wanglab/gogpt-training-data huggingface dataset:
Protein: Global transcriptional regulator CodY (B5XI03)
Organism: Streptococcus pyogenes serotype M49 (strain NZ131)
Function: DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00621}.
Interaction partners:
Sequence:
MPNLLEKTRKITSILQRSVDSLETELPYNTMASRLADIIDCNACIINGGGTLLGYAMKYKTNTDRVEEFFEAKQFPDTYVKAASRVYDTEANLSVENELTIFPVESKDTYPGGLTTIAPIYGGGMRLGSLIIWRNDNEFSDDDLILVEISSTVVGIQLLNLQTENLEDTIRKQTAVNMAINTLSYSEMKAVAAILGELDGNEGRLTASVIADRIGITRSVIVNALRKLESAGIIESRSLGMKGTYLKVINEGIFAKLKEF
Protein: Dihydroxy-acid dehydratase (DAD) (EC 4.2.1.9) (P05791)
Organism: Escherichia coli (strain K12)
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
Interaction partners:
- Branched-chain-amino-acid aminotransferase
- L-threonine dehydratase biosynthetic IlvA
- Ketol-acid reductoisomerase
- 2-isopropylmalate synthase
- Acetolactate synthase isozyme 2 small subunit
- Acetolactate synthase isozyme 1 large subunit
- 3-isopropylmalate dehydrogenase
- 3-isopropylmalate dehydratase small subunit
- 3-isopropylmalate dehydratase large subunit
- Valine--pyruvate aminotransferase
Sequence:
MPKYRSATTTHGRNMAGARALWRATGMTDADFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDSQSDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIVELTKRYYEQNDESALPRNIASKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTQKYHMEDVHRAGGVIGILGELDRAGLLNRDVKNVLGLTLPQTLEQYDVMLTQDDAVKNMFRAGPAGIRTTQAFSQDCRWDTLDDDRANGCIRSLEHAYSKDGGLAVLYGNFAENGCIVKTAGVDDSILKFTGPAKVYESQDDAVEAILGGKVVAGDVVVIRYEGPKGGPGMQEMLYPTSFLKSMGLGKACALITDGRFSGGTSGLSIGHVSPEAASGGSIGLIEDGDLIAIDIPNRGIQLQVSDAELAARREAQDARGDKAWTPKNRERQVSFALRAYASLATSADKGAVRDKSKLGG
Protein: Eukaryotic translation initiation factor 2 subunit 3, X-linked (EC 3.6.5.3) (Eukaryotic translation initiation factor 2 subunit gamma, X-linked) (eIF2-gamma X) (Q9Z0N1)
Organism: Mus musculus (Mouse)
Function: As a subunit of eukaryotic initiation factor 2 (eIF-2), involved in the early steps of protein synthesis. In the presence of GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a step that determines the rate of protein translation. The 43S PIC binds to mRNA and scans downstream to the initiation codon, where it forms a 48S initiation complex by codon-anticodon base pairing. This leads to the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of Pi, which makes GTP hydrolysis irreversible, causes the release of the eIF-2-GDP binary complex from the 40S subunit, an event that is essential for the subsequent joining of the 60S ribosomal subunit to form an elongation-competent 80S ribosome. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP exchange factor (GEF) eIF-2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09130}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- Ubiquitin-like protein FUBI
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit C
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Translation initiation factor eIF2B subunit epsilon
Sequence:
MAGGEGGVTLGQPHLSRQDLATLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD
Protein: Queuine tRNA-ribosyltransferase catalytic subunit 1 (EC 2.4.2.64) (Guanine insertion enzyme) (tRNA-guanine transglycosylase) (Q9BXR0)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03218}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03218}. Note=Weakly associates with mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218}.
Interaction partners:
- Queuine tRNA-ribosyltransferase accessory subunit 2
- Ubiquitin carboxyl-terminal hydrolase 14
- Thymidylate synthase
- Amyloid beta precursor protein binding family B member 1
- Ubiquitin carboxyl-terminal hydrolase 8
- Ubiquitin carboxyl-terminal hydrolase 6
Sequence:
MAGAATQASLESAPRIMRLVAECSRSRARAGELWLPHGTVATPVFMPVGTQATMKGITTEQLDALGCRICLGNTYHLGLRPGPELIQKANGLHGFMNWPHNLLTDSGGFQMVSLVSLSEVTEEGVRFRSPYDGNETLLSPEKSVQIQNALGSDIIMQLDDVVSSTVTGPRVEEAMYRSIRWLDRCIAAHQRPDKQNLFAIIQGGLDADLRATCLEEMTKRDVPGFAIGGLSGGESKSQFWRMVALSTSRLPKDKPRYLMGVGYATDLVVCVALGCDMFDCVFPTRTARFGSALVPTGNLQLRKKVFEKDFGPIDPECTCPTCQKHSRAFLHALLHSDNTAALHHLTVHNIAYQLQLMSAVRTSIVEKRFPDFVRDFMGAMYGDPTLCPTWATDALASVGITLG
Protein: Cytochrome P450 1A (EC 1.14.14.1) (Q8UW07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}. Microsome membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}.
Interaction partners:
- Aryl hydrocarbon receptor 1a.
- Aryl hydrocarbon receptor 2.
- Epoxide hydrolase
- UDP-glucuronosyltransferase
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Aromatase
- Transmembrane O-methyltransferase homolog
- Aryl hydrocarbon receptor nuclear translocator.
- Sulfotransferase
- Hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 2
Sequence:
MALTILPILGPISVSESLVAIITICLVYLLMRLNRTKIPDGLQKLPGPKPLPIIGNVLEIGNNPHLSLTAMSKCYGPVFQIQIGMRPVVVLSGNDVIRQALLKQGEEFSGRPELYSTKFISDGKSLAFSTDQVGVWRARRKLALNALRTFSTVQGKSPKYSCALEEHISNEGLYLVQRLHSVMKADGSFDPFRHIVVSVANVICGICFGRRHSHDDDELVRLVNMSDEFGKIVGSGNPADFIPFLRILPSTTMKKFLDINERFSKFMKRLVMEHYDTFDKDNIRDITDSLINHCEDRKLDENSNLQVSDEKIVGIVNDLFGAGFDTISTALSWAVVYLVHYPEVQERLQRELDEKIGKDRTPLLSDRANLPLLESFILEIFRHSSFLPFTIPHCTSKDTSLNGYFIPKDTCVFVNQWQVNHDPELWKDPSSFIPDRFLTADGTELNKLEGEKVLVFGLGKRRCIGESIGRAEVFLFLAILLQRLKFTGMPGEMLDMTPEYGLTMKHKRCLLRVTPQPGF
Protein: Protein SSP120 (P39931)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein EMP47
- Endoplasmic reticulum transmembrane protein 3
- Peptidyl-prolyl cis-trans isomerase FPR2
Sequence:
MRFLRGFVFSLAFTLYKVTATAEIGSEINVENEAPPDGLSWEEWHMDHEHQLKDYTPETFFALHDIKKKGFLDENDILSLYGLNREEIVGAGDGMGQHDESEKIDNEMAKRVVSLIMRLLDVDDNTKITKEEYLQFAKRGNKFPDLGVGVGHHSDFELEYEIHHWNKFHKDKDPDVKVVHKEDIEHELLHHEHEIEHEEEIQRGASRATVITDDELESRIELKNIPEKFKNGIF
Protein: Lysozyme 3 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase 3) (Invertebrate-type lysozyme 3) (cv-lysozyme 3) (B3A003)
Organism: Crassostrea virginica (Eastern oyster)
Function: Has antibacterial activity against the Gram-negative bacterium E.coli. No antibacterial activity detected against the Gram-negative bacterium V.vulnificus.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P83673}.
Interaction partners:
Sequence:
MNGLFLFCVATTAALAYGSDAPCTNSGGVCQDDHLACHNGHYQSGLCTGGAHRRCCLTSASHTGSFSTGIVSQQCLQCICNVESGCKAIGCHFDVNSDSCGYFQIKEGYWHDCGSPGSSWRSCANDLACASKCVQAYMSRYIGFSGCSHSCESYARIHNGGPAGCKHTNTLGYWSHVHAQGCSHNSK
Protein: E3 ubiquitin-protein ligase TRIM68 (EC 2.3.2.27) (RING finger protein 137) (RING-type E3 ubiquitin transferase TRIM68) (SSA protein SS-56) (SS-56) (Tripartite motif-containing protein 68) (Q6AZZ1)
Organism: Homo sapiens (Human)
Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity.
Subcellular location: Cytoplasm, perinuclear region. Nucleus. Note=Colocalized with AR in nucleus.
Interaction partners:
Sequence:
MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVEKVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAWKLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQVLWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSEDRKRVHYGDTNQKLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCKQNVDRKEVVYLSPHYGFWVIRLRKGNEYRAGTDEYPILSLPVPPRRVGIFVDYEAHDISFYNVTDCGSHIFTFPRYPFPGRLLPYFSPCYSIGTNNTAPLAICSLDGED
Protein: Glucose dehydrogenase (Q9F5L5)
Organism: Bacillus subtilis
Interaction partners:
Sequence:
MYPDLKGKVVVITGSSTGLGKAMAIRFATAKAKVVVNYRSKEDEANSVLEEIKKVGGEAIAVKGDVTVESDVINLVQSAIKEFGKLDVMINNAGLENPVSSHEMSLSDWIKVIDTNLTGAFLGSREAIKYFVENDIKGTVINMSSVHEKIPWPLFVHYAASKGGMKLMTETLALEYAPKGIRVNNIGPGAINTPINAEKFADPEQSADVESMIPMGYIGEPEETAAVAAWLASSEASYVTGITLFADGGMTQYPSFQAGRG
Protein: Sulfhydryl oxidase (EC 1.8.3.2) (Q9ICB8)
Organism: African swine fever virus (ASFV)
Interaction partners:
Sequence:
MLHWGPKYWRALHLYAIFFSDAPGWKEKYEAIQWILNFIESLPCTRCRHHAFSYLTKNPLTLNNSEDFQYWTFAFHNNVNNRLNKKIISWSEYKNIYEQSILKTIEYGKTDFIGAWSSL
Protein: Uncharacterized protein (Q385U4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAGLQSALAYRLALVDQERQQQQRGYDFLRRSLLHKVVAACAQGGSAAKLDRHGGRVSSSDELVIRDERGIASIGDSDVVSNAGDDMTGVSVSSQWPSPDEETEEPPSRKLLGFQSTPMESVGAKGKKREEGTFGAGVLETTGGRLQGLDDSDVVPSFRPTISLVSARLARQRRLKDRAEGLPISEYLFQRGKATNRVGKQEQGETVRAHADPTVATRVRKVTFTASTVERLYSNPKGKQGNDTQHRKQQLQDISPTDIDLRFHPLISERAAKLQRGTSRKVHDDLYEHGVRRQLQKNCAQPRNEPSFHPTINQVSEMIVRGLSNPAVAGLT
Protein: Probable E3 ubiquitin-protein ligase HERC4 (EC 2.3.2.26) (HECT domain and RCC1-like domain-containing protein 4) (HECT-type E3 ubiquitin transferase HERC4) (Q6PAV2)
Organism: Mus musculus (Mouse)
Function: Probable E3 ubiquitin-protein ligase involved in either protein trafficking or in the distribution of cellular structures. Required for spermatozoon maturation and fertility, and for the removal of the cytoplasmic droplet of the spermatozoon. E3 ubiquitin-protein ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer it to targeted substrates.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5GLZ8}.
Interaction partners:
Sequence:
MLCWGNASYGQLGLGGIDEEIVLEPRRSDFFVNKKVRDVGCGLRHTVFVLDDGTVYTCGCNDLGQLGHEKSRKKPEQVVALDAQNIVAVACGEAHTLALNDKGQVYAWGLDSDGQLGLQGSEECIRVPRNIKSLSDIQIVQVACGYYHSLALSKASEVFCWGQNKYGQLGLGIDCQKQTSPQLIKSLLGIPFMQVAAGGAHSFVLTLSGAIFGWGRNKFGQLGLNDENDRYVPNLLKSLRSQKIVYICCGEDHTAALTKEGGVFTFGAGGYGQLGHNSTSHEINPRKVFELMGSIVTQVACGRQHTSAFVPSSGRIYSFGLGGNGQLGTGSTSNRKSPFTVKGNWFSYNGQCPQDIGSEDYFCVKRIFSGGDQSFSHYSSPQNCGPPDDFRCSDPSKQIWTVNEALIQKWLSYPSGRFPVEIANEIDGTFSSSGCLNGSFLAISNDDHYRTGTRFSGVDMNAARLLFHKLIQPDHPQISQQVAASLEKNLIPKLTSSLPDVEALRFYLTLPECPLMSDCNNFTTIAIPFGTALVNLEKAPLKVLENWWSVLEPPLFLKIVELFKEVVVHLLKLYKIGIPPSERRIFNSFLHTALKVLEILHRVNEKTGQLIQYDKFYIHEVQELIDIRNDYINWVQQQAYGVDVSHGVTELADIPVTICTYPFVFDAQAKTTLLQTDAVLQMQMAIDQAHRQNVSSLFLPVIESVNPCLILVVRRENIVGDAMEVLRKTKNIDYKKPLKVIFVGEDAVDAGGVRKEFFLLIMRELLDPKYGMFRYYEDSRLIWFSDKTFEDSDLFHLIGVICGLAIYNFTIVDLHFPLALYKKLLKRKPSLDDLKELMPAVGRSMQQLLDYPEDDIEETFCLNFTITVENFGATEVKELVLNGADTAVNRQNRQEFVDAYVDYIFNKSVASLFDAFHAGFHKVCGGKVLLLFQPNELQAMVIGNTNYDWKELEKNTEYKGEYWADHPTIKIFWEVFHELPLEKKKQFLLFLTGSDRIPILGMKSLKLVIQSTGGGESYLPVSHTCFNLLDLPKYTEKETLRCKLIQAIDHNEGFSLI
Protein: Uncharacterized protein (E9M5R0)
Organism: Cricetid gammaherpesvirus 2
Interaction partners:
Sequence:
MANRSGMGGCMMLSLLIAGMSLMLGHCGPVGEPVASEINEASKVSSRLLTQDILFRKDRQATISLPIKLPVEDIITQTCDKITYGPLKFLDLLEKETAVLPLSTDITCPACLGRAVLVGKWECPAHVAVNESDLTVFGPNKEEHVPQFVTVQQPSDGKMQRLFFAKFLGTEESLAVLRVPGPDGHLCIQEALIHFKELSGAGVCSLWKANDSREEGLEMKQVDCLETTVLENQTCIATTLSKKIYHRLYCGERLMTGGQVSTRVLLTALGFYKRQPYTFHRVPKGMVYVHLIDSGSEDYMEYSECEEVTPGRYEDKQISYTFYTDLFQTADGEPVLASVWGTSGLKDSAYESCAFVIPTKGRRKLVPRRIMSKCYPFRLTYHPSTMTVRLDVRVEKHHGATDQGFVFLKMESGTYSEGREYYLDRVLWGEDSSTNNVLQ
Protein: EOR-1 (Zinc finger protein) (G5EDU4)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- EOR-2
- Protein lin-25
- ETS domain-containing protein
Sequence:
MTLVASSENTGLCPMTFDDSSGQTSHMLFQRLQYQRKTGRFCDVEIVVQNKSFAAHRNILAAHSPYFDAIFKYCKITKEQLTINSKSPQVFELFLNYMYSGTVIIDRSSVSELLRFANNFLIVKLKVYCAAYLDRYLDAANCLSIRTLAQRYNLPGLVKSATDYFDSNLNRCLLESRDIIGYTYTQLTRLIGDPKYVDCITSDTYLKLIVRWVGEEVSKREEIFRLLLESCEFREVSADTLEFLLDYSPLLSKSQKSRFLLLHVMETNNMLMEKYSTQLSSLRQKIVDLPILHDPSQFEDDIYDSSDSEEDPDDYIADGHPTSAQVVEYGNDVNNRLKMKIAFQPGNEKKRLKRPKGMKKHHLHPIPPINATENESIPWIDEDEIDGVYATCSLEGCHTYGPVDNLDPDDCEDEEDQPDENGPSTCIFCGLRTANEELLEKHKARHHNRNTYYMCHLCEFETNWSKQFYLHCAEHWTEIPYRCETCPFTSNEIQEFLTHRLQHTDERFFKCGECAWKGRTRSQLFAHERMHSVLDDRSLHCEECGRGFQQHSTLDHHVASHNDPRPYICEDCGFATKTADHLSLHRRQHTGDNFSCHIAGCDYSSTKKSQLAAHLRTHMAVRAHLCKICGRGFIEKSHLVRHERIHLEEKPFKCDQCEYASSRRDKLKEHIIKHHNSEVLTFQKTQRRKYKRQRMLAAASNIVNNPDALFRPITSDDAVSNWQATNDFSTYSPNPNDYGGPSTYGNPSSPQRAFSVVHPSQHQHHAQSPGCMSMMNVPLRDNHHQMQRQDSPGDSVGGGQGGGGGGGPEGSDNTHGVLMTPNLVMRSPHNRSAVQPQFNNLSTNSDPQQQQQQQQLRPFSLPTYGQMDLAQAAQLQQLQQQLQAAGLPPTGTPNNQDNSNNAWNPWNVQ
Protein: Zinc finger protein 324A (Zinc finger protein ZF5128) (O75467)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation. May be involved in regulation of cell proliferation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MAFEDVAVYFSQEEWGLLDTAQRALYRRVMLDNFALVASLGLSTSRPRVVIQLERGEEPWVPSGTDTTLSRTTYRRRNPGSWSLTEDRDVSGEWPRAFPDTPPGMTTSVFPVAGACHSVKSLQRQRGASPSRERKPTGVSVIYWERLLLGSGSGQASVSLRLTSPLRPPEGVRLREKTLTEHALLGRQPRTPERQKPCAQEVPGRTFGSAQDLEAAGGRGHHRMGAVWQEPHRLLGGQEPSTWDELGEALHAGEKSFECRACSKVFVKSSDLLKHLRTHTGERPYECAQCGKAFSQTSHLTQHQRIHSGETPYACPVCGKAFRHSSSLVRHQRIHTAEKSFRCSECGKAFSHGSNLSQHRKIHAGGRPYACAQCGRRFCRNSHLIQHERTHTGEKPFVCALCGAAFSQGSSLFKHQRVHTGEKPFACPQCGRAFSHSSNLTQHQLLHTGERPFRCVDCGKAFAKGAVLLSHRRIHTGEKPFVCTQCGRAFRERPALFHHQRIHTGEKTVRRSRASLHPQARSVAGASSEGAPAKETEPTPASGPAAVSQPAEV
Protein: Ras-related protein RabC (P34143)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MEEEILYKIILVGESGVGKSSILVRFTDNTFSQHFAPTLGVDFNVKTIRNKETGQTVKLQLWDTAGQERFKSITQTFYRGSHGVIVVYDVTDPKSFERCKNWVEDINQYTQDGMIIILVGNKSDMVAQRKVTFEQGQEMAEQLKTKFLEVSAKENNGVTQVFDLLVQDIEATMKNSKVAQNQLNLNSEVGQKRGCC
Protein: Hook microtubule-tethering protein 1 (A0A8I6AX65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MDVREQLAGIGSPHLPMCVLEIEHRLQTFKTASPCQDVKQLTNGVTMAQVLHQIDVAWFSESWLSRIKDDVGDNWRIKASNLKKVLHGITSYYHEFLGQQISEELIPDLNQITESSDPVELGRLLQLILGCAVNCEKKQEHIKNIMTLEESVQHVVMTAIQELMSKEIVSSPASDAVGELEQQLKRALEELQEALAEKEELKQRCQELDMQVTALQDEKNSLVSENEMMNEKLDQLDGSFDDPNTMVAKKYFHVQLQLEQLQEENYRLEAAKDDYRVHCEELEKQLIEFQHRNDELTSLAEETRALKDEIDVLRATSDKANKLESTVEVYRQKLQDLNDLRKQVKSLQETNMMYMHNTVSLEEELKKANAARAQLETYKRQVQDLHTKLSSESKRADTLAFEMKRLEEKHETLLKEKERLIEQRDTLKETNEELRCSKAQQDHLNQADSSATKSYENLAAEIMPVEYREVFIRLQHENKMLRLQQEGTENERIEQLQEQLEQKHRKMNELETEQRLSKERIGELQQQIEDLQKSLQEQGSKSEGESSSKLKQKLEAHMEKLTEVHEELQKKQELIEDLQPDISQNAQKISELEAALQKKDEDMKAMEERYKMYLEKARNVIKTLDPKLNPASAEIMLLRKQLAEKDRRIEILESECKVAKFRDYEEKLIVSAWYNKSLAFQKLGMESRLVSGASACKDSVAAAPARSFLAQQRHITSTRRNLSVKVPAAASD
Protein: Serine/threonine/tyrosine-protein kinase HT1 (EC 2.7.10.1) (EC 2.7.11.1) (High leaf temperature protein 1) (Q2MHE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine/tyrosine kinase involved in the control of stomatal movement in response to CO(2). Functions as a major negative regulator of CO(2)-induced stomatal closing. Does not seem to be involved in stomatal closure in response to abscisic acid (ABA) or light. Involved in the control of red light-induced stomatal opening. Is epistatic to SRK2E/OST1 function during stomatal responses to red light and altered CO(2). Phosphorylates SRK2E/OST1 and GHR1 to prevents SRK2E/OST1- and GHR1-induced activation of SLAC1, thus preventing stomatal closure.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25599916}.
Interaction partners:
- Protein DETOXIFICATION 56
- Guard cell S-type anion channel SLAC1
- Protein unc-13 homolog
- Beta carbonic anhydrase 4
- Aluminum-activated malate transporter 12
- Beta carbonic anhydrase 1, chloroplastic
Sequence:
MSGLCFNPFRLRWSLRSKLPLEPSLPNLPCNPSSSKTNRYAEAETMEKKRFDSMESWSMILESENVETWEASKGEREEWTADLSQLFIGNKFASGAHSRIYRGIYKQRAVAVKMVRIPTHKEETRAKLEQQFKSEVALLSRLFHPNIVQFIAACKKPPVYCIITEYMSQGNLRMYLNKKEPYSLSIETVLRLALDISRGMEYLHSQGVIHRDLKSNNLLLNDEMRVKVADFGTSCLETQCREAKGNMGTYRWMAPEMIKEKPYTRKVDVYSFGIVLWELTTALLPFQGMTPVQAAFAVAEKNERPPLPASCQPALAHLIKRCWSENPSKRPDFSNIVAVLEKYDECVKEGLPLTSHASLTKTKKAILDHLKGCVTSISSPFSSSSVPVNA
Protein: 26S proteasome regulatory subunit S10B homolog B (26S proteasome AAA-ATPase subunit RPT4b) (26S proteasome subunit S10B homolog B) (Regulatory particle triple-A ATPase subunit 4b) (Q9MAK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome regulatory subunit 4 homolog B
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 12 homolog A
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit 6A homolog B
- 26S proteasome regulatory subunit RPN13
Sequence:
MSDGDDAARRRTAAVTDYRKKLLHHKELESRVRTARENLRAAKKEFNKTEDDLKSLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEKLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDQLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMEILKIHASGIAKHGEIDYEAIVKLGEGFNGADLRNICTEAGMFAIRAERDYVIHEDFMKAVRKLSEAKKLESSSHYNADFGKE
Protein: Phosphorylase b kinase regulatory subunit beta (Phosphorylase kinase subunit beta) (Q93100)
Organism: Homo sapiens (Human)
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Calmodulin-1
- Calmodulin-1
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
Sequence:
MAGAAGLTAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDHYYRIVKSTLLLYQSPTTGLFPTKTCGGDQKAKIQDSLYCAAGAWALALAYRRIDDDKGRTHELEHSAIKCMRGILYCYMRQADKVQQFKQDPRPTTCLHSVFNVHTGDELLSYEEYGHLQINAVSLYLLYLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCISYPAFALDDEVLFSQTLDKVVRKLKGKYGFKRFLRDGYRTSLEDPNRCYYKPAEIKLFDGIECEFPIFFLYMMIDGVFRGNPKQVQEYQDLLTPVLHHTTEGYPVVPKYYYVPADFVEYEKNNPGSQKRFPSNCGRDGKLFLWGQALYIIAKLLADELISPKDIDPVQRYVPLKDQRNVSMRFSNQGPLENDLVVHVALIAESQRLQVFLNTYGIQTQTPQQVEPIQIWPQQELVKAYLQLGINEKLGLSGRPDRPIGCLGTSKIYRILGKTVVCYPIIFDLSDFYMSQDVFLLIDDIKNALQFIKQYWKMHGRPLFLVLIREDNIRGSRFNPILDMLAALKKGIIGGVKVHVDRLQTLISGAVVEQLDFLRISDTEELPEFKSFEELEPPKHSKVKRQSSTPSAPELGQQPDVNISEWKDKPTHEILQKLNDCSCLASQAILLGILLKREGPNFITKEGTVSDHIERVYRRAGSQKLWLAVRYGAAFTQKFSSSIAPHITTFLVHGKQVTLGAFGHEEEVISNPLSPRVIQNIIYYKCNTHDEREAVIQQELVIHIGWIISNNPELFSGMLKIRIGWIIHAMEYELQIRGGDKPALDLYQLSPSEVKQLLLDILQPQQNGRCWLNRRQIDGSLNRTPTGFYDRVWQILERTPNGIIVAGKHLPQQPTLSDMTMYEMNFSLLVEDTLGNIDQPQYRQIVVELLMVVSIVLERNPELEFQDKVDLDRLVKEAFNEFQKDQSRLKEIEKQDDMTSFYNTPPLGKRGTCSYLTKAVMNLLLEGEVKPNNDDPCLIS
Protein: CENP-ana, isoform B (EC 5.6.1.3) (CENP-ana, isoform C) (X2J5P0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MENGKAVNLGEQFETHKAKSKQMEEELLSSISEKDSTIVSLQQSLEELSRDVLRNSKEDQMRSMCPELESSCERICNKCLELERLLPLASASGLDSVACQFDQLRSEIAATRMKLESMLSTFSHASCEVSQKTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEQCQQLQDENSKLQAEIGTLKERVEEIHSELLEVPNPDTHPEDMELQNQELKKRLSKLQWEFDEIQLNYECLSNELMSTIQECDALREEHKQRTTNSDLESMKSSGVGTECSDPENELDTDLLQQFTKLSKSIQQIELTDYSGGRRLFIYNHAEQDQSVPSLKLCLEPAKYLEGDGKQHDASDSVFLKGFLKCQRFQIVKINQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQKVNGGDVSIELNSSNGSPTPAAVPATKKPLDCNSAECVPKKSSSLETAERKNRRMTAYDENRKQFC