wanglab/gogpt-training-data huggingface dataset:
Protein: Aminopeptidase N (EC 3.4.11.-) (M1 alanyl aminopeptidase) (PfM1AAP) (M1 family aminopeptidase) (PfA-M1) [Cleaved into: p120 form; p96 form; p68 form; p35 form] (O96935)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.
Subcellular location: [Aminopeptidase N]: Parasitophorous vacuole membrane {ECO:0000269|PubMed:20591164}; Peripheral membrane protein {ECO:0000305}. Note=In trophozoites, partially localizes to the parasitophorous vacuole membrane. {ECO:0000269|PubMed:20591164}.; SUBCELLULAR LOCATION: [p120 form]: Nucleus {ECO:0000269|PubMed:21659511}.; SUBCELLULAR LOCATION: [p96 form]: Cytoplasm {ECO:0000269|PubMed:33536500}.; SUBCELLULAR LOCATION: [p68 form]: Cytoplasm {ECO:0000269|PubMed:33536500}. Vacuole lumen {ECO:0000269|PubMed:17895246, ECO:0000269|PubMed:20591164}. Note=In trophozoites, partially localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:20591164}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12166515, ECO:0000269|PubMed:9879894}. Note=In trophozoite and schizonts, localizes to the cytoplasm (PubMed:12166515). In trophozoites, also localizes around the digestive vacuole (PubMed:12166515). In schizonts, also localizes to discrete vesicle-like structures and in released merozoites localizes to a single discrete structure (PubMed:12166515). In ruptured schizonts, localizes around the digestive vacuole (PubMed:12166515). {ECO:0000269|PubMed:12166515}.
Interaction partners:
Sequence:
MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKNYNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNNNGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNVENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNVGEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPETNYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKVNEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVSKLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKKNSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTRLSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYKKGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNYDAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFVFNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNYNEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNLDTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNTLLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLLQEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKLIAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLRLTNKL
Protein: Ubiquitin-like protein NEDD8 (Neddylin) (Q9VJ33)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ubiquitin-like protein which plays an important role in cell cycle control, embryogenesis and neurogenesis. Covalent attachment to its substrates requires prior activation by the E1 complex Uba3-Ula1 and linkage to the E2 enzyme UbcE2M. Attachment of Nedd8 to cullins activates their associated E3 ubiquitin ligase activity, and thus promotes polyubiquitination and proteasomal degradation of cyclins and other regulatory proteins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15843}.
Interaction partners:
- Nedd8-activating enzyme E1 catalytic subunit
- Nedd8-conjugating enzyme UbcE2M
- Cullin homolog 1
- COP9 signalosome complex subunit 5
- Nedd8-activating enzyme E1 regulatory subunit
- Cullin-5
- COP9 signalosome complex subunit 6
- Cullin 3, isoform F
- Cullin-2
- Deneddylase 1, isoform C
Sequence:
MLIKVKTLTGKEIEIDIEPTDKVDRIKERVEEKEGIPPQQQRLIFSGKQMNDDKTAADYKVQGGSVLHLVLALRGGDSILTPCV
Protein: Sin3A associated protein 130 (Sin3A-associated protein, 130kDa, isoform CRA_d) (A0A2R8YDB8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSQQFPRLGAPSTGLSQAPSQIANSGSAGLINPAATVNDESGRDSEVSAREHMSSSSSLQSREEKQEPVVVRPYPQVQMLSTHHAVASATPVAVTAPPAHLTPAVPLSFSEGLMKPPPKPTMPSRPIAPAPPSTLSLPPKVPGQVTVTMESSIPQASAIPVATISGQQGHPSNLHHIMTTNVQMSIIRSNAPGPPLHIGASHLPRGAAAAAVMSSSKVTTVLRPTSQLPNAATAQPAVQHIIHQPIQSRPPVTTSNAIPPAVVATVSATRAQSPVITTTAAHATDSALSRPTLSIQHPPSAAISIQRPAQSRDVTTRITLPSHPALGTPKQQLHTMAQKTIFSTGTPVAAATVAPILATNTIPSATTAGSVSHTQAPTSTIVTMTVPSHSSHATAVTTSNIPVAKVVPQQITHTSPRIQPDYPAERSSLIPISGHRASPNPVAMETRSDNRPSVPVQFQYFLPTYPPSAYPLAAHTYTPITSSVSTIRQYPVSAQAPNSAITAQTGVGVASTVHLNPMQLMTVDASHARHIQGIQPAPISTQGIQPAPIGTPGIQPAPLGTQGIHSATPINTQGLQPAPMGTQQPQPEGKTSAVVLADGATIVANPISNPFSAAPAATTVVQTHSQSASTNAPAQGSSPRPSILRKKPATDGMAVRKTLIPPQPPDVASPRVESSMRSTSGSPRPAGAKPKSEIHVSMATPVTVSMETVSNQNNDQPTIAVPPTAQQPPPTIPTMIAAASPPSQPAVALSTIPGAVPITPPITTIAAAPPPSVTVGGSLSSVLGPPVPEIKVKEEVEPMDIMRPVSAVPPLATNTVSPSLALLANNLSMPTSDLPPGASPRKKPRKQQHVISTEEGDMMETNSTDDEKSTAKSLLVKAEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYSDVRVKEEKKAMLQEIANQKGVSCRAQGWKVHLCAAQLLQLTNLEHDVYERLTNLQEGIIPKKKAATDDDLHRINELIQGNMQRCKLVMDQISEARDSMLKVLDHKDRVLKLLNKNGTVKKVSKLKRKEKV
Protein: Membrane-associated protein (Q57TU3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSVTTGSSFYAAVLLVLLLTVTQCGNSKFPNLHCDNVWDGPSARNDPLTCIMDTDRILAQWRMLAMPALCAFLFVAVLIAFPISCFLTCLCSSRCKPSSKDGGKEQRCCLWMWIMFALIWAFGVAAFVFFGVKQLWATSNYFLDVTLMNPLNVVNCTAEKVIDFASNWTSGNREPYADGVDVSFFYDISENAVRVVEMLRGRAGDYIKLLPVVSYAVGSVCIALMAPMVILACCRRGPLIVPECFACAYFVFGLVFSVGGAVLFLLSYASSSVCGEIALHRERKPGIIQWYGIPLCNSKFRPDAINKKVTDAEIGICREACNYLLDNCDNLDMRGPSMSRFSGSSVSYDGYVPSGYLKDRNGKPNTRSSDISPDAPASFIASGFVSHAAARNVGGTFPVKVLTCGKNITSSDECPNFGITATVLEDTRVKAFVGSCPTPGNSCTVVECAANCTEGRAKNVSIEVVRVAARSRNVSVALSIGRPLLECNFMLDIALTAMPDCEDITPGVFMLSVGFLLGSLMFAVGIYVMLRGSCVWGSAKTSPEAS
Protein: Phosphoenolpyruvate carboxykinase [GTP], mitochondrial (PEPCK-M) (EC 4.1.1.32) (Q8BH04)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q16822}.
Interaction partners:
- Pyruvate carboxylase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- ATP-citrate synthase
- Citrate synthase, mitochondrial
- Citrate synthase
- Alpha-enolase
- Malate dehydrogenase, cytoplasmic
- Gamma-enolase
Sequence:
MAAMYLPGLRLSRHGLRPWCWSPCRSIQTLHVLSGDMSQLPAGVRDFVARSAHLCQPEGIHICDGTEAENTAILALLEEQGLIRKLPKYKNCWLARTDPKDVARVESKTVIVTPSQRDTVPLLAGGARGQLGNWMSPDEFQRAVDERFPGCMQGRIMYVLPFSMGPVGSPLSRIGVQLTDSAYVVASMRIMTRLGTPVLQALGDGDFIKCLHSVGQPLTGHGDPVGQWPCNPEKTLIGHVPDQREIVSFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITNPAGKKRYVAAAFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGQLRAINPENGFFGVAPGTSAATNPNAMATIQSNTLFTNVAETSDGGVYWEGIDQPLPPGVTITSWLGKPWKPGDKEPCAHPNSRFCVPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFNWRHGVFVGSAMRSESTAAAEHKGKTIMHDPFAMRPFFGYNFGRYLEHWLSMEGQKGARLPRIFHVNWFRRDEAGRFLWPGFGENARVLDWICRRLEGEDSAQETPIGLVPKEGALDLSGLSAVDTSQLFSIPKDFWEQEVRDIRGYLTEQVNQDLPKEVLAELEALEGRVQKM
Protein: Osteocrin (Osteocrin precursor) (E7F404)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphatase, orphan 2
Sequence:
MLGCGCVLLSCLLTLTLFHCSAESLHIPQGRPEYVESSVVEGRSVQRGQMEQKTSGALSAKLLLHDQLVRLENDVIETKRKRSFPGSNTPLDRLSISTMDPKSNKQRKAVELPRRRVSVPIDRIGVGRLPSSRG
Protein: Protein RMD5 homolog (Q9T075)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
Interaction partners:
- Protein GID8 homolog
- Ran-binding protein M homolog
- Protein MAEA homolog
- WD repeat-containing protein 26 homolog
- At4g09200
- WD repeat-containing protein WDS homolog
- SPla/RYanodine receptor
- ARM repeat superfamily protein
- At3g02460
- TBC1 domain family member 15
Sequence:
MELKSIKDAFDRVATKQKLSYSKTNEIVHMLSQEIDKALSILEETPSSDTMLLDHRSILADVKKVFMEIAPITQLEATEKELHAALTKYPKVLEKQLNPDISKAYRHNVEFDTHIVNQIIANFFYRQGMFDIGDCFVAETGESECSTRQSFVEMYRILEAMKRRDLEPALNWAVSNSDKLKEARSDLEMKLHSLHFLEIARGKNSKEAIDYARKHIATFADSCLPEIQKLMCSLLWNRKLDKSPYSEFLSPALWNNAVKELTRQYCNLLGESSESPLSITVTAGTQALPVLLKYMNVVMANKKLDWQTMEQLPVDAQLSEEFQFHSVFVCPVSKEQSSDDNPPMMMSCGHVLCKQTINKMSKNGSKSSFKCPYCPTDVDISRCRQLHF
Protein: Factor arrest protein 8 (Q05040)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Participates in the control of the reentry into the cell cycle following pheromone treatment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Factor arrest protein 11
- Factor arrest protein 7
- Vacuolar protein sorting-associated protein 64
- Factor arrest protein 10
- Factor arrest protein 3
- Protein phosphatase PP2A regulatory subunit A
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
Sequence:
MAINQAHVHPHYTLPGVMHYLQTEFTKNERDRITWELERSEMKARIAELEGENRDLKHQLNQIQSKAVSPEGEKEEKHVPDSLLQSKLAVQENVKEIIYLLKGPNTVNQLESLNSREAGSELHDLEKLNVNTPKEEGSAKTNGMDILNNALLDTKPNPKQGPSESPSPTKVKSLFSTANKRENNETISKIHSELSKVDIISSYGDCMALYDADTKSLEIHQVDANLNSKLLKKISLGQDSDIMKFFWVSTSKLLVIEKSFHLKLFSISSASLISDVDLLQDSEQPFSSSDIINIDFKNKWLLIASKNKSQIRIWELDNIEAPEDVPINIKETYEITHDNDDDDSNDSTNILDCILGITEKSLILLSSNPYQLTIYDFEGKLLQKIDLKIDTILSGKPEEEGYHLFLDRKTSKLLIQLSNERLLVYSFDKKKVVLKEQLTPSSTLPIQLDLNDSIITVSYSNGDFEFRNLENLKPSIDEFVVADINFSERKEPVVFSSNLIVDSTPVLITVNKNNEVLLHKIKI
Protein: Transient receptor potential cation channel subfamily V member 2 (Transient receptor potential cation channel, subfamily V, member 2) (Q5EA32)
Organism: Bos taurus (Bovine)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Transient receptor potential cation channel subfamily M member 2.
- Insulin-like growth factor 1
- Transient receptor potential cation channel subfamily A member 1
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 4
- Transient receptor potential cation channel subfamily C member 3
- Short transient receptor potential channel 1
- Transient receptor potential cation channel subfamily M member 3
- Transient receptor potential cation channel subfamily M member 3
Sequence:
MTTPSSSPAFRLETSDGGDEDGAQGDTGNGGRSSEPPPMESRFQSEDRNSSPQIRVNLNFRRAAGASQPDPNRFGRDRLFSAVARGAPEDLAGLPEYLRRTSKYLTDSEYREGSTGKTCLMKALLNLRDGANACIEPLLQIDRDSGNPHPLVNAQCMDEYYRGHSALHIAIEKRSLVCVKLLVENGADVHARACGQFFQKRREETCFYFGELPLSLAACTQQWDVVTYLLKNTHQPASLQATDSLGNTVLHALVMIADNSPENSMLVTHMYDRLLQVGGLQLEDMTNLQGLTPLKLAAKEGKIEIFRHILQRELPEPYQSLSRKFTEWSYGPVRVSLYDLASVDSWEENSVLEIIAFHSRSPLRHRMVVLEPLNKLLKAKSNLLIPRFLFNFLCYLTYMLIFTAVTYYQPALEKDFLPLEVTAGNTMLLLGHVLLLLGGVNLLMGQLWYFWRRRLFIWISFMDSYFEILFLVQALLTVLSQVLRFLAVKGYLPLLVCSLVLGWLNLLYYMRGFQYTGIYSVMIQKVILRDLLRFLGVYLVFLFGFAVALVSLSREPQDTGAPAGSNTTEVAGKEDKEAPYRGILDTSLELFKFTIGMGELAFQDQLHFRGVVLLLLLAYVLLTYVLLLNMLIALMSETVNSVATDSWSIWKLQKAISVLEMEKGYWWCRRKQQRAGVKLTVGSRPDGSPDERWCFRVEEVNWAAWEQTLPTVFEEPSGRGGPGAITSPALASQSSQDSAVEEDHVPLQPLESH
Protein: ATP-dependent helicase DinG (EC 5.6.2.3) (DNA 5'-3' helicase DinG) (P9WMR5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Probable helicase involved in DNA repair and perhaps also replication.
Interaction partners:
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA polymerase I
- CysO-cysteine peptidase
- DNA 3'-5' helicase XPB
- Probable helicase HelZ
- Calcineurin-like phosphoesterase domain-containing protein
- Helicase ATP-binding domain-containing protein
- Uncharacterized protein
Sequence:
MSESVSMSVPELLAIAVAALGGTRRRGQQEMAAAVAHAFETGEHLVVQAGTGTGKSLAYLVPAIIRALCDDAPVVVSTATIALQRQLVDRDLPQLVDSLTNALPRRPKFALLKGRRNYLCLNKIHNSVTASDHDDERPQEELFDPVAVTALGRDVQRLTAWASTTVSGDRDDLKPGVGDRSWSQVSVSARECLGVARCPFGSECFSERARGAAGLADVVVTNHALLAIDAVAESAVLPEHRLLVVDEAHELADRVTSVAAAELTSATLGMAARRITRLVDPKVTQRLQAASATFSSAIHDARPGRIDCLDDEMATYLSALRDAASAARSAIDTGSDTTTASVRAEAGAVLTEISDTASRILASFAPAIPDRSDVVWLEHEDNHESARAVLRVAPLSVAELLATQVFARATTVLTSATLTIGGSFDAMATAWGLTADTPWRGLDVGSPFQHAKSGILYVAAHLPPPGRDGSGSAEQLTEIAELITAAGGRTLGLFSSMRAARAATEAMRERLSTPVLCQGDDSTSTLVEKFTADAATSLFGTLSLWQGVDVPGPSLSLVLIDRIPFPRPDDPLLSARQRAVAARGGNGFMTVAASHAALLLAQGSGRLLRRVTDRGVVAVLDSRMATARYGEFLRASLPPFWQTTNATQVRAALRRLARADAKAH
Protein: Telomeric repeat-binding factor 1 (NIMA-interacting protein 2) (TTAGGG repeat-binding factor 1) (Telomeric protein Pin2/TRF1) (P54274)
Organism: Homo sapiens (Human)
Function: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways.
Subcellular location: Nucleus {ECO:0000269|PubMed:24692559}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11943150}. Chromosome, telomere {ECO:0000269|PubMed:24692559}. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitotic spindle (PubMed:11943150). Colocalizes with TRIOBP isoform 1 at the telomeres in interphase (PubMed:24692559). {ECO:0000269|PubMed:11943150, ECO:0000269|PubMed:24692559}.
Interaction partners:
- Adrenocortical dysplasia protein homolog
- Telomeric repeat-binding factor 2-interacting protein 1
- Poly [ADP-ribose] polymerase tankyrase-1
- Protection of telomeres protein 1
- TERF1-interacting nuclear factor 2
- Poly [ADP-ribose] polymerase tankyrase-2
- Telomeric repeat-binding factor 2
- F-box only protein 4
- Tripeptidyl-peptidase 1
- Telomere repeats-binding bouquet formation protein 1
Sequence:
MAEDVSSAAPSPRGCADGRDADPTEEQMAETERNDEEQFECQELLECQVQVGAPEEEEEEEEDAGLVAEAEAVAAGWMLDFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIQAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYNHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKNLFLSKLQHGTQQQDLNKKERRVGTPQSTKKKKESRRATESRIPVSKSQPVTPEKHRARKRQAWLWEEDKNLRSGVRKYGEGNWSKILLHYKFNNRTSVMLKDRWRTMKKLKLISSDSED
Protein: Zinc-finger homeodomain protein 14 (AtZHD14) (Homeobox protein 32) (AtHB-32) (Q9LQW3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative transcription factor.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cation/H
- Homeobox-DDT domain protein RLT3
- Peptide methionine sulfoxide reductase A2
Sequence:
MQSTCVYRECMRNHAAKLGSYAIDGCREYSQPSTGDLCVACGCHRSYHRRIDVISSPQINHTRFPFTSLRRVKQLARLKWKTAEERNEEEEDDTEETSTEEKMTVQRRRKSKFTAEQREAMKDYAAKLGWTLKDKRALREEIRVFCEGIGVTRYHFKTWVNNNKKFYH
Protein: Polynucleotidyl transferase, ribonuclease H-like superfamily protein (F4JEB4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 2
- Mitotic spindle checkpoint protein MAD2
- Anaphase-promoting complex subunit 10
- Ubiquitin-conjugating enzyme E2 22
- Anaphase-promoting complex subunit 7
Sequence:
MGSTMEDEKDAFYIVRKGDIIGVYRSLSECQGQAGSSVSHPAMSVYKGYGWPKGAEDLLSSFGIKNALFSVNASHVKDDAFGKLIPCPVQQPSSSQGESLNKSSPSKRLQDMGSGESGSFSPSPPQKQLKIENDMLRRIPSSLLTRTPIRQNDSCTIEFDGASKGNPGKAGAGAVLRASDNSVLFYLREGVGNATNNVAEYRALLLGLRSALDKGFKNVHVLGDSMLVCMQVQGAWKTNHPKMAELCKQAKELMNSFKTFDIKHIAREKNSEADKQANSAIFLADGQTQVISGG
Protein: Fic family protein (Q83EF1)
Organism: Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Interaction partners:
- Hypothetical membrane spanning protein
- Hypothetical membrane spanning protein
Sequence:
MRKNRNIRGSRNTPHWYNSKTNQGLLIITSVAILAYLFQNLFNVNSISSDNKTGVAEPSPSALRENSEEEPLMLQILLQLPLQLGLVALCNALKQEKVRRRIITEPKVGLIGNFQKEHPHLGRIVESPLTKAESKRQWKSIYYVITAFPKRVEVCQSMVARWNKIEELVEGLRSSIKITTSDQLKSLSKEENKFIEKLASVSNTINGISLHAGLVSKKESEHASINFKKAYALIQDWVKNKEPLSKIDIRTLKKLHALLTRGHGSSAFRDKSRISLGRDGYFTQPSNLDSVANDIINFLKSDSPAIYKAITAQELLLSAHLFRDGNHRLASLIRIWVLETHGIPANVISTEEAERLMLLVKPLRMPGAIPPEEAKQLDFNSKDAETLAGRWFRYAPRFLNNIGLFSRIELNLERLYIKRKKEILEMMTSRIEERLETLCKILHCEQNLENRFSY
Protein: AT3g27560/MMJ24_11 (Nearly identical to protein kinase ATN1) (Protein kinase superfamily protein) (Q9LT56)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 21
- Protein kinase family protein
Sequence:
MGSASGFYSNEEFELDPKWLVDPRHLFVGPKIGEGAHAKVYEGKYRNQTVAIKIIKRGESPEEIAKRDNRFAREIAMLSKVQHKNLVKFIGACKEPMMVIVTELLLGGTLRKYLVSLRPKRLDIRLAVGFALDIARAMECLHSHGIIHRDLKPENLILSADHKTVKLADFGLAREESLTEMMTAETGTYRWMAPELYSTVTLRQGEKKHYNHKVDAYSFAIVLWELILNKLPFEGMSNLQAAYAAAFKNLRPSAEDLPGDLEMIVTSCWKEDPNERPNFTEIIQMLLRYLTTVSAPQIIPPPNRRVFSSENIVLSPESPGTCSLMSVRDGDVSRQTVNTADSSEKQTKGSFFSCCS
Protein: Protein disulfide-isomerase tigA (EC 5.3.4.1) (Q00216)
Organism: Aspergillus niger
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
Sequence:
MVRLSNLVSCLGLASAVTAAVVDLVPKNFDDVVLKSGKPALVEFFAPWCGHCKNLAPVYEELGQAFAHASDKVTVGKVDADEHRDLGRKFGVQGFPTLKWFDGKSDEPEDYKGGRDLESLSSFISEKTGVKPRGPKKEPSKVEMLNDATFKGAVGGDNDVLVAFTAPWCGHCKNLAPTWEALANDFVLEPNVVIAKVDADAENGKATAREQGVSGYPTIKFFPKGSTESVPYEGARSEQAFIDFLNEKTGTHRTVGGGLDTKAGTIASLDELIASTSAADLAAAVKKAATELKDKYAQYYVKVADKLSQNAEYAAKELARLEKILAKGGSAPEKVDDLISRSNILRKFVGEEKEAKDEL
Protein: La-related protein 1C (AtLARP1c) (Q94K80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes leaf senescence mediated by abscisic acid (ABA), salicylic acid (SA) and jasmonic acid (MeJA), probably though the induction of expression of senescence-associated genes (SAGs) and defense-related genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22965746}. Note=Present in cytoplasmic foci.
Interaction partners:
- Chromatin modification-related protein EAF1 A
- Eukaryotic translation initiation factor isoform 4G-1
- Calcium-binding EF hand family protein
- Protein HLB1
- AT1G11360 protein
- Ubinuclein-1
- Protein phosphatase inhibitor 2
- Calcium-binding EF hand family protein
- G-box-binding factor 2
- UBP1-associated protein 2B
Sequence:
MASATSNNPASSSMSPRRISGNHGSPTASVAQSPRRPSRQVSSPWTQIVRGESEPIAAAAAVAGPSSPQSRAPIEPIASVSVAAPTAAVLTVEAAAGDEKSEASGGQDNAGKKPVWKRPSNGASEVGPVMGASSWPALSETTKAPSNKSSSDSLKSLGDVPSSSSASSSVPVTQGIANASVPAPKQAGRANPNPTPNHSRQRSFKQRNGASGSANGTVSQPSAQGSFTELPSHNPSPRGQNQKNGFASQNHGGTENPSQRDSYRNQNGNHHQSHGGRRNQEHGNQNWTFQRSFNGREGNAQSQRGTPAFVRHPSPTVQPIPQFMAAQPFPSHIPFPTELAQSSYYPRMPYMTPIPHGPQFFYHYQDPPLHMKLHKQIQYYFSDENLITDIYLRGFMNNEGFVPLRVVAGFKKVAELTDNIQQIVEALQNSPHVEVQGDFIRKRDNWQNWVLRRNPTGSGPQSVDRADAVAKRLGNLSVDQSSADPIGGSSSQLQPTEALSDDQQQSSSTAPVSNHNAPDGANR
Protein: MKI67 FHA domain-interacting nucleolar phosphoprotein (Nucleolar phosphoprotein Nopp34) (Nucleolar protein interacting with the FHA domain of pKI-67) (hNIFK) (Q9BYG3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus. Chromosome. Note=Localizes to mitotic chromosomes in conjunction with MKI67.
Interaction partners:
- Ribosome production factor 1
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein BRX1 homolog
- Ribosomal L1 domain-containing protein 1
- ATP-dependent RNA helicase DDX18
- Ribosome biogenesis regulatory protein homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- Probable rRNA-processing protein EBP2
- Nucleolar complex protein 2 homolog
- Ribosome biogenesis protein WDR12
Sequence:
MATFSGPAGPILSLNPQEDVEFQKEVAQVRKRITQRKKQEQLTPGVVYVRHLPNLLDETQIFSYFSQFGTVTRFRLSRSKRTGNSKGYAFVEFESEDVAKIVAETMNNYLFGERLLECHFMPPEKVHKELFKDWNIPFKQPSYPSVKRYNRNRTLTQKLRMEERFKKKERLLRKKLAKKGIDYDFPSLILQKTESISKTNRQTSTKGQVLRKKKKKVSGTLDTPEKTVDSQGPTPVCTPTFLERRKSQVAELNDDDKDDEIVFKQPISCVKEEIQETQTPTHSRKKRRRSSNQ
Protein: Small ribosomal subunit protein eS6 (40S ribosomal protein S6) (Phosphoprotein NP33) (P62754)
Organism: Mus musculus (Mouse)
Function: Component of the 40S small ribosomal subunit (By similarity). Plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62753}.
Interaction partners:
- Small ribosomal subunit protein eS4
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS24
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL20
Sequence:
MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK
Protein: AP2-associated protein kinase 1 (EC 2.7.11.1) (Adaptor-associated kinase 1) (Q2M2I8)
Organism: Homo sapiens (Human)
Function: Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis. Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1. Preferentially, may phosphorylate substrates on threonine residues. Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes. Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes. Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:F1MH24}; Peripheral membrane protein {ECO:0000250|UniProtKB:F1MH24}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11877461}. Presynapse {ECO:0000250|UniProtKB:P0C1X8}. Note=Active when found in clathrin-coated pits at the plasma membrane. In neuronal cells, enriched at presynaptic terminals. In non-neuronal cells, enriched at leading edge of migrating cells. {ECO:0000250|UniProtKB:P0C1X8}.
Interaction partners:
- AP-2 complex subunit mu
- RalBP1-associated Eps domain-containing protein 1
- Epidermal growth factor receptor substrate 15
- AP-2 complex subunit beta
- AP-2 complex subunit sigma
- SH3-containing GRB2-like protein 3-interacting protein 1
- RalA-binding protein 1
- Adaptin ear-binding coat-associated protein 2
- Clathrin coat assembly protein AP180
- Clathrin light chain B
Sequence:
MKKFFDSRREQGGSGLGSGSSGGGGSTSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFAIVFLVRTSNGMKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQTEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGNFTIPDNSRYSQDMHCLIRYMLEPDPDKRPDIYQVSYFSFKLLKKECPIPNVQNSPIPAKLPEPVKASEAAAKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPPPQAAGSSNQPGLLASVPQPKPQAPPSQPLPQTQAKQPQAPPTPQQTPSTQAQGLPAQAQATPQHQQQLFLKQQQQQQQPPPAQQQPAGTFYQQQQAQTQQFQAVHPATQKPAIAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQQQLATALHQQQLMTQQAALQQKPTMAAGQQPQPQPAAAPQPAPAQEPAIQAPVRQQPKVQTTPPPAVQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLQAAAAEASLNKSKSATTTPSGSPRTSQQNVYNPSEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKHPEKLGGSAESLIPGFQSTQGDAFATTSFSAGTAEKRKGGQTVDSGLPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGEDSLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGFDVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL