wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich repeat protein (LRRP), putative (Q38D13)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVWKGQAKGKQQNNGKNILKGKRRLLATGPQQEPEVNTPTVNANSNVMKSLRKRDRPTEELQQVGDVSVGATEASSVLNNAERERKDTSAADGDTTHPNLLSDGQEVSLKGTKVDKNTLQPLQASVTLRKLSVTVKEEDVDVQQLTSLKMLKDLCIEYVSGKILNVTSLKELSHMERLCFKGSCIEELEELTLNGCEELKKIEGIHLLPNLTILNLGRTSTNDDFLKELSVCKKLSKLTLSGCPGLENVEQLSNFATLKELSLSWCSNIIHGWEGIGQLPQLRVLHLEGNKITNRTLEPISKSKSLVSLDVSFCEKLTDATPLCRVKTLEELNLHATKITSGIDNLVLLPRLRVLDVRQLQLSAFDTILSTFAAVRYGIRLSSFCNGFDIQSISSIQTLEELSVGGFFCAAIQFGSIGGLPRLRVLRLSSKTMFDESLKGISHSRSLVAFDLSGCSCLEDISSISGIKTLEALSLRDCTNVSDGWIALGELPLLRILDLSCTKIQDVMLRVLFPKLKLDCLSLAGCENITHIGPLINVKSLKNLVLEECSELKAGFEALLELPLLTWVDLCYVNDNKTVKDTLVARGVDMRSVWSIIGNCTSLFDWWRAK
Protein: Metallothionein A (MT-A) (P68503)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Metallothioneins have a high content of cysteine residues that bind various heavy metals.
Interaction partners:
Sequence:
MDPCECSKTGSCNCGGSCKCSNCACTSCKKASCCDCCPSGCSKCASGCVCKGKTCDTSCCQ
Protein: Mediator of RNA polymerase II transcription subunit 20a (Q6NPF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 33A
- Mediator of RNA polymerase II transcription subunit 33B
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 32
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 16
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 25
Sequence:
MPVKWVLHWQPNQGSTVSSQILNEATQCVESINGVKEGRWKATLNYYKPMLKDQANQLEFPRDFLGISLADQPNKYYFIIRTQRIVLEADSSIQLIMEKLQSYKSKVALYFDGFQYQLGDFRLRVGKVVPTHSENVRGIVMEVEYLPISSMEKAQKVMEEFLEIWNEALAKRSLPGKFVNIDLNFGEFGLGDIYTPQHTAVRYALVMAHMIATVQAVRG
Protein: ABC transporter C family member 3 (ABC transporter ABCC.3) (AtABCC3) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 3) (Glutathione S-conjugate-transporting ATPase 3) (Multidrug resistance-associated protein 3) (Q9LK64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates. Mediates the transport of glutathione conjugates such as chlorodinitrobenzene-GS (DNB-GS), and of chlorophyll catabolites such as Bn-NCC-1. Transports also heavy metals such as cadmium (Cd).
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Glutathione gamma-glutamylcysteinyltransferase 1
- Vacuolar cation/proton exchanger 4
- Metal transporter Nramp4
- Putative inactive cadmium/zinc-transporting ATPase HMA3
- Metal transporter Nramp3
- Putative cadmium/zinc-transporting ATPase HMA4
Sequence:
MDFLGSTTGSGTLAMLFSFSESILPLDSRSFLLKPLFLRWLSGFLHSVLLLVLFFSWVRKKIRGDSGVTESLKDRRDFGFKSALFCSLALSLLNLVLMSLSGFYWYESGWLDNEQLVSSLGFLLGMVSWGVLSICLHRCRDCEHKKAPFLLRLWLVFYLVVSCYSLVVDFVMYERRETVPVHLLVFDIVAFIAAVFLGYVAVLKKDRSNSNGVLEEPLLNGGDSRVGGDDSVELNKTNGSGEATPYSRAGILSLLTFSWMSPLIDIGNKKTLDLEDVPQLHDTDSVVGLAPKFRSMLESPDGGERSGVTTFKLIKALYFTAQWEILVTAFFAFIYTVASYVGPALIDTFVQYLNGRRQYNHEGYVLVITFFAAKIVECLSQRHWFFRLQKVGIRMRSALVAMIYEKGLTLSCQSKQGRTSGEIINFMTVDAERIGNFSWYMHDPWMVLLQVGLALWILYRNLGLASIAALVATIIVMLINFPFGRMQERFQEKLMEAKDSRMKSTSEILRNMRILKLQGWEMKFLSKIFDLRKSEEGWLKKYVYNSAVISFVFWGAPTLVSVSTFGACILLGIPLESGKILSALATFRILQEPIYNLPDTISMIVQTKVSLDRLASYLCLDNLQPDIVERLPKGSSDVAVEVINSTLSWDVSSSNPTLKDINFKVFPGMKVAVCGTVGSGKSSLLSSLLGEVPKVSGSLKVCGTKAYVAQSPWIQSGKIEDNILFGKPMERERYDKVLEACSLSKDLEILSFGDQTVIGERGINLSGGQKQRIQIARALYQDADIYLFDDPFSAVDAHTGSHLFKEVLLGLLCSKSVIYVTHQVEFLPAADLILVMKDGRISQAGKYNDILNSGTDFMELIGAHQEALAVVDSVDANSVSEKSALGQENVIVKDAIAVDEKLESQDLKNDKLESVEPQRQIIQEEEREKGSVALDVYWKYITLAYGGALVPFILLGQVLFQLLQIGSNYWMAWATPVSEDVQAPVKLSTLMIVYVALAFGSSLCILLRATLLVTAGYKTATELFHKMHHCIFRSPMSFFDSTPSGRIMSRASTDQSAVDLELPYQFGSVAITVIQLIGIIGVMSQVSWLVFLVFIPVVAASIWYQRYYIAAARELSRLVGVCKAPLIQHFSETISGATTIRSFSQEFRFRSDNMRLSDGYSRPKFYTAGAMEWLCFRLDMLSSLTFVFSLVFLVSIPTGVIDPSLAGLAVTYGLSLNTLQAWLIWTLCNLENKIISVERILQYASVPSEPPLVIESNRPEQSWPSRGEVEIRDLQVRYAPHMPLVLRGITCTFKGGLRTGIVGRTGSGKSTLIQTLFRIVEPSAGEIRIDGVNILTIGLHDLRLRLSIIPQDPTMFEGTMRSNLDPLEEYTDDQIWEALDKCQLGDEVRKKEQKLDSSVSENGDNWSMGQRQLVCLGRVLLKRSKILVLDEATASVDTATDNLIQKTLREHFSDCTVITIAHRISSVIDSDMVLLLSNGIIEEYDTPVRLLEDKSSSFSKLVAEYTSRSSSSFD
Protein: UPF0266 membrane protein YobD (P67601)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- UPF0162 protein YchA
- PTS system mannose-specific EIID component
Sequence:
MTITDLVLILFIAALLAFAIYDQFIMPRRNGPTLLAIPLLRRGRIDSVIFVGLIVILIYNNVTNHGALITTWLLSALALMGFYIFWIRVPKIIFKQKGFFFANVWIEYSRIKAMNLSEDGVLVMQLEQRRLLIRVRNIDDLEKIYKLLVSTQ
Protein: Oligophrenin-1 (Q99J31)
Organism: Mus musculus (Mouse)
Function: Stimulates GTP hydrolysis of members of the Rho family. Its action on RHOA activity and signaling is implicated in growth and stabilization of dendritic spines, and therefore in synaptic function. Critical for the stabilization of AMPA receptors at postsynaptic sites. Critical for the regulation of synaptic vesicle endocytosis at presynaptic terminals (By similarity). Required for the localization of NR1D1 to dendrites, can suppress its repressor activity and protect it from proteasomal degradation.
Subcellular location: Postsynapse {ECO:0000269|PubMed:21874017}. Presynapse {ECO:0000269|PubMed:21874017}. Cell projection, axon {ECO:0000269|PubMed:21874017}. Cell projection, dendritic spine {ECO:0000269|PubMed:21874017}. Cell projection, dendrite {ECO:0000269|PubMed:21874017}. Cytoplasm {ECO:0000269|PubMed:21874017}. Note=Present in both presynaptic and postsynaptic sites. {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- Transforming protein RhoA
- Rho guanine nucleotide exchange factor 6
Sequence:
MGHPPLEFSDCYLDSPDFRQRLKYYEEELERTNKFIKDVIKDGSALISAMRNYSSAVQKFSQTLQSFQFDFIGDTLTDDEINIAESFKEFAELLNEVENERMMMVQNASDLLIKPLETFRKEQIGFTKERKKKFEKDGERFYSLLDRHLHLSSKKKESQLLEADLQVDKERHNFFESSLDYVYQIQEVQESKKFNIVEPVLAFLHSLFISNSLTVELTQDFLPYKQQLQLSLQNTRNHFSSTREEMEELKKRMKEAPQTCKLPGQPTIEGYLYTQEKWALGISWAKYYCRYEKETRMLTMIPMEQKPGAKQGPVDLTLKYCVRRKTESIDKRFCFDIETNERPGTITLQAPSEANRRLWMEAMDGKEPIYHTPITKQEEMELNEVGFKFVRKCINFIETKGIKTEGLYRTVGSNIQVQKLLYAFFDPKCPGDVDFHNSDWDIKTITSSLKFYLRNLSEPVMTYKLHKELVSAAKSDNLDYRLGAIHSLVYKLPEKNREMLELLIKHLVNVCEHSKENLMTPSNMGVIFGPTLMRAQEDTVAAMMNIKFQNIVVEILIEHFGKIYLGPPEDSQVPPVPPPRVTARRHKPITISKRLLREKTVFYTSSLDENKDESHHQTPNGTITSNLDPPKLLQHLKPPMQKSGETDPGRKSPSRPVSDCQSEPCLETDVGRLLFRLQDGGTKATPKASNGPVPGSGHTKTSSFHIRRPAPRPMAHHKEGDTDGFSKVRPPGEKQTIIRPPVRPPDPPCRSITPQKPEPKPETGSGNADEIPSSVVASRTRFFETASRKTGSSQGKLPGDES
Protein: Actin-87E (EC 3.6.4.-) (P10981)
Organism: Drosophila melanogaster (Fruit fly)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9344535}. Note=Associated with spectrosomes during female cystocyte proliferation and differentiation, but dissociates, or becomes undetectable, upon fusome maturation (PubMed:9344535). Component of the inner rim of ring canals connecting the cytoplasm of nurse cells and oocyte during oogenesis (PubMed:9344535). {ECO:0000269|PubMed:9344535}.
Interaction partners:
- Actin, larval muscle
- Adenylyl cyclase-associated protein
- Actin-42A
- Actin, indirect flight muscle
- RuvB-like helicase 1
- DNA methyltransferase 1-associated protein 1
- Enhancer of polycomb-like protein
- RuvB-like helicase 2
- Brahma associated protein 55kD
- Transcription-associated protein 1
Sequence:
MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANIVMSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF
Protein: Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2) (Q6H8Q1)
Organism: Homo sapiens (Human)
Function: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity.
Subcellular location: Cytoplasm. Note=In skeletal muscle, sarcomeric or cosarcomeric localization. {ECO:0000250}.
Interaction partners:
- Actin-binding Rho-activating protein
Sequence:
MSAVSQPQAAPSPLEKSPSTAILCNTCGNVCKGEVLRVQDKYFHIKCFVCKACGCDLAEGGFFVRQGEYICTLDYQRLYGTRCFSCDQFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECMCQKCSLPVSVGSSAHLSQGLRSCGGCGTEIKNGQALVALDKHWHLGCFKCKSCGKLLNAEYISKDGLPYCEADYHAKFGIRCDSCEKYITGRVLEAGEKHYHPSCALCVRCGQMFAEGEEMYLQGSSIWHPACRQAARTEDRNKETRTSSESIISVPASSTSGSPSRVIYAKLGGEILDYRDLAALPKSKAIYDIDRPDMISYSPYISHSAGDRQSYGEGDQDDRSYKQCRTSSPSSTGSVSLGRYTPTSRSPQHYSRPGSESGRSTPSLSVLSDSKPPPSTYQQAPRHFHVPDTGVKDNIYRKPPIYRQHAARRSDGEDGSLDQDNRKKSSWLMLKGDADTRTNSPDLDTQSLSHSSGTDRDPLQRMAGDSFHSRFPYSKSDPLPGHGKNGLDQRNANLAPCGADPDASWGMREYKIYPYDSLIVTNRIRVKLPKDVDRTRLERHLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF
Protein: Solute carrier organic anion transporter family member (A0A089G2A6)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}.
Interaction partners:
Sequence:
MSVETKAPRVPCCSKLKLFLISLSFVYFAKAFGGSYMKSSVTQIERRFDIPSSLIGVIDGSFEIGNLLVIAFVSYFGAKLHRPRLIGIGCLIMAAGAFLTALPHFFQGQYVYETTLSHIPEENSTESILPCLANTSHLVMNDLSTAASKAACEKEAGSSMWIYVFLGNMLRGIGETPVMPLGVSYLDDYARKENTAIYLACLQTVGILGPVFGFMFGSFCAKIYVDIGSVDLESISINHKDSRWVGAWWLGFLVSGFLMLLAGIPFWFLPNTLAKQCKSPSKKRQKEDIQAKSSSDTPEVEPEQGSFLPEDNTEEDAPQPVTMAAMAKDFAPSLKRLFSNKVYLLIILTSVVAFNGFIGMITFKPKFMEQVYGQSPSKAIFLIGSMNLPAVAVGVIVGGLVIKRFKLSVLGAARLSIVSSFLSFCLLLIQYFLQCDNSEVAGLTMTYQGATEVSYQQESLLSQCNMGCSCSLKHWDPVCARNGITYASPCLAGCQTSTGVGKEMEFHNCTCMQELKGGLMAPPTNMSAILGQCPRKSDCDRMFKFYMAVTVLGAFVSACGGTSGYIVLLRSIHPDLKSLALGMHTLIGRTLGGIPPPIYFGALIDRTCLKWGLKRCGGQGACRFYDSHAFRITFLGLVYCLYGLANLLWGVLYLQLSKRQKKLELRSQAKATALEANGNNNPNGHAMVSIFKNKDDRDRDNESTI
Protein: CBFA2/RUNX1 partner transcriptional co-repressor 3 (H3BNI7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTLMNGSSHSPTAINGAPCTPNGFSNGPATS
Protein: Curing of [URE3] protein 1 (Q06469)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the curing of prion [URE3]. Nuclear localization of this protein may suggest a role in transcription regulation, so it might exert an effect on [URE3] through known prion-curing chaperones or BTN2.
Subcellular location: Nucleus {ECO:0000269|PubMed:18833194}.
Interaction partners:
- Protein SIS1
- Heat shock protein 42
- Protein BTN2
- Mitochondrial protein import protein MAS5
- Heat shock protein 104
- Transcriptional regulator URE2
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF12
- SAGA complex/transcription factor TFIID complex subunit TAF5
- SAGA complex subunit SPT3
Sequence:
MAAACICQPNLLEINVSDGPLDMIRKKRKIQQPQLRPPLRENKCQPHFSVRKVNQSYIISLHKEITCQLIAEIVKQKLSRIWEKVYIPSYELISDKDGNQIYVEQSVDENRLTSEIMEKLDPNNIDIEAIEILFDDYHLELSRLTNGIIISSANDHFYREFSFNNIIDDNFKICGTSMSADSFDKIYGVMWIEVPFNGNGLQNDSAVNRVSTSHNQIEELNDIEQEIRAFNISRSNQESIIKKEVSRRLNGR
Protein: Crescerin-like protein che-12 (Q17423)
Organism: Caenorhabditis elegans
Function: Required for normal structure and function of sensory cilia on amphid neurons, especially for the formation of distal ciliary structures, but is less important for normal assembly of middle and basal ciliary structures. Plays a role in the organization of axoneme microtubule bundles in sensory cilia. Required for normal structure and function of the ASER neuron that mediates attraction to NaCl. Required for normal chemotaxis to NaCl. Required for normal avoidance response to high osmolarity. In contrast, is not required for normal chemotaxis to isoamyl alcohol. Does not play a role in intraflagella transport (IFT). Promotes dauer formation in response to pheromones such as the ascarosides ascr#2, ascr#3, ascr#5, ascr#8 and icas#9.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}. Perikaryon {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}. Cell projection, dendrite {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}. Note=Detected in neuronal cell bodies, and to a lesser extent in dendrites. Detected in ASER cilia (PubMed:18245347, PubMed:26378256). Requires the intraflagella transport (IFT) machinery for normal location in cilia, but does not play a role in IFT itself (PubMed:18245347). {ECO:0000269|PubMed:18245347, ECO:0000269|PubMed:26378256}.
Interaction partners:
- Rootletin
- WD_REPEATS_REGION domain-containing protein
- Serpentine Receptor, class AB
- F59G1.4
- Intraflagellar transport protein osm-1
- Intraflagellar transport protein 88 homolog
- Intraflagellar transport protein che-13
Sequence:
MTSLFDALSRSNDRLPSPNFLPEDFLELLKSNDFDTKLTTLIRAATIAKREEDWFHKFQKKGELFKCIDKIICDDRWELQHQCIKFLVEAMPTFGSATEYCMCFVMPNLIPKLVSNKVTVRKITHQAIATFLRLKPEALQSFLKMLSNFMPNCNSKSELITELHHILIPELVKSNWTCLVENFTTESNIQGCEDQAGVLMKKLHYFIGNEFWQKIITNLSPEKREVLEQITANVQVEHTESKAGSGVLRASAKPQSGGERRLRFGIVPSLVCALIAEDTDANQRISGLEKMKQVVDQITPEEIARLVPHLHSYLLMLSNVLEDLNFKVVVLALDIVRATGHHLKGHMEAHIQQFVNLVAKHFGNQKSVIKQIIMMTFMELFQNINPKTVGGCLRVFLENKNSRVREEVINIYTASLMTISPSKFNLQPLVNILVPMFHDVKKRVRLAAFEQLSVLAYLLNGKTEIIMKPVRDFEQDQNSRGLTEAVTARIRRQVLPRIRYDGLIEYSTPPMMDSFDLAEAEMSLPSNADLSWIVSNGGVEPDPFERTMSPISLAGNLATIRRNRVIQQQGQAEKPSFSLPQQPAQQASHQAQRLPNGIEKSHETSENSSLDIGQRIVMTRMKSDDSFVRRQGSAASNPNSSTSSWEAPKRPPISPSEKSSISATKKEVNNNHIVKKGNLKSMRARSDTNLSEDHGEEEMENDPPRSFDDRPAKASGQYSFQDFDAAIVPSSMGKKSISHHSLPITSHPPLKHAISQPQKRINNNGTFLRSGQGQRTKSVSKPHRELTAVSKTYSLLDTSNMSVNQALKKMSSDEWADKVDGLNMISTLSETQPRMVADNLKEVIIAILNECKNLRSSVSRVAIVTIGTVAQNLNSKIDSEMEKICAVLLSKSGDVSNAFIRDDATDSLNKLVKAATAGKALQGIILAGAKSKNNTIRSSCANFVYDIITIQGSSAILNNQNALSNVLPVLLQFSRDQSPQVRNPGKQSLCFLSKDPNFDRLMRKNALESEIKAVKDVLANVEKRGGVDSLESTANLSGSLSRIGSTRRVQKKLPDSLQLDLDEIRTELLAAGWERRLTGLQRFEEMCGHASKAVASDTRLIEAFISRLGDTNGKVASCAMETYISTMGSMAKLYSTESNLKAVMNQLAHALTAHLSSKSEEHKHLARTCIQHTIRSIEPVSLLPAMTSATKKSNVKQRPFILTQYCELSKLAYKSKPKQVEVMALPLLWDSVKNSAPDVDNKKATQYLAKTLAKLIGEKQLLDLATSELDPNRKKQLDALIR
Protein: SEC7 domain-containing protein (Q581Z8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ADP-ribosylation factor-like protein, putative
Sequence:
MQLAPNKTVVDLENRATFMVQLHAFLLQARHVVSGTPKGKLQEVLRNVDEWIKEVSLGDATTSSGSASGNASVTERTGGEASGPLRQGASEADTGAAEDPKPPPNSSPSASPCEDPSPATAVAAEGDERGQLVHPDPNAGFSSDLSKRNLEDLARFLATLFVGTSSENGKLRNIARNAARIVITRCFSIIDNTLRQVLREVYDDPTANNGGEAGGNGAARRKESNPLFVSLGHDINVCRNTIGICVDTLSGSTDFPSVRFAVQVCIDILKQLRQCVVHFERQFASREIGHIQDMVEATGNGHNGEVRAADDEEDRCMAEQRVEELKRLLGPTLLESITHLVGLVRPVVGYLFSIVSVKSATASEDERTTKSDVVSNLFGFAKWYGRTSHLSRCGDASVDDSVTLSRSTEFDDNVPIHSRSHRILCCVLESVLATSFSPEYTACVAQHCGDRAEGQFLAVRLLKDTVSELCEGSAAELEYVLRHDNWRKRILDGIFNCVMSLRPSVLDAGLETLRRVVTSCPDCLSTEVGSIYCNGIFGLLGSDSTPPFMQRSFLHHIIDTFFQGSAVSGEAPLLLRCYRRFDLNVHWHQLNLIQKVVTVLSRAVCTARPEEFVDIEGPKPRASGTASGSAVGNAEASNESIVYAETGGGDSANVTQTVNCASFADDGTVMMQRSVPFLALHGLALVVEILTKQIPQNTGLSNWKPLPRLLNRKKKIEQLRFVEAINSSPIKGLRKLFNIRDEEWQTEADRAIAENNWSHRHIPEPATPQAEEKVQHIAQFLMETPSLNSDAVAEILSYPAVISLQVCRAFMDLLPLAGKTLINGLRELFRVVKLPKEGQRIERLIEFFCSAYYKAGSRSCVDTDVFPFASEDACFIAGIGIIMLNTNLHNPNVSTTKMTAASFYAQMRGCNDNKDFPRRFTDSVFEEVSTRSLSNVHESMLTEAKRRGSVVSHMRMDAFFFTSEDRKEAEFNVVRRRLTDETRELLFRSSRLCEDDGEIREGGDTEQEYWTSVTQDLFLSTWPSLNAVFGAAVDGNQIPEDALLLYATGLRSSLLLSAAFGLHTECDAAQMALVRLSAFDSLRDVCHGCLLEVASSRHSVHFSSRCWLPVVELLVTIRKEQSQTQSQQSYQQQSQSQQQQRRAILVQMESLFGHLEEITREYCNMSVHEAPPVIVVAVRELLQGVAALLRDQGMDFPTLTAALYVVRRVLSYSVISHDQELGPVVTNLINVRDLSGIVMPALVDVVEARREKGDECLHAVTSFVVDVLSVVWNSCVRDANCSHQAVKLTELANCFCFFQMCHERCVNSSVVQMHMLQGVKELVSCTVLAESSVKQRTTRGVQTRVSFTMALVWERLLHSVAHALSGKSTVGTETCSLAVHVLQKLVLICCGAGSVPPSVQMRQEPLNVLLSLLCNVAYVGGMCSDVESAQSCLAQLSCVCTAALNREVTTSLEATAVTSDEDDYEVDGLNEVQVQLTRRLLQGIQGQDDFTVLHALERICMLLGCHTQETRTEAIGVLRAVSKQLGVRDQKQHLAVQLADTVLQVLLGHTAPGSKSSANTPEAAEDVGRVSFAILNLRTPPTMRKCPAVAFHATLPQLLNFMSHELIVDASLEDVASLGAVVMERCLLPLAVSQKSSSHVRPLAVRSMMQCATLCVAALGKLSESSAAREKAAGDRCLNAIINSVSLVLLDTHLFKQSIVPHNAQYVGSRWDAGLSQMLGAYSKAGRSAIRALSASDPCNITGSRGCVTLSMRMLHEEQVSEHSKVAPNDLPGKKQGTVAGCEEGLSSGTDSTVLSDEQLVEYCNLMAPLLSPLPKVLAAITPAMYTRSERPFSGDEGASTTEGCEQPVWWSPPPCNYKLMAELLLDAEGAFFAVLWRVNHASEMDQFVMQSVTKGREATPLSKSSALLPHTAVRGGLNAYLSLALQMDFSHLRHVLVEILEEVAFVQSLSSGSRKPRRTGDSMSDSPVGQQLSPREQQHVRSCNVGMYQELTSVVVHWVKNLMYQLDPETSALTGQRQSELADVVRDPEVFKGLVQLLTAAGGSIVSTVRDYLTWYIEAQQR
Protein: Type 1 encapsulin shell protein (Q2RVS0)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Shell component of a type 1 encapsulin nanocompartment. Assembles into proteinaceous icosahedral shells 24 nm in diameter in the presence and absence of its ferritin cargo protein. The center of cargo-loaded nanocompartments is loaded with iron. The empty encapsulin nanocompartment sequesters about 2200 Fe ions while the cargo-loaded nanocompartment can maximally sequester about 4150 Fe ions. Does not have any detectable ferroxidase activity.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:27529188}.
Interaction partners:
- Encapsulated ferritin-like protein
Sequence:
MNDLMRDLAPISAKAWAEIETEARGTLTVTLAARKVVDFKGPLGWDASSVSLGRTEALAEEPKAAGSAAVVTVRKRAVQPLIELCVPFTLKRAELEAIARGASDADLDPVIEAARAIAIAEDRAVFHGFAAGGITGIGEASAEHALDLPADLADFPGVLVRALAVLRDRGVDGPYALVLGRTVYQQLMETTTPGGYPVLQHVRRLFEGPLIWAPGVDGAMLISQRGGDFELTVGRDFSIGYHDHDAQSVHLYLQESMTFRCLGPEAAVPLRGLSQAATKA
Protein: Protein SPT2 homolog (E1BUG7)
Organism: Gallus gallus (Chicken)
Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription. Binds DNA and histones and promotes nucleosome assembly (in vitro) (By similarity). Modulates RNA polymerase 1-mediated transcription. Required for optimal growth in the presence of the DNA damaging agents actinomycin D or mitomycin C (in vitro). Facilitates formation of tetrameric histone complexes containing histone H3 and H4 (By similarity). Modulates RNA polymerase 1-mediated transcription (By similarity). Binds DNA, with a preference for branched DNA species, such as Y-form DNA and Holliday junction DNA (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:23378026}.
Interaction partners:
- M-phase phosphoprotein 8
- Mitochondrial ribosomal protein L40.
- Non imprinted in Prader-Willi/Angelman syndrome 2
- Prune homolog 2 with BCH domain.
Sequence:
MDFHNILVMASEQQGLNAVPKRYSLAVGPPKKVPKVKGVESAAVQAFLRRKEEEKRKKELEEKRKKERLLAKRIELKHDRKARAMASRTKDNFYGYNGIPVEEKPKKRRRTCENVSQAPEAEYATENEAEQLEFAQTESEYEQEEYDEKPSKAAVKPKAPPKSAPAPLNFADLLRLAEKKQYEPVEIKVVKKIEERPRTAEELREREYLERKNKRVETQKKKSEKEVKSAGISSSSKKATSLKECADAKLSRSAADKHAPPKSSLSSLSGTDKKPKAPALTEKHSRSFSSSKLSQMEKGKTSQNSSLKSPAAGSHSKLPANGMGKTGSSFPVPSSKPMANGAQRLPSAKESSLKKPVHTKPGNAAALQHETNSSAKRPSSSLGKGGSGHPAGGSSAGPGRSSSNSGTGPGRPGSVSSPGPGRQGSSSAAGPGRPSSSSSLGPGRLGSGSGVGPGRPGGSSSTGLGRPGGSSGTGPGRPGNSTNTAPGRLGSGMGTGPGRPGVGPSAGPGRPGSSSGTGPGRPGVSPSAGPGRPGLTAVKPRCTVVSETISSKNLVTRPSNGQINGMRSPPGHRPVFRPQGIGRPPVGYKRQIDDDDDDDEYDSEMDDFIEDEGEPQEEISKHIREIFGYDRKRYKDESDYALRYMESSWREQQKEEARSLRLGVQEDLEELRREEEELKRKRQSKKLRTR
Protein: Mitochondrial carrier protein, putative (Q38BB0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLAKDVDAGRSTTSSTTGVPYIPTDVIVKKVAPLIFLPPEHIRELVQCFDHEGKGGLSEAQWSRFCEEHHKRFTSLGQYEIDFERFQYYGEFSATEEPSSAARVVQGVVRFLEGFAAGGIAGAVSKTVIAPADKVKIIFQVDSQRRFSLYNACKLGMATVRKHGIAGLWIGNGATMIRVVPYAAVTFVTFDYYREGFQYLLIADRTSTSKNEGTMVIIRFLSGSLSGATATACTYPLDLMRARLAVHNFDKGVIPSYCRAYRSLVADHGWRSLYSGLVPTVIGIMPYAGCSFAVFETLKSYIVRWRELSSEKSISVHERIVAGGFAGLVAQSATYPLDIVRRRMQVTPGRYRGVFHALRVIYKEEGFLQGWYKGLSMNWIKGPIAVSTVFTVNDIVKRRMREYDEEVVKYSRRGNLVSLPEGLVCGMMAACVAQTCTAALLQLKILFQVCLGRLYSRTTGRHGPLSSGLLCWRGVAAHGGDVTMMRVISYGALTYSLFDICQTASERLLFSLTPTPATNFVAGAVATAAATALLYPIAHVGARAVKHTTPRHFHSHYWLLHDIAKAQSPRSFREWSTFAAMGVGPVGGVGFATYEFLKEHCHCTSFGQRLFAGVLASFVGHVTTYFINVGRRRGQVEQLTSSGVVDAKSVCLKPGFYASFRRCMPRRWPVSATTFGISLAVNDMCRDLVIQERKEILHDIFFTR
Protein: Mitotic spindle assembly checkpoint protein MAD2A (HsMAD2) (Mitotic arrest deficient 2-like protein 1) (MAD2-like protein 1) (Q13257)
Organism: Homo sapiens (Human)
Function: Component of the spindle-assembly checkpoint that prevents the onset of anaphase until all chromosomes are properly aligned at the metaphase plate. In the closed conformation (C-MAD2) forms a heterotetrameric complex with MAD1L1 at unattached kinetochores during prometaphase, the complex recruits open conformation molecules of MAD2L1 (O-MAD2) and then promotes the conversion of O-MAD2 to C-MAD2. Required for the execution of the mitotic checkpoint which monitors the process of kinetochore-spindle attachment and inhibits the activity of the anaphase promoting complex by sequestering CDC20 until all chromosomes are aligned at the metaphase plate.
Subcellular location: Nucleus {ECO:0000269|PubMed:19010891}. Chromosome, centromere, kinetochore. Cytoplasm {ECO:0000269|PubMed:19010891}. Cytoplasm, cytoskeleton, spindle pole. Note=Recruited by MAD1L1 to unattached kinetochores (Probable). Recruited to the nuclear pore complex by TPR during interphase. Recruited to kinetochores in late prometaphase after BUB1, CENPF, BUB1B and CENPE. Kinetochore association requires the presence of NEK2. Kinetochore association is repressed by UBD. Sequestered to the cytoplasm upon interaction with isoform 3 of MAD1L1 (PubMed:19010891). {ECO:0000269|PubMed:19010891, ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase Nek2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 20 homolog
- Mitotic spindle assembly checkpoint protein MAD1
- Mitotic checkpoint protein BUB3
- Anaphase-promoting complex subunit 10
- Cell division cycle protein 27 homolog
- Cell division cycle protein 16 homolog
Sequence:
MALQLSREQGITLRGSAEIVAEFFSFGINSILYQRGIYPSETFTRVQKYGLTLLVTTDLELIKYLNNVVEQLKDWLYKCSVQKLVVVISNIESGEVLERWQFDIECDKTAKDDSAPREKSQKAIQDEIRSVIRQITATVTFLPLLEVSCSFDLLIYTDKDLVVPEKWEESGPQFITNSEEVRLRSFTTTIHKVNSMVAYKIPVND