wanglab/gogpt-training-data huggingface dataset:
Protein: Afadin- and alpha-actinin-binding protein (ADIP) (Afadin DIL domain-interacting protein) (SSX2-interacting protein) (Q9Y2D8)
Organism: Homo sapiens (Human)
Function: Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (By similarity). Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome. Involved in ciliogenesis. It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia.
Subcellular location: Cell junction, adherens junction {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:23816619, ECO:0000269|PubMed:24356449}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:24356449}. Note=Not found at cell-matrix AJs. {ECO:0000250}.
Interaction partners:
- Afadin
- Alpha-actinin-1
- Alpha-actinin-4
- WD repeat-containing protein WRAP73
- Protein SSX3
- Protein SSX4
- Coiled-coil domain-containing protein 14
- Protein SSX1
- Pericentriolar material 1 protein
- Pericentrin
Sequence:
MGDWMTVTDPGLSSESKTISQYTSETKMSPSSLYSQQVLCSSIPLSKNVHSFFSAFCTEDNIEQSISYLDQELTTFGFPSLYEESKGKETKRELNIVAVLNCMNELLVLQRKNLLAQENVETQNLKLGSDMDHLQSCYSKLKEQLETSRREMIGLQERDRQLQCKNRNLHQLLKNEKDEVQKLQNIIASRATQYNHDMKRKEREYNKLKERLHQLVMNKKDKKIAMDILNYVGRADGKRGSWRTGKTEARNEDEMYKILLNDYEYRQKQILMENAELKKVLQQMKKEMISLLSPQKKKPRERVDDSTGTVISDVEEDAGELSRESMWDLSCETVREQLTNSIRKQWRILKSHVEKLDNQVSKVHLEGFNDEDVISRQDHEQETEKLELEIQQCKEMIKTQQQLLQQQLATAYDDDTTSLLRDCYLLEEKERLKEEWSLFKEQKKNFERERRSFTEAAIRLGLERKAFEEERASWLKQQFLNMTTFDHQNSENVKLFSAFSGSSDWDNLIVHSRQPQKKPHSVSNGSPVCMSKLTKSLPASPSTSDFCQTRSCISEHSSINVLNITAEEIKPNQVGGECTNQKWSVASRPGSQEGCYSGCSLSYTNSHVEKDDLP
Protein: TIR domain-containing protein (EC 3.2.2.6) (AtTIK) (TIR-KASH protein) (Q0WSX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Could play a role in nuclear morphology, specifically nuclear size.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:25217773}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- SUN domain-containing protein 3
- SUN domain-containing protein 1
- SUN domain-containing protein 2
- SUN domain-containing protein 4
- Protein SINE1
- SUN domain-containing protein 5
- Protein SINE2
- WPP domain-interacting tail-anchored protein 2
- Protein SINE4
- Protein KAKU4
Sequence:
MDEQVQEPLSDQVFINFRGDELREIFVNHLELQLRNAGINVFIDTKEQKGRRLQYLFTRIKKSKIALAIFSKRYCESKWCLDELVTMNEQMKEKKLVVIPIFYNVRSDDVKRAANPDGEGNLDGEFSLPFKQLKQNHAGEPERVEGWERALRSVTKRIGFSRSNSKYKHDTDFVLDIVKEVKKQLNIPTDNSWSAIGVAFLAITINLIFSFFIAPKYLPDQKFFQTPEWFIGTLAVVLASWFWYKNNQNKAPPPS
Protein: Calcitonin gene-related peptide type 1 receptor (CGRP type 1 receptor) (Calcitonin receptor-like receptor) (CRLR) (Q16602)
Organism: Homo sapiens (Human)
Function: Receptor for calcitonin-gene-related peptide (CGRP) together with RAMP1 and receptor for adrenomedullin together with RAMP3 (By similarity). Receptor for adrenomedullin together with RAMP2. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30115739}; Multi-pass membrane protein {ECO:0000269|PubMed:32296767}.
Interaction partners:
- Pro-adrenomedullin
- Receptor activity-modifying protein 2
- Calcitonin
- Protein ADM2
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 1
- Calcitonin gene-related peptide 2
- Islet amyloid polypeptide
- Guanine nucleotide-binding protein G
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MEKKCTLYFLVLLPFFMILVTAELEESPEDSIQLGVTRNKIMTAQYECYQKIMQDPIQQAEGVYCNRTWDGWLCWNDVAAGTESMQLCPDYFQDFDPSEKVTKICDQDGNWFRHPASNRTWTNYTQCNVNTHEKVKTALNLFYLTIIGHGLSIASLLISLGIFFYFKSLSCQRITLHKNLFFSFVCNSVVTIIHLTAVANNQALVATNPVSCKVSQFIHLYLMGCNYFWMLCEGIYLHTLIVVAVFAEKQHLMWYYFLGWGFPLIPACIHAIARSLYYNDNCWISSDTHLLYIIHGPICAALLVNLFFLLNIVRVLITKLKVTHQAESNLYMKAVRATLILVPLLGIEFVLIPWRPEGKIAEEVYDYIMHILMHFQGLLVSTIFCFFNGEVQAILRRNWNQYKIQFGNSFSNSEALRSASYTVSTISDGPGYSHDCPSEHLNGKSIHDIENVLLKPENLYN
Protein: LD25144p (Q86PA4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQPNQLSCGNCNLLSRLMHSKFAATDRDDMVETMLHMCGSLSSFSDACANIVLTYFNDIYDRMRKPMNTKCHKVIDKYGDKIADLLLKEMDPKLICTELGMCILADLDDLEVDEALKYDVIALPRQDNKLSSSIKEPPTCVLCEFIMTKLDADLKNKTEQDDIKRAIEAVCNRLPATVRKQCDTFVDGYASAVLKLLSDVPPKQVCQKLQLCFSVAVTDEVLECGVCHGVTQALLPFLREKKDNVSEVTALQMTSVGCENLPAKYYKICSEMISIYGSSIKNLAKRPYIDQSHICAEIGKCFESEKSSLAFARISA
Protein: Ubiquitin activating enzyme, putative (Q384R4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin-activating enzyme E1, putative
- SUMO-conjugating enzyme UBC9
- Small ubiquitin protein, putative
Sequence:
MNADEKTRYDRQMRLWGKSTQERLRRTEVNIKGITSANAEVAKNLVLAGVGSVVLDDTAPVEAADLKHSFILQGCKLGERRGEASAGKLQSLNPYVAVSSSREIRNRDGAPQSNSSLRVVLARAKCEADMLECAGDPLSGSADVMLLTVDLGHLTAGFFLYRKQKIPFVAQLRALLDEEVGTRPVVFQRVLLLLKMAECPQELNYFERLLFAKDFVRQRSLLQLTREDIEFAAAATGELMHSTAIETTVAGGVFAQLIIHTIGMGSEEMGEGEYAWAISDTSDGVEVQVGHLRNP
Protein: Ribosomal protein S23, retrogene 1 (D3Z250)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTFSTKSSNQNFIIFLNEVQAAIIGHERCDLLPVLNELHPDALPDGRIWLFGLNPYFFQHNSLCMRGTPKRIGLQGCAQVGFLVLFVMPLLIPSVTAELPGSSETTTLAHLAGATGP
Protein: BRISC and BRCA1-A complex member 2 (BRCA1-A complex subunit BRE) (BRCA1/BRCA2-containing complex subunit 45) (Brain and reproductive organ-expressed protein) (Q8K3W0)
Organism: Mus musculus (Mouse)
Function: Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex, thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin (By similarity). May regulate TNF-alpha signaling through its interactions with TNFRSF1A.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NXR7}. Nucleus {ECO:0000250|UniProtKB:Q9NXR7}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q9NXR7}.
Interaction partners:
- Lys-63-specific deubiquitinase BRCC36
- BRISC and BRCA1-A complex member 1
- BRCA1-A complex subunit RAP80
- BRCA1-A complex subunit Abraxas 1
- BRISC complex subunit Abraxas 2
- Serine hydroxymethyltransferase, mitochondrial
- Lys-63-specific deubiquitinase BRCC36-like
- BRCA1-associated RING domain protein 1
- Breast cancer type 1 susceptibility protein homolog
- Breast cancer type 2 susceptibility protein homolog
Sequence:
MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLKSGCTSLTPGPNCDRFKLHIPYAGETLKWDIIFNAQYPELPPDFIFGEDAEFLPDPSALHNLASWNPSNPECLLLVVKELVQQYHQFQCGRLRESSRLMFEYQTLLEEPQYGENMEIYAGKKNNWTGEFSARFLLKLPVDFSNIPTYLLKDVNEDPGEDVALLSVSFEDTEATQVYPKLYLSPRIEHALGGSSALHIPAFPGGGCLIDYVPQVCHLLTNKVQYVIQGYHKRREYIAAFLSHFGTGVVEYDAEGFTKLTLLLMWKDFCFLVHIDLPLFFPRDQPTLTFQSVYHFTNSGQLYSQAQKNYPYSPRWDGNEMAKRAKAYFKTFVPQFQEAAFANGKL
Protein: Ferric vibriobactin reductase ViuB (EC 1.16.1.7) (Ferric chelate reductase) (FCR) (Ferric reductase) (Ferric-vibriobactin utilization protein) (Vibriobactin utilization protein B) (A5F660)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Function: Involved in intracellular removal of iron from iron-vibriobactin complex. Vibriobactin is an iron-chelating compound involved in the transport of iron from the bacterial environment into the cell cytoplasm.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSNEVERVYPRLLDFVRKKYVSKNLLRVTLTGEDLIGFPEDQNGSHIKVFFPNQASGILQLPIREGDKVIWPEHKPVPRAYTVRQYRAQSNELDIDFVVHGEGTPGGGWALKAQTGSQLGLIGPGGPDPLIEPADWHIMAGDLSAVPAISAILEKMPSQAKGYVFLEVDDIEDKHDISHPEQMVIKWLVRDPNQAQPVLAMAIEQLPVPQGAESLSAFVAGENESVIACRKILRNEYRIARDKIYAIPYWKRGKNEEAYHEERHVVMDEEF
Protein: Serine/threonine-protein phosphatase PP-Z1 (EC 3.1.3.16) (P26570)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the maintenance of cell size and integrity in response to osmotic stress.
Interaction partners:
- Phosphopantothenoylcysteine decarboxylase subunit SIS2
- Serine/threonine-protein phosphatase PP-Z2
- Phosphopantothenoylcysteine decarboxylase subunit VHS3
- Protein phosphatase 1 regulatory subunit SDS22
- Type 1 phosphatases regulator YPI1
- GLC7-interacting protein 2
- Coenzyme A biosynthesis protein 3
- COMPASS component SWD2
- High-affinity potassium transport protein
- Serine/threonine-protein phosphatase 1 regulatory subunit PIG1
Sequence:
MGNSSSKSSKKDSHSNSSSRNPRPQVSRTETSHSVKSAKSNKSSRSRRSLPSSSTTNTNSNVPDPSTPSKPNLEVNHQRHSSHTNRYHFPSSSHSHSNSQNELLTTPSSSSTKRPSTSRRSSYNTKAAADLPPSMIQMEPKSPILKTNNSSTHVSKHKSSYSSTYYENALTDDDNDDKDNDISHTKRFSRSSNSRPSSIRSGSVSRRKSDVTHEEPNNGSYSSNNQENYLVQALTRSNSHASSLHSRKSSFGSDGNTAYSTPLNSPGLSKLTDHSGEYFTSNSTSSLNHHSSRDIYPSKHISNDDDIENSSQLSNIHASMENVNDKNNNITDSKKDPNEEFNDIMQSSGNKNAPKKFKKPIDIDETIQKLLDAGYAAKRTKNVCLKNNEILQICIKAREIFLSQPSLLELSPPVKIVGDVHGQYGDLLRLFTKCGFPPSSNYLFLGDYVDRGKQSLETILLLFCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWKTFIDTFNTLPLAAIVAGKIFCVHGGLSPVLNSMDEIRHVVRPTDVPDFGLINDLLWSDPTDSPNEWEDNERGVSYCYNKVAINKFLNKFGFDLVCRAHMVVEDGYEFFNDRSLVTVFSAPNYCGEFDNWGAVMSVSEGLLCSFELLDPLDSAALKQVMKKGRQERKLANQQQQMMETSITNDNESQQ
Protein: Histocompatibility 2, M region locus 2 (MHC class Ib antigen) (Q6W9J6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
METSAFFTLLFTLYLLLGASLALAQTFKGSHSLRYFDIAVSRPGLEETHYMTVGYVDDTEFVHFDNEAENPRFEPRVPWMEQMGQKYWDDQTRIAKAAEQQIRVYFQKLRDYYNQSQNSSHTIQRMTGCYIGPDGHLLHAYRQFGYDGQDYLTLNEDLSTWTAADAAAEITRREWEATNVAEFWRVYLEGPCMVWLFKYLTVGNETLLRTEPPKAYVTHHPRPEGDVTLRCWALGFYPSDIIMIWQRDGEDQTQDMDVIETRPAGDGTFQKWVAVVVPSGKEQNYTCHVAHEGLPEPLTLRWSK
Protein: Pentatricopeptide repeat-containing protein At3g02330, mitochondrial (Mitochondrial editing factor 13) (Q9FWA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in C-to-U editing of mitochondrial RNA. Required for RNA editing at 8 sites in 6 different mRNAs in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26048647}.
Interaction partners:
- Multiple organellar RNA editing factor 3, mitochondrial
- Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial
- Multiple organellar RNA editing factor 1, mitochondrial
- Multiple organellar RNA editing factor 2, chloroplastic
- Multiple organellar RNA editing factor 9, chloroplastic
- Pentatricopeptide repeat-containing protein DWY1, chloroplastic
- Transmembrane 9 superfamily member 7
Sequence:
MAESLRLLHMTRSVVSFNRCLTEKISYRRVPSFSYFTDFLNQVNSVSTTNFSFVFKECAKQGALELGKQAHAHMIISGFRPTTFVLNCLLQVYTNSRDFVSASMVFDKMPLRDVVSWNKMINGYSKSNDMFKANSFFNMMPVRDVVSWNSMLSGYLQNGESLKSIEVFVDMGREGIEFDGRTFAIILKVCSFLEDTSLGMQIHGIVVRVGCDTDVVAASALLDMYAKGKRFVESLRVFQGIPEKNSVSWSAIIAGCVQNNLLSLALKFFKEMQKVNAGVSQSIYASVLRSCAALSELRLGGQLHAHALKSDFAADGIVRTATLDMYAKCDNMQDAQILFDNSENLNRQSYNAMITGYSQEEHGFKALLLFHRLMSSGLGFDEISLSGVFRACALVKGLSEGLQIYGLAIKSSLSLDVCVANAAIDMYGKCQALAEAFRVFDEMRRRDAVSWNAIIAAHEQNGKGYETLFLFVSMLRSRIEPDEFTFGSILKACTGGSLGYGMEIHSSIVKSGMASNSSVGCSLIDMYSKCGMIEEAEKIHSRFFQRANVSGTMEELEKMHNKRLQEMCVSWNSIISGYVMKEQSEDAQMLFTRMMEMGITPDKFTYATVLDTCANLASAGLGKQIHAQVIKKELQSDVYICSTLVDMYSKCGDLHDSRLMFEKSLRRDFVTWNAMICGYAHHGKGEEAIQLFERMILENIKPNHVTFISILRACAHMGLIDKGLEYFYMMKRDYGLDPQLPHYSNMVDILGKSGKVKRALELIREMPFEADDVIWRTLLGVCTIHRNNVEVAEEATAALLRLDPQDSSAYTLLSNVYADAGMWEKVSDLRRNMRGFKLKKEPGCSWVELKDELHVFLVGDKAHPRWEEIYEELGLIYSEMKPFDDSSFVRGVEVEEEDQWCYC
Protein: Homeobox protein BEL1 homolog (Q38897)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role in ovule patterning and in determination of integument identity via its interaction with MADS-box factors. Formation of complex with AG-SEP dimers negatively regulates the carpel identity process and favors the maintenance of ovule identity. BEL1-STM complex maintains the indeterminacy of the inflorescence meristem. Required, with SPL, for cytokinin-induced PIN1 expression in ovules.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11701881, ECO:0000269|PubMed:8521490}.
Interaction partners:
- Homeobox protein knotted-1-like 2
- Homeobox protein knotted-1-like 1
- Protein KNATM
- Agamous-like MADS-box protein AGL11
- Homeobox protein knotted-1-like 5
- Transcription repressor OFP4
- Agamous-like MADS-box protein AGL5
- Large ribosomal subunit protein uL14my
- Agamous-like MADS-box protein AGL1
- Transcription repressor OFP1
Sequence:
MARDQFYGHNNHHHQEQQHQMINQIQGFDETNQNPTDHHHYNHQIFGSNSNMGMMIDFSKQQQIRMTSGSDHHHHHHQTSGGTDQNQLLEDSSSAMRLCNVNNDFPSEVNDERPPQRPSQGLSLSLSSSNPTSISLQSFELRPQQQQQQGYSGNKSTQHQNLQHTQMMMMMMNSHHQNNNNNNHQHHNHHQFQIGSSKYLSPAQELLSEFCSLGVKESDEEVMMMKHKKKQKGKQQEEWDTSHHSNNDQHDQSATTSSKKHVPPLHSLEFMELQKRKAKLLSMLEELKRRYGHYREQMRVAAAAFEAAVGLGGAEIYTALASRAMSRHFRCLKDGLVGQIQATSQALGEREEDNRAVSIAARGETPRLRLLDQALRQQKSYRQMTLVDAHPWRPQRGLPERAVTTLRAWLFEHFLHPYPSDVDKHILARQTGLSRSQVSNWFINARVRLWKPMIEEMYCEETRSEQMEITNPMMIDTKPDPDQLIRVEPESLSSIVTNPTSKSGHNSTHGTMSLGSTFDFSLYGNQAVTYAGEGGPRGDVSLTLGLQRNDGNGGVSLALSPVTAQGGQLFYGRDHIEEGPVQYSASMLDDDQVQNLPYRNLMGAQLLHDIV
Protein: Follistatin-related protein 4 (Follistatin-like protein 4) (m-D/Bsp120I 1-1) (Q5STE3)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MKPGGFWPHLALLGVSLPAVLGWMDQGASRSPNMVPGESQAEETRGFEVTRREGLPSPGLSASCGKKLCSHGSRCLLNRTTGQPSCQCLEVCRPRYMPVCGSDGRLYGNHCELRRAACLLGKRIVSVHSKDCFLKGDMCTMAGYARLKNVLLALQSRRQPLPQGTPRQSLASQKRLLVESLFKDLDADGNGHLGSLELAQYVLKEQDMDGSLNRCSPSDLLRFDDYNSDGSLTLGEFYTAFQVIQLSLAPEDKVSVTTVTVGLSTVLTCAIRGDLRPPIIWKRNGLTLSFLGLEDINDFGEDGSLYITKVTTVHMGNYTCHALGHEQLVQTHVLQVNVPPVIRVYPETQAQEPGVAASLRCHAEGIPLPRIIWLKNGMDVSTQMSKQLSLLANGSELHIGSVRYEDTGAYTCIAKNEVGVDEDISSLFIEDSARKTLANILWREEGLSVGNMFYVFAEDGIVVIHPVDCEVQRRLKPTEKIFMSYEEICPRVEGDATQPCQWASAVNVRNRYIYVAQPALNRVLVVDVQAQKVLQSIGVDPLPVKLSYDKSHDQVWVLSWGDMHKSQPSLQVITEASTGQGQHLIRTPFAGVDNFFIPPTNLIINHIRFGFIFNKTDPAVHKVDLETLMALKTISLRHYGCMPQAMAHTHLGGYFFVQCQQDTPTSTGPQLLIDSVTDSVLGPNSDITGTPHVSPDGRFIVSVSNKGPWLHVQEVTVRGEIQTLYDLKINPGISDLAFQHSFTEGSQYNAYATLDKEPDLLFLELSTGKMGRLKNLKEPPRGPAPTWGGPRRVLRDSGLFGQYLLTPAQESLFLVNGRQNALRCEVSGIKGAATVVWVGEV
Protein: SKP1-like protein 10 (AtSK10) (Q9LSX8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-like protein 3
- Putative cullin-like protein 2
- Putative cullin-like protein 1
- Cullin-2
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Cullin-3A
Sequence:
MSTKKIILKSSDGHSFEVEEEAACQCQTIAHMSEDDCTDNGIPLPEVTGKILEMVIEYCNKHHVDAANPCSDEDLKKWDKEFMEKYQSTIFDLIMAANYLNIKSLLDLACQTVADMIKDNTVEHTRKFFNIENDYTHEEEEAVRRENQWGFE
Protein: 3-phosphoinositide-dependent protein kinase 2 (AtPDK2) (EC 2.7.11.1) (Q4V3C8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Membrane-associated after cell stimulation leading to its translocation. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase AtPK2/AtPK19
- Serine/threonine-protein kinase AtPK1/AtPK6
- Cytochrome b561 and DOMON domain-containing protein At5g35735
- Putative defensin-like protein 148
- Protein PELOTA 1
- Protein DUF642 L-GALACTONO-1,4-LACTONE-RESPONSIVE GENE 1
- Protein STRICTOSIDINE SYNTHASE-LIKE 9
- Putative glutamine amidotransferase GAT1_2.1
Sequence:
MLTMDKEFDSKLTLQGNSSSNGETISRSKSFAFKAPQENFTYHDFELGKIYGVGSYSKVVRAKKKDNGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIVKLFFTFQDTQSLYMALESCEGGELFDQITRKGRLSEDEARFYSAEVVDALEYIHNMGLIHRDIKPENLLLTLDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTDPSRRPGAGSEGYDSLKRHPFFKGVDWKNLRSQTPPKLAPDPASQSASPERDGSPWNPTHVGDTSVLQNDGHNGLSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPRLIYVDPSKLVVKGNIIWSDNSNDLNVQVSSPSHFKICTPKKVLSFEDAKQRALQWKKAIETLQNR
Protein: ATPase 2, plasma membrane-type (PM H(+)-ATPase 2) (Plasma membrane-type ATPase 2) (EC 7.1.2.1) (Proton pump 2) (P19456)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses. Involved in maintaining the membrane potential and delta-pH, together forming the plasma membrane protonmotive force (PMF) required for root and hypocotyl elongation and root tropism. Important for root growth and development during different nitrogen regimes. Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10995773, ECO:0000269|PubMed:25267325, ECO:0000269|PubMed:26071421, ECO:0000305|PubMed:15308754}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ferric reduction oxidase 2
- Phytosulfokine receptor 1
- Fe
- RPM1-interacting protein 4
- Cyclic nucleotide-gated ion channel 17
- CBL-interacting serine/threonine-protein kinase 11
- Tyrosine-sulfated glycopeptide receptor 1
- 14-3-3-like protein GF14 phi
- Protein RALF-like 1
- Transcription factor ORG2
Sequence:
MSSLEDIKNETVDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANGDGRPPDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEFDFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDNNHELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVYANWEFAKIRGIGWGWAGVIWLYSIVTYFPLDVFKFAIRYILSGKAWLNLFENKTAFTMKKDYGKEEREAQWALAQRTLHGLQPKEAVNIFPEKGSYRELSEIAEQAKRRAEIARLRELHTLKGHVESVVKLKGLDIETPSHYTV
Protein: Elongation factor TU, putative (Q388R1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein uL5
- Ribosomal protein
- 50S ribosomal protein L17, putative
- 40S ribosomal protein S15a, putative
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S18, putative
- Small ribosomal subunit protein uS5
- Elongation factor Ts, mitochondrial
- 40S ribosomal protein S5, putative
- Large ribosomal subunit protein bL21m
Sequence:
MFRAAFRCSLLNAKKEAFVRGKPHLIIGTIGHVDHGKTTLTSAITTVLAKAGKARALDYFAIDKSPEEKSRKITINATHVEYESEKRHYGHIDCPGHMDFVKNMITGAAQMDGGILVVAANDGCMPQTREHLLICSQIGLPALVGFINKCDLMQGQEDMIELVEMELRELLEKYKFPAEETPLVRGSAVKALEGDTDSEARIMELVAKCDEWIPDPPRATEKPFLMPIEHVYEIGKDKKSVIVTGRVDQGLMKLGADAELSGFSAKKLTVKVTGIEMYHKTLEECMPGDSVGASILGTGDTTTLSKDNVERGMVLSAPGATKLFNKVRAQVYVLTKDEGGRHTAFSPHYRPQLFFRCADVTADLNFPESEQKVAELNKKYGKDADEQKKKDAELKEFEKTLVCMPGDSRELVLTLAYPMPMEKGLKFTIREGKITVGWGAVTECLALDPKVNIEGVKQVKAVTGKSKKKK
Protein: HLA-C protein (A0A583ZBW8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MRVMEPRTLILLLSGALALTETWACSHSMRYFYTAVSRPSRGEPHFIAVGYVDDTQFVRFDSDAASPRGEPRGRWVEQEGPEYWDRETQKYNRQAQTDRVNLRKLRGYYNQSEAGSHTLQRMYGCDLGPDGRLLRGYDQSAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAAREAEEWRAYLEGECVEWLRRYLENGKEKLQRAEHPKTHVTHHPVSDHEATLRCWALGFYPTEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEPSSQPTIPIVGIVAGLAVLAVLAVLGAVVAVVMCRRKSSGGKGGSCSQAASSNSAQGSDESLIASKA
Protein: 5-deoxy-D-ribulose 1-phosphate aldolase (EC 4.1.2.-) (5-deoxyribose disposal aldolase) (P0DTQ0)
Organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)
Function: Catalyzes the cleavage of 5-deoxy-D-ribulose 1-phosphate to yield dihydroxyacetone phosphate (DHAP) and acetaldehyde, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. Is also able to catalyze the reverse reaction, using several aldehydes as substrate, with acetaldehyde being the preferred substrate.
Interaction partners:
Sequence:
MLLQKEREEIVAYGKKMISSGLTKGTGGNISIFNREQGLVAISPSGLEYYETKPEDVVILNLDGEVIEGERKPSSELDMHLIYYRKREDINALVHTHSPYAKTIASLGWELPAVSYLIAFAGPNVRCAPYETFGTKQLADAAFEGMIDRRAVLLANHGLIAGANNIKMAFTVAEEIEFCAQIYYQTKSIGEPKLLPEDEMENLAKKFEGYGQQ
Protein: Krueppel-like factor 1 (Erythroid krueppel-like transcription factor) (EKLF) (Q13351)
Organism: Homo sapiens (Human)
Function: Transcription regulator of erythrocyte development that probably serves as a general switch factor during erythropoiesis. Is a dual regulator of fetal-to-adult globin switching. Binds to the CACCC box in the beta-globin gene promoter and acts as a preferential activator of this gene. Furthermore, it binds to the BCL11A promoter and activates expression of BCL11A, which in turn represses the HBG1 and HBG2 genes. This dual activity ensures that, in most adults, fetal hemoglobin levels are low. Able to activate CD44 and AQP1 promoters. When sumoylated, acts as a transcriptional repressor by promoting interaction with CDH2/MI2beta and also represses megakaryocytic differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21055716, ECO:0000269|PubMed:25585695}. Note=Colocalizes with SUMO1 in nuclear speckles. {ECO:0000250}.
Interaction partners:
- Erythroid transcription factor
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- Hemoglobin subunit gamma 1
- T-cell acute lymphocytic leukemia protein 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-B
- Alpha-hemoglobin-stabilizing protein
- Glycophorin-A
- Protein 4.2
Sequence:
MATAETALPSISTLTALGPFPDTQDDFLKWWRSEEAQDMGPGPPDPTEPPLHVKSEDQPGEEEDDERGADATWDLDLLLTNFSGPEPGGAPQTCALAPSEASGAQYPPPPETLGAYAGGPGLVAGLLGSEDHSGWVRPALRARAPDAFVGPALAPAPAPEPKALALQPVYPGPGAGSSGGYFPRTGLSVPAASGAPYGLLSGYPAMYPAPQYQGHFQLFRGLQGPAPGPATSPSFLSCLGPGTVGTGLGGTAEDPGVIAETAPSKRGRRSWARKRQAAHTCAHPGCGKSYTKSSHLKAHLRTHTGEKPYACTWEGCGWRFARSDELTRHYRKHTGQRPFRCQLCPRAFSRSDHLALHMKRHL