wanglab/gogpt-training-data huggingface dataset:
Protein: D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (Q95XG9)
Organism: Caenorhabditis elegans
Function: Catalyzes oxidative deamination of D-amino acids, in particular D-alanine, and could be responsible for the degradation of diet-derived D-alanine in the intestine. Acts on a variety of D-amino acids with greater preference towards those with basic and aromatic groups followed by those bearing neutral groups. Has no activity against acidic D-amino acids, L-amino acids or N-methyl-L-aspartic acid. May play a role in egg-laying events and early development.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:17140416}.
Interaction partners:
- Uncharacterized protein R102.4
- Putative sarcosine oxidase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Glycine cleavage system P protein
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase
- Aminotransferase class I/classII large domain-containing protein
- Bifunctional glyoxylate cycle protein
- FMN hydroxy acid dehydrogenase domain-containing protein
- Rab-GAP TBC domain-containing protein
Sequence:
MPKIAVLGAGINGIASALAIQERLPNCEVTIIAEKFSPNTTSDVAAGLIEPFLCDDDVDRIINWTSATISRIHEYQADGNPGAEEQSGYWLQSVKSEPKWLKLMKNVHILTDAEMKQVARRPEHKFGIFYTTWYLEPTPYIKWCTDKFLKNGGKFKKQKIENIDDVARSYDVTVNCTGLGSRALIGDKEVYPTRGQILKVSCPRVKHFFIDDKYYALLNDSTITLGGTFEAHQWDLTINSELSQKILKENIHNIPSLRTAQILSSHVDMRPSRGTVRLQAELGRSLVHNYGHGGSGITLHWGCALECAEIVENVLKMKKSKL
Protein: Regulator of G-protein signaling 7-binding protein (R7 family-binding protein) (Q5FVH8)
Organism: Rattus norvegicus (Rat)
Function: Regulator of G protein-coupled receptor (GPCR) signaling. Regulatory subunit of the R7-Gbeta5 complexes that acts by controlling the subcellular location of the R7-Gbeta5 complexes. When palmitoylated, it targets the R7-Gbeta5 complexes to the plasma membrane, leading to inhibit G protein alpha subunits. When it is unpalmitoylated, the R7-Gbeta5 complexes undergo a nuclear/cytoplasmic shuttling. May also act by controlling the proteolytic stability of R7 proteins, probably by protecting them from degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21343290}. Cytoplasm {ECO:0000250|UniProtKB:Q8BQP9}. Cell membrane {ECO:0000269|PubMed:21343290}; Lipid-anchor {ECO:0000250|UniProtKB:Q8BQP9}. Note=Shuttling between the plasma membrane, the cytoplasm and the nucleus is regulated by palmitoylation. {ECO:0000269|PubMed:21343290}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 7
- Regulator of G-protein signaling 6
- Regulator of G-protein signaling 9
- Regulator of G-protein signaling 4
- Regulator of G-protein signaling 17
- Regulator of G-protein signaling 8
- Glutathione hydrolase 5 proenzyme
Sequence:
MSSAPNGRKKRPSRSTRSSIFQISKPPLQSGDWERRGSGSESAHKTQRALDDCKMLVQEFNTQVALYRELVISIGDVSVSCPSLRAEMHKTRTKGCEMARQAHQKLAAISGPEDGEIHPEICRLYIQLQCCLEMYTTEMLKSICLLGSLQFHRKGKEASGGAKSLDSKIEENAETPALEDSLSSPLDSQQQSWQVATDIENTERDMREMKNLLSKLRETMPLPLKNQDDSSLLNLTPYPMVRRRKRRFFGLCCLVSS
Protein: LD23686p (Q8T068)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNAQKEREQERVLKQKAHNTQLNVELSTLNEKIKELSQRICDTRAGVTNVKTVIDGMRTQRDTSMSEMSQLKARIKEQNAKLLQLTQERAKWEAKSKASGAALGGENAQQEQLNAAFAHKQLIINQIKDKVENISKEIESKKEDINTNDVQMSELKAELSALITKCEDLYKEYDVQRTSVLELKYNRKNETSVSSAWDTGSSSAWEETGTTVTDPYAVASNDISALAAPAVDLGGPAPEGFVKYQAVYEFNARNAEEITFVPGDIILVPLEQNAEPGWLAGEINGHTGWFPESYVEKLEVGEVAPVAAVEAPVDAQVATVADTYNDNINTSSIPAASADLTAAGDVEYYIAAYPYESAEEGDLSFSAGEMVMVIKKEGEWWTGTIGSRTGMFPSNYVQKADVGTASTAAAEPVESLDQETTLNGNAAYTAAPVEAQEQVYQPLPVQEPSEQPISSPGVGAEEAHEDLDTEVSQINTQSKTQSSEPAEIYSRPMSRTSSMTPGMRAKRSEIAQVIAPYEATSTEQLSLTRGQLIMIRKKTDSGWWEGELQAKGRRRQIGWFPATYVKVLQGGRNSGRNTPVSGSRIEMTEQILDKVIALYPYKAQNDDELSFDKDDIISVLGRDEPEWWRGELNGLSGLFPSNYVGPFVTSGKPAKANGTTKK
Protein: Repressor of RNA polymerase III transcription maf1 (O14109)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase III subunit rpc1
- DNA-directed RNA polymerase III subunit RPC2
- AP-1 complex subunit sigma-1
- AP-2 complex subunit sigma
- DNA-directed RNA polymerase III subunit rpc5
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerase III subunit rpc3
- Probable DNA-directed RNA polymerase III subunit rpc6
- Exportin-T
- DNA-directed RNA polymerase I subunit rpa1
Sequence:
MKFLELADLDTVNNALSFDADDCRIRGKCELYTTKSTNSDKKLFKAIENRCQEDLFALSSSKSPEYAFSLTQQSPFGPLDQSSSRRTFMYIVATLNASYPDHDFSSLQPTDFYKEPSLSRVVDSVNSTLNNIGRGRLSVNGIWEIIDRHINLSDCSVYSYTPDSDSDPYGDDALIWGMSYFFFNKNMKRMLYLSLHGLGKEVSGRNRYGNDDDSVFTPLADDAEPSDFDDDWVANMDD
Protein: 4-hydroxybenzoate geranyltransferase 1 (EC 2.5.1.93) (PHB geranyltransferase 1) (LePGT1) (Q8W405)
Organism: Lithospermum erythrorhizon (Purple gromwell) (Lithospermum officinale var. erythrorhizon)
Function: Prenyltransferase involved in the biosynthesis of shikonin, a naphthoquinone secondary metabolite. Could accept only geranyl diphosphate and not dimethylallyl diphosphate, farnesyl diphosphate, or geranylgeranyl diphosphate as substrate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVSSKQTQLKKGKQPSWIEMYLPKEVRPYAHLARLDKPIGSWLLAWPAFWSVALAADLESLPKMLAIFGWWAVWIRGAGCTINDYFDRNFDKKVERTKSRPLASGAVSPAQGLWWLAFQLFIGLGVLYQFNVLTLALAIVHVPFVFAYPLMKRITYWPQAFLGVMISWGALLGSSALKGSVVPSIAYPLYISSFFWTLVYDTIYAHQDKVDDAKAGIKSTALRFGDATKMWISWFGVGCIAALVIGGLILNIGLPYYVFVAIATGQLVWQIFTVDLLSPLDCGKKFVSNQWFGAIIFTGILLGRLFP
Protein: Envelope glycoprotein D (gD) (Glycoprotein IV) (P0CK30)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Function: Envelope glycoprotein that binds to host cell entry receptors. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity).
Subcellular location: Virion membrane {ECO:0000250|UniProtKB:Q05059}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q05059}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. {ECO:0000250|UniProtKB:Q69091}.
Interaction partners:
Sequence:
MQGPTLAVLGALLAVAVSLPTPAPRVTVYVDPPAYPMPRYNYTERWHTTGPIPSPFADGREQPVEVRYATSAAACDMLALIADPQVGRTLWEAVRRHARAYNATVIWYKIESGCARPLYYMEYTECEPRKHFGYCRYRTPPFWDSFLAGFAYPTDDELGLIMAAPARLVEGQYRRALYIDGTVAYTDFMVSLPAGDCWFSKLGAARGYTFGACFPARDYEQKKVLRLTYLTQYYPQEAHKAIVDYWFMRHGGVVPPYFEESKGYEPPPAADGGSPAPPGDDEAREDEGETEDGAAGREGNGGPPGPEGDGESQTPEANGGAEGEPKPGPSPDADRPEGWPSLEAITHPPPAPATPAAPDAVPVSVGIGIAAAAIACVAAAAAGAYFVYTRRRGAGPLPRKPKKLPAFGNVNYSALPG
Protein: Adenylyltransferase and sulfurtransferase UBA4 (Needs CLA4 to survive protein 3) (Ubiquitin-like protein activator 4) [Includes: Adenylyltransferase UBA4 (EC 2.7.7.-); Sulfurtransferase UBA4 (EC 2.8.1.-)] (P38820)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ubiquitin-related modifier 1
- Thiosulfate sulfurtransferase TUM1
- Cysteine desulfurase, mitochondrial
- Cytoplasmic tRNA 2-thiolation protein 1
- Cytoplasmic tRNA 2-thiolation protein 2
- Elongator complex protein 1
- Elongator complex protein 6
- Elongator complex protein 4
- Elongator complex protein 3
- Minichromosome maintenance protein 5
Sequence:
MNDYHLEDTTSELEALRLENAQLREQLAKREDSSRDYPLSLEEYQRYGRQMIVEETGGVAGQVKLKNTKVLVVGAGGLGCPALPYLAGAGVGQIGIVDNDVVETSNLHRQVLHDSSRVGMLKCESARQYITKLNPHINVVTYPVRLNSSNAFDIFKGYNYILDCTDSPLTRYLVSDVAVNLGITVVSASGLGTEGQLTILNFNNIGPCYRCFYPTPPPPNAVTSCQEGGVIGPCIGLVGTMMAVETLKLILGIYTNENFSPFLMLYSGFPQQSLRTFKMRGRQEKCLCCGKNRTITKEAIEKGEINYELFCGARNYNVCEPDERISVDAFQRIYKDDEFLAKHIFLDVRPSHHYEISHFPEAVNIPIKNLRDMNGDLKKLQEKLPSVEKDSNIVILCRYGNDSQLATRLLKDKFGFSNVRDVRGGYFKYIDDIDQTIPKY
Protein: 35 kDa gas vesicle protein (P81003)
Organism: Dactylococcopsis salina (strain PCC 8305) (Myxobactron salinum)
Function: May confer stability to the gas vesicle membranes. Gas vesicles are small, hollow, gas filled protein structures that are found in several microbial planktonic microorganisms. They allow the positioning of the organism at the favorable depth for growth.
Subcellular location: Gas vesicle shell {ECO:0000269|PubMed:1527496}. Note=Binds to the external surface of the gas vesicle. {ECO:0000269|PubMed:1527496}.
Interaction partners:
Sequence:
MVSLREQWNEQARERQREISARKTEIEEARSSIQKELQAQYEARLAATQQLQSELRQFYNNLANDTAGFLERTRTTREQMAQKLEQELTQLITDLENNTAALLQEANQERVRVSQQQKALAIELKNQLAQFHEQLETSVGNWRQETQEQQQQTAAQLREDLNAFSANLMAQVEKLLINLEETRTANAQQQREALFNFRRQLTVDVWGETESDSLKVEENTPSDVWGETESDFLEVEENTPFVT
Protein: Protein phosphatase 1 regulatory subunit 35 (Q8TAP8)
Organism: Homo sapiens (Human)
Function: During centriole duplication, plays a role in the centriole elongation by promoting the recruitment of the microtubule-binding elongation machinery through its interaction with RTTN, leading to the centriole to centrosome conversion. In addition, may play a role in the primary cilia assembly (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30168418}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}. Note=Recruited to the nascent daughter centriole early in the duplication cycle and localizes to the proximal centriolar lumen just above the cartwheel (PubMed:30168418, PubMed:30230954). Co-localizes with RTTN at the centriole (PubMed:30168418). {ECO:0000269|PubMed:30168418, ECO:0000269|PubMed:30230954}.
Interaction partners:
- Rotatin
Sequence:
MMMGCGESELKSADGEEAAAVPGPPPEPQVPQLRAPVPEPGLDLSLSPRPDSPQPRHGSPGRRKGRAERRGAARQRRQVRFRLTPPSPVRSEPQPAVPQELEMPVLKSSLALGLELRAAAGSHFDAAKAVEEQLRKSFQIRCGLEESVSEGLNVPRSKRLFRDLVSLQVPEEQVLNAALREKLALLPPQARAPHPKEPPGPGPDMTILCDPETLFYESPHLTLDGLPPLRLQLRPRPSEDTFLMHRTLRRWEA
Protein: U4/U6.U5 tri-snRNP-associated protein 1 (SNU66 homolog) (hSnu66) (Squamous cell carcinoma antigen recognized by T-cells 1) (SART-1) (hSART-1) (U4/U6.U5 tri-snRNP-associated 110 kDa protein) (allergen Hom s 1) (O43290)
Organism: Homo sapiens (Human)
Function: Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:11350945, ECO:0000269|PubMed:9449708}. Note=Found in the nucleus of mitogen-activated peripheral blood mononuclear cells (PBMCs), tumor cells, or normal cell lines, but not in normal tissues except testis and fetal liver or in unstimulated PBMCs, suggesting preferential expression in proliferating cells.
Interaction partners:
- Splicing factor 3B subunit 4
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D1
- U6 snRNA-associated Sm-like protein LSm8
- Splicing factor 3A subunit 3
- U6 snRNA-associated Sm-like protein LSm2
- Splicing factor 3B subunit 1
- 116 kDa U5 small nuclear ribonucleoprotein component
- NHP2-like protein 1
- Pre-mRNA-processing-splicing factor 8
Sequence:
MGSSKKHRGEKEAAGTTAAAGTGGATEQPPRHREHKKHKHRSGGSGGSGGERRKRSRERGGERGSGRRGAEAEARSSTHGRERSQAEPSERRVKREKRDDGYEAAASSKTSSGDASSLSIEETNKLRAKLGLKPLEVNAIKKEAGTKEEPVTADVINPMALRQREELREKLAAAKEKRLLNQKLGKIKTLGEDDPWLDDTAAWIERSRQLQKEKDLAEKRAKLLEEMDQEFGVSTLVEEEFGQRRQDLYSARDLQGLTVEHAIDSFREGETMILTLKDKGVLQEEEDVLVNVNLVDKERAEKNVELRKKKPDYLPYAEDESVDDLAQQKPRSILSKYDEELEGERPHSFRLEQGGTADGLRERELEEIRAKLRLQAQSLSTVGPRLASEYLTPEEMVTFKKTKRRVKKIRKKEKEVVVRADDLLPLGDQTQDGDFGSRLRGRGRRRVSEVEEEKEPVPQPLPSDDTRVENMDISDEEEGGAPPPGSPQVLEEDEAELELQKQLEKGRRLRQLQQLQQLRDSGEKVVEIVKKLESRQRGWEEDEDPERKGAIVFNATSEFCRTLGEIPTYGLAGNREEQEELMDFERDEERSANGGSESDGEENIGWSTVNLDEEKQQQDFSASSTTILDEEPIVNRGLAAALLLCQNKGLLETTVQKVARVKAPNKSLPSAVYCIEDKMAIDDKYSRREEYRGFTQDFKEKDGYKPDVKIEYVDETGRKLTPKEAFRQLSHRFHGKGSGKMKTERRMKKLDEEALLKKMSSSDTPLGTVALLQEKQKAQKTPYIVLSGSGKSMNANTITK
Protein: Eukaryotic translation initiation factor 3 subunit J (eIF3j) (Eukaryotic translation initiation factor 3 subunit 1) (eIF-3-alpha) (eIF3 p35) (O75822)
Organism: Homo sapiens (Human)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit D
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit F
- Eukaryotic translation initiation factor 3 subunit H
Sequence:
MAAAAAAAGDSDSWDADAFSVEDPVRKVGGGGTAGGDRWEGEDEDEDVKDNWDDDDDEKKEEAEVKPEVKISEKKKIAEKIKEKERQQKKRQEEIKKRLEEPEEPKVLTPEEQLADKLRLKKLQEESDLELAKETFGVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVCISLEIDDLKKITNSLTVLCSEKQKQEKQSKAKKKKKGVVPGGGLKATMKDDLADYGGYDGGYVQDYEDFM
Protein: Hybrid signal transduction histidine kinase C (EC 2.7.13.3) (Q95PI2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts in a signal transduction pathway that regulates the slug versus culmination choice. Believed to be the first component of a phosphorelay that couples the sensing of ammonia to the modulation of PKA activity and hence activates culmination and spore germination. Ammonium transporters amtA and amtC are thought to respectively activate and inhibit dhkC phosphorelay. This protein probably undergoes an ATP-dependent autophosphorylation at conserved His residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ammonium transporter 3
- Phosphorelay intermediate protein rdeA
Sequence:
MIVEVELGFLLSTLFFTIISIILFYFFINNKNNLIDQCQEVTKLNNKDNKIVNNNNNNYNNNNFNKIEEINDDKNKEIIKLINNSNNKNLKIKIQEIDSGNNNNNNNNNNNNNNNNLNKNSNEIFRNFKIFSGSLLVIDQDLNIISSSESVRDIFSNINDINGVNQQVIGSLQNYSFINLVHQKDKDRVSTFLKLKFKNNNNIKHQQFSEDIINEKDELKEIQIEDNKELIIINNNNNNNNDNVLKFGNNNSNNSSIILFQGVYHLNNTDLSKPFNLQVSILPFISENYIVLSLKDLSPPPLRLLLNKTSSALSPRSLSSSSSSSPSSSNNNGNTNNSGSLSPRSSNSNGSAVSPRNVSSNSMSPRGQNSDRSISSPRGSSSSSSSSSNELAISPRNSNGTISSPRTSNLSIESVLNNKSIDMISHLSHELRTPIHSVIASIQLFRSTILTVTQNEYLSIIDTSANTLLELVSNVLDYKRIRSGKLTLNNVDFNLCHVIEDVCAMVSPQAQAKSLQIASFIFIHCPLSFYGDPIRLRQVLLNLIGNGLKYTNKGQVCISVEPEQVNEHCMYLHFQVKDSGIGIKEENMSKLFAGFSQVNNGGTTQEALGSGLGLAISKDLVELMGGKIWCSSNATQNNGEAGCTFHFVIPLETNPKQLPCPIQNFNGLSVLVVDKNPYIQTVLCQYLEGWNCQVIKSSDIKEASNKLKDLRREQIEVVMIDIDNIDFRDFIQFKDAFNRLEFGRIGLITMSSDRSMVNEMGFGTSKLTKPFRQSHLVACLLASMPEHSSSTTNCFSNIVGMNSNINNNNNINNNSNNNNNNMQTHNSNSVYGNGNYGNCTPFSNNNNRIHMMSSGDKPSINNRRMSISLGKIPTFNSGGSNSPRSKKLFEEVLQQQQLQQQLQQQLQQQQQLQQQQQQQQQQQQQQQQQLQQQQQQLNTIDDDSNNYCNTTGTMDSIDEINKNNYSDSESDELNDDQAPIIAPVQQLSFGRVTRRHSIDIIMFENSRELSELRNLEDSTRYLSPRSMNNNNGNNDNGINGGSGNSLFGSSIKEEIGGTSDTSSLAQSPNSLSPRAPTKIMILDDNPVSLKLMQRILESRGFECYPFDCSEKAVAQLDQVNPAIIFMDCEMPKMNGFECTQLIRKREQESLCLLKDRKIIIALTAHINPEIQVKCFDAGMNDFISKPFKPQCLELILRKWEDCISNNQLNYNNSLINNQTTIQEQV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (X1WG08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSENLNDKMVKFLSPPSKNTNGSSSDTLVGEHLGVDVRRRHHTMDRELLKAEHRFFRRSVINDSNATALELPSKNAILTHSTDSHAPVCEPPALETKAASVITQSAPEKKVADVVEMVIESTPVLITNAALHLSAEAPSLVSEVKSGDGIDGKREAEKEEDEDSKEKAARAEAELRDAKKEEEDNEEIETNAVGTSPDGRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESSLKGRKCIVLVTELMTSGTLKTYLKRFKEMKIKVLRSWCRQILKGLHFLHTRSPPIIHRDLKCDNIFITGPTGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRVTSGVKPGSFDKVAIPEVKEIIEGCIRQNKDERYCIKDLLSHAFFQEETGVRVELAEEDDGELVAIKLLLRIEDVKKLKGKYKENEAIEFSFDLDKDVPDDVAQEMVESGYICEGDHKTIAKAIKDRVSLISRKREQRKLVREEQEKRKMEQENDAAQQTNPTVKSPGSALASVIMESEEAETDQHQQPGASASAVGFVDPQSSVTILEAHPVQPNTSFSTTQPDPQPQHTIIRPQSMSQHPVQAPLQQPSSTLTLGPVPQTSPPQVIGQTASLPSTVQSIVPLQYRQPPQDGITLPQSLPSAQVLQAPLSVSQSQPVEQTQPQTSLVPASTESGHSDPASGLSDGNEGRHEGRSMKRPQRRSVRSRSRHEKTAKVKLNVLNISNIGDRVAECQLETHNRKMVTFKFDLDGDNPVEIAEIMVKSDFILESERESFIEQVQLVIQNADQKGKAPQNSQTQVISNSSQQVPEILTSSVPGMPPSLAAQVVHSAGRRFIVSPVPEARLREPLFGTPSANTSFEDTAPAPDPTSASSAPQDQANFASDSNQISVVPPTPGDLAPESSIPPTSQSPYQNPVPSSTATLTVTTTQVSTPTPTTTPQPITGRTSPSPAPTEPPAARRMSLPSPSQTPQIAPGESNGLDQAQASNQQVTQPSATGDSESDVQGKPPGIEDIHALDQKLRSLFKDSSQNSCSQPDGSGETSTTSPPNTISTNTPGFVSGVTPSSLSLNSSGNFAPGAFASIGTPTSYTQTPSTDQSPPRPQIAVGVTQPDGHNSTEEKEPQLEKAFQLGRFQVSVASDQDPPTALDPGVVVSSSSATPSSTSSSSSSSSSPSSLSSPENTIHKSQTPPPRVSPEPVPPTTTVGRFQVTCSTDIKLGRFSVTPAERKSSSVEGPDTAKEPKLTPSSVSITNHYLSSDNDSEPEDEGLRREMNRLKERHKVEIMALQNKQKKEIEELFTRLGKTPSVVVPPTVAMTPGRRRPAKGKGNRPRSGSATQAASFQQGNKQAVQSGSLSQSASEKTSPSETAPSSNNDVQDNTSPVRKENGQSHDQDQTPTTNLPRKGTFTDDLHQLVDNWARDAMNMMPQVKKGSKKNVHEMPRKYSAPGQLCSTGGHIPATINPTAGRKGSIGVANQQFGYTCPNYNMPQWNQVGTISSTAPPAGLQQGFLIPSGAHQTGNNCGSSNLRTTQAS
Protein: Centromere protein W (A0A0A0MRK5)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALSTIVSQRKQIKRKAPRGFLKRVFKRKKPQLRLEKSGDLLKSPGQTLVRVNVESLTRSMYWPQQR
Protein: Protein S100-A12 (Calgranulin-C) (CAGC) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (S100 calcium-binding protein A12) (P80310)
Organism: Sus scrofa (Pig)
Function: S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites (By similarity).
Subcellular location: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation is secreted via a microtubule-mediated, alternative pathway (By similarity). {ECO:0000250}.
Interaction partners:
- Protein S100
- Protein S100-A9
- Natural resistance-associated macrophage protein 1
- Advanced glycosylation end product-specific receptor
- Protein S100-A11
- Protein S100-A6
Sequence:
MTKLEDHLEGIINIFHQYSVRLGHYDTLIKRELKQLITKELPNTLKNTKDQGTIDKIFQNLDANQDEQVSFKEFVVLVTDVLITAHDNIHKE
Protein: Protein BEARSKIN2 (NAC domain-containing protein 70) (ANAC070) (Q9SV87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator. Together with BRN1 and SMB, regulates cellular maturation of root cap. Promotes the expression of genes involved in secondary cell walls (SCW) biosynthesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- AT-hook motif nuclear-localized protein 11
- NAC domain protein
- At3g10000
Sequence:
MGSSSNGGVPPGFRFHPTDEELLHYYLKKKISYQKFEMEVIREVDLNKLEPWDLQERCKIGSTPQNEWYFFSHKDRKYPTGSRTNRATHAGFWKATGRDKCIRNSYKKIGMRKTLVFYKGRAPHGQKTDWIMHEYRLEDADDPQANPSEDGWVVCRVFMKKNLFKVVNEGSSSINSLDQHNHDASNNNHALQARSFMHRDSPYQLVRNHGAMTFELNKPDLALHQYPPIFHKPPSLGFDYSSGLARDSESAASEGLQYQQACEPGLDVGTCETVASHNHQQGLGEWAMMDRLVTCHMGNEDSSRGITYEDGNNNSSSVVQPVPATNQLTLRSEMDFWGYSK
Protein: Gamma-interferon-inducible lysosomal thiol reductase (EC 1.8.-.-) (Gamma-interferon-inducible protein IP-30) (M9WEU5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU369109}. Lysosome {ECO:0000256|RuleBase:RU369109}.
Interaction partners:
Sequence:
MKGIILFTLLTIWSNVDCKSCSYSPSQWCTSLDSAIECGVLKQCLETNATKPNTLEQSVQVELYYESLCPACRYFLTSQLLPTWTMLQDAMSVTLVPYGNAGESFDGKKYQFTCQHGEEECLGNMIETCILNVTGSNAFQIIYCMEASTDVVKAGEKCVELYDPTTKWDSIMTCVKGDQGNQLMHQNAVKTGALKPTHNYVPWIVINGEHTEELQDKAMSSLFALVCSMYKGSKPEACSTALMKRHRSYCHDE