPTLLVEPPDFCLYKGEKGIKGIPGMVGLPGPPGRKGESGIGAKGEKGIPGFPGPRGDPGSYGSPGFPGLKGELGLVGDPGLFGLIGPKGDPGNRGHPGPPGVLVTPPLPLKGPPGDPGFPGRYGETGDVGPPGPPGLLGRPGEACAGMIGPPGPQGFPGLPGLPGEAGIPGRPDSAPGKPGKPGSPGLPGAPGLQGLPGSSVIYCSVGNPGPQGIKGKVGPPGGRGPKGEKGNEGLCACEPGPMGPPGPPGLPGRQGSKGDLGLPGWLGTKGDPGPPGAEGPPGLPGKHGASGPPGNKGAKGDMVVSRVKGHKGERGPDGPPGFPGQPGSHGRDGHAGEKGDPGPPGDHEDATPGGKGFPGPLGPPGKAGPVGPPGLGFPGPPGERGHPGVPGHPGVRGPDGLKGQKGDTISCNVTYPGRHGPPGFDGPPGPKGFPGPQGAPGLSGSDGHKGRPGTPGTAEIPGPPGFRGDMGDPGFGGEKGSSPVGPPGPPGSPGVNGQKGIPGDPAFGHLGPPGKRGLSGVPGIKGPRGDPGCPGAEGPAGIPGFLGLKGPKGREGHAGFPGVPGPPGHSCERGAPGIPGQPGLPGYPGSPGAPGGKGQPGDVGPPGPAGMKGLPGLPGRPGAHGPPGLPGIPGPFGDDGLPGPPGPKGPRGLPGFPGFPGERGKPGAEGCPGAKGEPGEKGMSGLPGDRGLRGAKGAIGPPGDEGEMAIISQKGTPGEPGPPGDDGFPGERGDKGTPGMQGRRGEPGRYGPPGFHRGEPGEKGQPGPPGPPGPPGSTGLRGFIGFPGLPGDQGEPGSPGPPGFSGIDGARGPKGNKGDPASHFGPPGPKGEPGSPGCPGHFGASGEQGLPGIQGPRGSPGRPGPPGSSGPPGCPGDHGMPGLRGQPGEMGDPGPRGLQGDPGIPGPPGIKGPSGSPGLNGLHGLKGQKGTKGASGLHDVGPPGPVGIPGLKGERGDPGSPGISPPGPRGKKGPPGPPGSSGPPGPAGATGRAPKDIPDPGPPGDQGPPGPDGPRGAPGPPGLPGSVDLLRGEPGDCGLPGPPGPPGPPGPPGYKGFPGCDGKDGQKGPVGFPGPQGPHGFPGPPGEKGLPGPPGRKGPTGLPGPRGEPGPPADVDDCPRIPGLPGAPGMRGPEGAMGLPGMRGPSGPGCKGEPGLDGRRGVDGVPGSPGPPGRKGDTGEDGYPGGPGPPGPIGDPGPKGFGPGYLGGFLLVLHSQTDQEPTCPLGMPRLWTGYSLLYLEGQEKAHNQDLGLAGSCLPVFSTLPFAYCNIHQVCHYAQRNDRSYWLASAAPLPMMPLSEEAIRPYVSRCAVCEAPAQAVAVHSQDQSIPPCPQTWRSLWIGYSFLMHTGAGDQGGGQALMSPGSCLEDFRAAPFLECQGRQGTCHFFANKYSFWLTTVKADLQFSSAPAPDTLKESQAQRQKISRCQVCVKYS
Protein: Transcription factor MYB25 (Myb-related protein 25) (AtMYB25) (O04192)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for male gametophyte (pollen) development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Transmembrane protein
- Putative pectinesterase 63
Sequence:
MNGEISRPPELISSRNPCKSFENAIHKAVEAELAELAKSDANGGGKSKVKGPWLPEQDEALTRLVKMCGPRNWNLISRGIPGRSGKSCRLRWCNQLDPILKRKPFSDEEEHMIMSAQAVLGNKWSVIAKLLPGRTDNAIKNHWNSNLRRKPAEQWKIPLLMSNTEIVYQLYPSMVRRISNASPKEHLPQEEETGVLSDDKMDDEAKEPPREQNSKTGVYRPVARMGAFSVCKPGYMAPCEGPLVQASRPDSLAGKFLQSLCYDPIIPSKCGHGCCNHQDSTTLSSSSVLGSEFVDYEEHSSAELDKELISISNDLNNTAWIRSGKEAEQSLKADDQFRREYAHSKFSGMVNNGVSSQMVRQDLRALS
Protein: Uncharacterized protein (Q586P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTEATNENLQILLTKLMTDRFCSGEVNDIDACVQNFVPQASDGSWVDQSIHRRGMKKCEPYREVARRCLEDEKKQKMVFKAATEVSTCREERRKLEKCRYAGGDCEQEALEVLYCGMVGLIQRQRGRQEQRR
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVH5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MVKPLVLLSLLAYAQAYVKLDFTKTPGSDLAKRDVVDPEAAQLTFDKDQYIVEVAVGTPPQKVLLQIDTGSSDLFVIEESNPYCKNNKNKAPKKKDLESPGDDYPRTPNQVPKSDRTLDCKKYGFYNRNESSTFNSNGTDLFITYGDNGFVRGTWGTDSVSVGNLNLSNLSIGVSPMTNTSTGILGVGLPGEESTFNYSSNVTGPSNYQYSNFPIRLKEEGLIEKIAYSIYLNETGSKYGSILFGAVDHSKYQGPLYTFPLVNSKYKEGSDPFQFEITMNGVGLVGKTDNITLYDQKLPTLLDSGSTISLLPRDVADLVAQQVNGTVDGKGNCIKLPKCPSKKDNQKLIFNFSGAEFSVNVTDFMEKHKGKCYLQFSALDGINFALLGDNFMNNVYTVFNLDDKELSLAQANYNSSLKPDIEEIKDTVPSAVLAPQYYNTFSADPTATAVTGNIFAPEATMSMAAPANASRNSSLNSTFNSSSNYSRVQMKKRTYPNSSSSLQANSAILIMIAAAITAMFL
Protein: Uncharacterized protein C685.08 (Q9Y7L9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Putative lysine N-acyltransferase C17G9.06c
- Putative uncharacterized protein C23C4.04c
- Putative amidase PB8B6.03
- Uncharacterized protein C16G5.19
- Putative uncharacterized protein C27E2.12
- Uncharacterized protein PB1A10.16
- Uncharacterized mitochondrial membrane protein C800.14c
- Fluoride export protein 2
- Probable circularly permuted 1,3-beta-glucanase P23A10.11c YJL171C
- Phospholipase D1
Sequence:
MVLVKFKREKLTVMLEVQPGLSVYDAVKLLKSALNLPPDSILRIGSFEQNDWVAMENDALSKTIITNNTEYAFAEGEEPLLVEKPKDYDDMSEEISP
Protein: Uncharacterized protein (Q585K3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLRDDILALTATLSRLSRARDTATASDCTETRVDDTISAVSVAAEDDETRDNTAPSLMCMPVPRSGGRKMEEDTFTILPNSRDTTALPRGEATADRCCASNDNARSKRLSTPSGQEVAVSQRPPLAPTEGVTWNHSHGRSSIADDETNSCIDPVSSESCGVSTEPSGAEPSPCQVEEAYKRIARRLLSEIQRLDLCIATVSARHVDERKEFLHTQRELKERLVERDALIGTLQHQLKLAESSESTVRCRCCFGRANCAPVQSRATATVSTERFTSRSRSDSGVPTTAAPICHQGLDIATNTQGTDEAKGPRGRSNQHHPATEEVDTYATRASSLAGLACHENVTAVIPKTAIAAGTSEGPVPVTTSGCARARASSLSRSEGRDGSDDPAVRGTVTNSVTVPTDRAPSPHASFPTDCCPRVSQASYRVGVAAAVGGRAKGLRRTPKTTPLRRRRQHVLECSGDTAWRGSLHCRTCREDVLPTAPEVQQGTLTGSSANPLPSSFPSPFVSTATTGARFNHGVPNRAFSQSPSHRKKRRSSNRVRCPVAASGDELLRGLIAKSAFLEAGLRGVMERLDEQQGELHDVTCLLHKLVLSSMHGSA
Protein: PHD finger protein 20 (Q5JWZ0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTKHPPNRRGISFEVGAQLEARDRLKNWYPAHIEDIDYEEGKVLIHFKRWNHRYDEWFCWDSPYLRPLEKIQLRKEGLHEEDGSSEFQINEQVLACWSDCRFYPAKVTAVNKDGTYTVKFYDGVVQTVKHIHVKAFSKDQNIVGNARPKETDHKSLSSSPDKREKFKEQRKATVNVKKDKEDKPLKTEKRPKQPDKEGKLICSEKGKVSEKSLPKNEKEDKENISENDREYSGDAQVDKKPENDIVKSPQENLREPKRKRGRPPSIAPTAVDSNSQTLQPITLELRRRKISKGCEVPLKRPRLDKNSSQEKSKNYSENTDKDLSRRRSSRLSTNGTHEILDPDLVVSDLVDTDPLQDTLSSTKESEEGQLKSALEAGQVSSALTCHSFGDGSGAAGLELNCPSMGENTMKTEPTSPLVELQEISTVEVTNTFKKTDDFGSSNAPAVDLDHKFRCKVVDCLKFFRKAKLLHYHMKYFHGMEKSLEPEESPGKRHVQTRGPSASDKPSQETLTRKRVSASSPTTKDKEKNKEKKFKEFVRVKPKK
Protein: 14-3-3-like protein GF14 omicron (General regulatory factor 11) (Q9S9Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- At1g12030
- Amino acid transporter AVT6B
- Protein CONSERVED IN THE GREEN LINEAGE AND DIATOMS 27
- thiohydroximate-O-sulfate sulfate/sulfur-lyase
- Uncharacterized protein At3g61930
- Uncharacterized protein
- AT5g05250/K18I23_5
- TRM32-like protein
- Solute carrier family 40 member 2
- Dual specificity phosphatase Cdc25
Sequence:
MENERAKQVYLAKLNEQAERYDEMVEAMKKVAALDVELTIEERNLLSVGYKNVIGARRASWRILSSIEQKEESKGNEQNAKRIKDYRTKVEEELSKICYDILAVIDKHLVPFATSGESTVFYYKMKGDYFRYLAEFKSGADREEAADLSLKAYEAATSSASTELSTTHPIRLGLALNFSVFYYEILNSPERACHLAKRAFDEAIAELDSLNEDSYKDSTLIMQLLRDNLTLWTSDLEEGGEQSKGHNQQDEN
Protein: C-Jun-amino-terminal kinase-interacting protein 2 (JIP-2) (JNK-interacting protein 2) (Islet-brain-2) (IB-2) (JNK MAP kinase scaffold protein 2) (Mitogen-activated protein kinase 8-interacting protein 2) (Q9ERE9)
Organism: Mus musculus (Mouse)
Function: The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. JIP2 inhibits IL1 beta-induced apoptosis in insulin-secreting cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13387}. Note=Accumulates in cell surface projections. {ECO:0000250|UniProtKB:Q13387}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- C-Jun-amino-terminal kinase-interacting protein 1
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase kinase kinase 11
- C-Jun-amino-terminal kinase-interacting protein 3
- Mitogen-activated protein kinase kinase kinase kinase 1
- Kinesin light chain 1
- Low-density lipoprotein receptor-related protein 8
Sequence:
MADRAEMFSLSTFHSLSPPGCRPPQDISLEEFDDEDLSEITDDCGLGLSYDSDHCEKDSLSLGRSEQPHPICSFQDDFQEFEMIDDNEEEDDEEEEEEEEEEEDGDRQGKAGGGPGSQALAGDSLIPSPSLEESHKLRPTTLHLTTLGAQDSLNNNNGGFTSAPPSSWQETVLRSPAQEPLKELPAPLLPAEEERHEVQSLARPGCDCEGNQPPEPPASSGGASPSSDPGIEADLRSHSSGGHEGRRSSQELSSPGSDSEDAGGARLGRMISSISETELELSSDGGSSSGRSSHLTNSIEEASSPASEPEPEPEPLHEPPRRPAFLPVGQDDTNSEYESGSESEPDLSEDADSPWLLSNLVSRMISEGSSPIRCPGQCLSPAPRLPEEAASQANSVPQDCQDPEAGPHVELVDMDTLCGPPPPAPAAPRLGPAQPGPCLFLSNPTRDTITPLWATPGRTARPGRSCSAACSEEEEEDEEEDEEDEEDAEDSVVPPGSRTTGSTAPLDASLVYDAVKYTLVVDEHTQLELVSLRRCAGLGNDSEEDSSCEASEEEAGATLLGSDQVPEDASPDSPDLTFSKKFLNVFVNSTSRSSSTESFGLFSCVVNGEEREQTHRAVFRFIPRHPDELELDVDDPVLVEAEEDDFWFRGFNMRTGERGVFPAFYAHAVPGPAKDLLGSKRSPCWVDRFDVQFLGSVEVPCHQGNGILCAAMQKIATARKLTVHLRPPASCDLEISLRGVKLSLSGGGPEFQRCSHFFQMKNISFCGCHPRNSCYFGFITKHPLLSRFACHVFVSQESMRPVARSVGRAFLEYYQEHLAFACPTEDIYLE
Protein: SPI-1 type 3 secretion system translocon protein SctB (SPI-1 T3SS translocon protein SctB) (Cell invasion protein SipC) (Effector protein SipC) (E1WAC8)
Organism: Salmonella typhimurium (strain SL1344)
Function: Actin-binding protein that interferes with host cell actin cytoskeleton. Nucleates actin polymerization and condensates actin filaments into cables (bundling). SipA potenciates SipC activity and both are required for an efficient bacterial internalization by the host cell (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:7608068}. Host membrane {ECO:0000250|UniProtKB:P0CL47}; Single-pass membrane protein {ECO:0000255}. Note=Secreted via the type III secretion system 1 (SPI-1 T3SS). {ECO:0000269|PubMed:7608068}.
Interaction partners:
Sequence:
MLISNVGINPAAYLNNHSVENSSQTASQSVSAKDILNSIGISSSKVSDLGLSPTLSAPAPGVLTQTPGTITSFLKASIQNTDMNQDLNALANNVTTKANEVVQTQLREQQAEVGKFFDISGMSSSAVALLAAANTLMLTLNQADSKLSGKLSLVSFDAAKTTASSMMREGMNALSGSISQSALQLGITGVGAKLEYKGLQNERGALKHNAAKIDKLTTESHSIKNVLNGQNSVKLGAEGVDSLKSLNMKKTGTDATKNLNDATLKSNAGTSATESLGIKDSNKQISPEHQAILSKRLESVESDIRLEQNTMDMTRIDARKMQMTGDLIMKNSVTVGGIAGASGQYAATQERSEQQISQVNNRVASTASDEARESSRKSTSLIQEMLKTMESINQSKASALAAIAGNIRA
Protein: Anhydro-N-acetylmuramic acid kinase (EC 2.7.1.170) (AnhMurNAc kinase) (P77570)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Interaction partners:
- N-acetylmuramic acid 6-phosphate etherase
- Beta-hexosaminidase
- Anhydromuropeptide permease
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- Membrane-bound lysozyme inhibitor of C-type lysozyme
- UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase
- N-acetyl-D-glucosamine kinase
Sequence:
MKSGRFIGVMSGTSLDGVDVVLATIDEHRVAQLASLSWPIPVSLKQAVLDICQGQQLTLSQFGQLDTQLGQLFADAVNALLKEQNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQIVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERRMVLNIGGIANLSLLIPGQPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKSTGREYFNYGWLERHLRHFPGVDPRDVQATLAELTAVTISEQVLLSGGCERLMVCGGGSRNPLLMARLAALLPGTEVTTTDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETVLGAIFPANP
Protein: Sphingosine-1-phosphate lyase (AtSPL1) (S1PL) (SP-lyase) (SPL) (EC 4.1.2.27) (Dihydrosphingosine phosphate lyase 1) (AtDPL1) (Sphingosine-1-phosphate aldolase) (Q9C509)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. May play a minor role in maintenance of sphingolipid metabolism during normal plant development and growth, but be required for maintaining sphingoid long chain bases (LCB) and their phosphorylated derivatives (LCB-P) levels when sphingolipid metabolism is perturbed. May play a role in dehydration stress.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17635905, ECO:0000305|PubMed:18849574}; Single-pass type III membrane protein {ECO:0000305|PubMed:17635905, ECO:0000305|PubMed:18849574}.
Interaction partners:
- Sphingosine kinase 1
- Sphingosine kinase 2
- Long chain base biosynthesis protein 1
- Lipid phosphate phosphatase delta
- Sphingoid long-chain bases kinase 1
- Long chain base biosynthesis protein 2b
- Ceramide kinase
- serine C-palmitoyltransferase
- Long chain base biosynthesis protein 2a
- 3-dehydrosphinganine reductase TSC10B
Sequence:
MDSFSYSSMKSMLIQARGSLNSRLSEFEPLVLLLVPLVSLFLAQIIGSVFGVVHEKGLKACLIGFIMGLLKMIPGVQNYIDAEKQKVVDQLQSGSSSKKKNKTEVLPVKGLGVEVLEKMENEKRNDAIWQGKCSGTVYIGGAESEGHFSLINQACSMFAHTNPLHIDVFQSVVRFESEVVAMTAALLGSKETASGGQICGNMTSGGTESIVLAVKSSRDYMKYKKGITRPEMIIPESGHSAYDKAAQYFKIKLWRVPVDKDFRADVKATRRHINRNTIMIVGSAPGFPHGIIDPIEELGQLALSYGICFHVDLCLGGFVLPFARKLGYQIPPFDFSVQGVTSISVDVHKYGLAPKGTSTVLYRNHEIRKHQFVAVTEWSGGLYVSPTIAGSRPGSLVAGAWAAMMSLGEEGYLQNTSKIMEASKRLEEGVREIHELFVIGKPDMTIVAFGSKALDIFEVNDIMSSKGWHLNALQRPNSIHICITLQHVPVVDDFLRDLREAVETVKANPGPITGGLAPIYGAAGKMPDRGMVNELLVSFMDSQY