wanglab/gogpt-training-data huggingface dataset:
Protein: Sex-determining region Y protein (Testis-determining factor) (Q05738)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that controls a genetic switch in male development. It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells. Involved in different aspects of gene regulation including promoter activation or repression. Binds to the DNA consensus sequence 5'-[AT]AACAA[AT]-3'. SRY HMG box recognizes DNA by partial intercalation in the minor groove and promotes DNA bending. Also involved in pre-mRNA splicing (By similarity). In male adult brain involved in the maintenance of motor functions of dopaminergic neurons (By similarity).
Subcellular location: Nucleus speckle {ECO:0000250|UniProtKB:Q05066}. Cytoplasm {ECO:0000269|PubMed:11535586, ECO:0000269|PubMed:15469996, ECO:0000269|PubMed:16488877, ECO:0000269|PubMed:19349578}. Nucleus {ECO:0000269|PubMed:19349578}. Note=Acetylation contributes to its nuclear localization and deacetylation by HDAC3 induces a cytoplasmic delocalization (By similarity). Colocalizes in the nucleus with ZNF208 isoform KRAB-O and tyrosine hydroxylase (TH) (PubMed:15469996). Colocalizes with SOX6 in speckles. Colocalizes with CAML in the nucleus (By similarity). Nuclear import is facilitated by XPO4, a protein that usually acts as a nuclear export signal receptor (PubMed:19349578). {ECO:0000250|UniProtKB:Q05066, ECO:0000269|PubMed:15469996, ECO:0000269|PubMed:19349578}.
Interaction partners:
- Steroidogenic factor 1
- Sulfhydryl oxidase 1
- Wilms tumor protein homolog
- Transcription factor SOX-9
- Forkhead box protein L2
- Muellerian-inhibiting factor
- ATP-dependent RNA helicase DDX3Y
- Transcription factor GATA-4
- Zinc finger Y-chromosomal protein 1
Sequence:
MEGHVKRPMNAFMVWSRGERHKLAQQNPSMQNTEISKQLGCRWKSLTEAEKRPFFQEAQRLKILHREKYPNYKYQPHRRAKVSQRSGILQPAVASTKLYNLLQWDRNPHAITYRQDWSRAAHLYSKNQQSFYWQPVDIPTGHLQQQQQQQQQQQFHNHHQQQQQFYDHHQQQQQQQQQQQQFHDHHQQKQQFHDHHQQQQQFHDHHHHHQEQQFHDHHQQQQQFHDHQQQQQQQQQQQFHDHHQQKQQFHDHHHHQQQQQFHDHQQQQQQFHDHQQQQHQFHDHPQQKQQFHDHPQQQQQFHDHHHQQQQKQQFHDHHQQKQQFHDHHQQKQQFHDHHQQQQQFHDHHQQQQQQQQQQQQQFHDQQLTYLLTADITGWKGIKHCTGPDPEPF
Protein: Neurogenin-1 (NGN-1) (Helix-loop-helix protein mATH-4C) (mATH4C) (Neurogenic basic-helix-loop-helix protein) (Neurogenic differentiation factor 3) (NeuroD3) (P70660)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional regulator. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Achaete-scute homolog 1
- POU domain, class 4, transcription factor 1
- Paired box protein Pax-6
- Voltage-dependent T-type calcium channel subunit alpha
Sequence:
MPAPLETCISDLDCSSSNSSSDLSSFLTDEEDCARLQPLASTSGLSVPARRSAPALSGASNVPGAQDEEQERRRRRGRARVRSEALLHSLRRSRRVKANDRERNRMHNLNAALDALRSVLPSFPDDTKLTKIETLRFAYNYIWALAETLRLADQGLPGGSARERLLPPQCVPCLPGPPSPASDTESWGSGAAASPCATVASPLSDPSSPSASEDFTYGPGDPLFSFPGLPKDLLHTTPCFIPYH
Protein: Antitoxin PrlF (HtrA suppressor protein SohA) (P15373)
Organism: Escherichia coli (strain K12)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the YhaV toxin and neutralizes its ribonuclease activity. Also acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribonuclease toxin YhaV
- mRNA interferase toxin RelE
- Toxin YoeB
- Antitoxin YefM
- Antitoxin DinJ
- mRNA interferase toxin YafQ
- Antitoxin MqsA
- Endoribonuclease toxin ChpB
- Antitoxin HigA
- Antitoxin YafN
Sequence:
MPANARSHAVLTTESKVTIRGQTTIPAPVREALKLKPGQDSIHYEILPGGQVFMCRLGDEQEDHTMNAFLRFLDADIQNNPQKTRPFNIQQGKKLVAGMDVNIDDEIGDDE
Protein: Actin-depolymerizing factor 2 (ADF-2) (AtADF2) (Q39251)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers. Required for normal cell growth, plant development, cell organ expansion and flowering. Essential for root-knot nematode infection.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q39250}.
Interaction partners:
- Profilin-1
- Profilin-2
- Profilin-4
- Profilin-5
- Profilin-3
- Cyclase-associated protein 1
- Villin-5
- Villin-1
- Protein phosphatase EYA
- Protein BRICK 1
Sequence:
MANAASGMAVHDDCKLKFMELKAKRTFRTIVYKIEDKQVIVEKLGEPEQSYDDFAASLPADDCRYCIYDFDFVTAENCQKSKIFFIAWSPDTAKVRDKMIYASSKDRFKRELDGIQVELQATDPTEMGLDVFKSRTN
Protein: Imidazole glycerol phosphate synthase subunit HisF (EC 4.3.2.10) (IGP synthase cyclase subunit) (IGP synthase subunit HisF) (ImGP synthase subunit HisF) (IGPS subunit HisF) (Q9X0C6)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Subcellular location: Cytoplasm.
Interaction partners:
- Histidine biosynthesis bifunctional protein HisIE
- Histidinol dehydrogenase
- 1-
- Imidazoleglycerol-phosphate dehydratase
- Imidazole glycerol phosphate synthase subunit HisH
- Histidinol-phosphate aminotransferase
- ATP phosphoribosyltransferase
- Bifunctional purine biosynthesis protein PurH
- Adenine phosphoribosyltransferase
- Adenylosuccinate lyase
Sequence:
MLAKRIIACLDVKDGRVVKGTNFENLRDSGDPVELGKFYSEIGIDELVFLDITASVEKRKTMLELVEKVAEQIDIPFTVGGGIHDFETASELILRGADKVSINTAAVENPSLITQIAQTFGSQAVVVAIDAKRVDGEFMVFTYSGKKNTGILLRDWVVEVEKRGAGEILLTSIDRDGTKSGYDTEMIRFVRPLTTLPIIASGGAGKMEHFLEAFLAGADAALAASVFHFREIDVRELKEYLKKHGVNVRLEGL
Protein: Myeloid differentiation primary response protein MyD88 (S6FDG5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|PIRNR:PIRNR037756}.
Interaction partners:
Sequence:
MSASLDLWNIPLRALNINVRKRLGLFLNPRNTVASDWMSVAENMGFSYLEIKNYEDCQDPTRKILEDWQARCPGAKVGKLVSILDNVDRKDVVEDLRVLIEEDCKRYIERQNEPPVQVPEVDSCVPRTPERQGITLEDDPEGGIPELFDAFICYCQSDFDFVHEMIQQLEQTDHKLKLCVFDRDVLPGSCVWTITSELIEKRCKRMVVVISDEYLDSDACDFQTKFALSLCPGARSKRLIPVKYKSMKKPFPSILRFLTVCDYTRPCTQSWFWVRLAKALSLP
Protein: Immunoglobulin lambda variable 3-27 (Ig lambda chain V-IV region Kern) (P01718)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWIPLLLPLLILCTVSVASYELTQPSSVSVSPGQTARITCSGDVLAKKYARWFQQKPGQAPVLVIYKDSERPSGIPERFSGSSSGTTVTLTISGAQVEDEADYYCYSAADNN
Protein: Metacaspase-9 (AtMC9) (EC 3.4.22.-) [Cleaved into: Metacaspase-9 subunit p20; Metacaspase-9 subunit p10 (Metacaspase 2f) (AtMCP2f)] (Q9FYE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Required for proteolytic processing of GRI.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:17028019}.
Interaction partners:
- Serpin-ZX
- Endonuclease 1
- Cysteine protease XCP1
- Cysteine protease XCP2
- Cysteine proteinase RD21A
- Pollen receptor-like kinase 5
- Protein GRIM REAPER
- Bifunctional nuclease 1
- Uncharacterized protein AT3g24100
- Peroxidase 20
Sequence:
MDQQGMVKKRLAVLVGCNYPNTRNELHGCINDVLAMKETILSRFGFKQDDIEVLTDEPESKVKPTGANIKAALRRMVDKAQAGSGDILFFHYSGHGTRIPSVKSAHPFKQDEAIVPCDFNLITDVDFRELVNQLPKGTSFTMISDSCHSGGLIDKEKEQIGPSSVSSNISPAIETTNKTITSRALPFKAVLDHLSSLTGITTSDIGTHLLELFGRDAGLKFRLPAMDLMDLLETMTAREKHVDSGILMSGCQADETSADVGVGNGKAYGAFSNAIQRVLNENEGAMKNKQLVMMARDVLERLGFHQHPCLYCSDQNADATFLSQP
Protein: Aristaless-related ALX3 (Q6RW14)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MDPERCAPFAVGPAAGPYAAARDEAPGPQGTPDAAPHLRPAPPRGPRLSRFPACGPLEPYLPEPAKPPAKYLQDLGPGPVLNGGHFYEGSSEAEEKASKAASFPQLPVDCRGGPRDGPSNVQGSPGPCLASLSVPLSPGLPDSMELAKSKSKKRRNRTTFSTFQLEELEKVFQKTHYPDVYAREQLALRTDLTEARVQVWFQNRRAKWRKRERYGKIQEGRNPFTTAYDISVLPRTDSHPQLQNSLWSSPGSGSPGGPCLMPPEGIPSPCMSPYSHSHGNVAGFMGVPASPAAHPGIYSIHGFPPALGGHSFEPSPDGDYKSPSLVSLRMKPKEPPSLLNWTT
Protein: NAC domain-containing protein 66 (ANAC066) (Protein NAC SECONDARY WALL THICKENING PROMOTING FACTOR 2) (Q9M274)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator of genes involved in biosynthesis of secondary walls. Together with NST1, required for the secondary cell wall thickening of the anther endocethium, which is necessary for anther dehiscence. May also regulate the secondary cell wall lignification of other tissues such as tracheary elements.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor MYB63
- Transcription factor MYB46
- Transcription factor MYB26
- Transcription factor MYB83
- Transcription factor MYB58
- MYB transcription factor
- MYB transcription factor
- Transcription factor MYB54
- Transcription factor MYB52
- At5g52380
Sequence:
MNISVNGQSQVPPGFRFHPTEEELLKYYLRKKISNIKIDLDVIPDIDLNKLEPWDIQEMCKIGTTPQNDWYFYSHKDKKYPTGTRTNRATTVGFWKATGRDKTIYTNGDRIGMRKTLVFYKGRAPHGQKSDWIMHEYRLDESVLISSCGDHDVNVETCDVIGSDEGWVVCRVFKKNNLCKNMISSSPASSVKTPSFNEETIEQLLEVMGQSCKGEIVLDPFLKLPNLECHNNTTITSYQWLIDDQVNNCHVSKVMDPSFITSWAALDRLVASQLNGPNSYSIPAVNETSQSPYHGLNRSGCNTGLTPDYYIPEIDLWNEADFARTTCHLLNGSG
Protein: ADP-ribosylation factor 6 (EC 3.6.5.2) (P62331)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein involved in protein trafficking that regulates endocytic recycling and cytoskeleton remodeling. Required for normal completion of mitotic cytokinesis. Involved in the regulation of dendritic spine development, contributing to the regulation of dendritic branching and filopodia extension. Plays an important role in membrane trafficking, during junctional remodeling and epithelial polarization. Regulates surface levels of adherens junction proteins such as CDH1. Required for NTRK1 sorting to the recycling pathway from early endosomes (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62330}. Cell membrane {ECO:0000269|PubMed:29420262}; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Endosome membrane; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Recycling endosome membrane {ECO:0000250|UniProtKB:P62330}; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P62330}; Lipid-anchor {ECO:0000250|UniProtKB:P62330}. Cell projection, ruffle {ECO:0000250|UniProtKB:P62330}. Cleavage furrow {ECO:0000250|UniProtKB:P62330}. Midbody, Midbody ring {ECO:0000269|PubMed:22522702}. Early endosome membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}. Note=Distributed uniformly on the plasma membrane, as well as throughout the cytoplasm during metaphase (By similarity). Subsequently concentrated at patches in the equatorial region at the onset of cytokinesis, and becomes distributed in the equatorial region concurrent with cleavage furrow ingression (By similarity). In late stages of cytokinesis, concentrates at the midbody ring/Flemming body (By similarity). Recruitment to the midbody ring requires both activation by PSD/EFA6A and interaction with KIF23/MKLP1 (By similarity). After abscission of the intercellular bridge, incorporated into one of the daughter cells as a midbody remnant and localizes to punctate structures beneath the plasma membrane (PubMed:22522702). Recruited to the cell membrane in association with CYTH2 and ARL4C (By similarity). Colocalizes with DAB2IP at the plasma membrane and endocytic vesicles (By similarity). Myristoylation is required for proper localization to membranes: myristoylation on Lys-3 allows ARF6 to remain on membranes during the GTPase cycle (By similarity). {ECO:0000250|UniProtKB:P62330, ECO:0000269|PubMed:22522702}.
Interaction partners:
- Cytohesin-2
- Cytohesin-3
- Cytohesin-1
- Cytohesin-4
- Phospholipase D2
- ADP-ribosylation factor-binding protein GGA3
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- C-Jun-amino-terminal kinase-interacting protein 4
- Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1
Sequence:
MGKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS
Protein: Autophagy-related protein 18 (Q9HDZ7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct atg9 trafficking to the preautophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). Required for the recruitment of the atg5-atg12/atg16 complex to the preautophagosomal structure.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. Vacuole membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 2
- Autophagy-related protein 9
- Autophagy-related protein 8
- Ubiquitin-like protein ATG12
- Serine/threonine-protein kinase atg1
- Autophagy protein 5
- Autophagy-related protein 3
- Polyphosphoinositide phosphatase
- Ubiquitin-like modifier-activating enzyme atg7
- Phosphatidylinositol 3-kinase pik3
Sequence:
MHFFVRKYRGKAALLSIGTFDGYKIYNCDPFGKCFHKIQGATSIVEMLFSTSLVALVEKDDGNNRKLKLINTKKSTTICELTFPTPLLAVKLNRKRLLAVLEEQIYVYDISNMLLLHTIETTSNVFAVCALSPNSENCYLAYPDSRDHEPRTEGESSSPNVSNSAVSGQVILWDVINCKQITKIEAHKDSLACLAFNSDGTMLATASDNGRIIRVFAIPSGQRLYQFRRGSLPAQIYSIAFHPDSSLLTVTSSTQTVHIFRLKEVYSNLERQGLLPSSPPPKESLLRRSSRSLIGTVGGYLPQSVSGMLDPERDFAYAHIPGDKVTSIAAFGPDNTIVNVATYDGNLYSFRVNLRTGGECAMVNHFCVGLTAA
Protein: Pterin-4-alpha-carbinolamine dehydratase 2 (PHS 2) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase 2) (DcoH-like protein DCoHm) (Dimerization cofactor of hepatocyte nuclear factor 1 from muscle) (HNF-1-alpha dimerization cofactor) (Q9CZL5)
Organism: Mus musculus (Mouse)
Function: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity).
Interaction partners:
- Tyrosine 3-monooxygenase
- Phenylalanine-4-hydroxylase
- Tryptophan 5-hydroxylase 1
- Tryptophan 5-hydroxylase 2
- Dihydropteridine reductase
- Pterin-4-alpha-carbinolamine dehydratase
- Hepatocyte nuclear factor 1-alpha
Sequence:
MVAAAAVAVAAVGARSAGRWLAALRSPGASRAAMSSDAQWLTAEERDQLIPGLKAAGWSELSERDAIYKEFSFKNFNQAFGFMSRVALQAEKMNHHPEWFNVYNKVQITLTSHDCGGLTKRDVKLAQFIEKAAASL
Protein: Non-structural protein NS3 (Q84362)
Organism: Aleutian mink disease parvovirus (strain G) (ADV)
Function: Plays a role in viral DNA replication.
Subcellular location: Host nucleus {ECO:0000269|PubMed:24606679}. Note=Does not localize within the viral DNA replication centers.
Interaction partners:
Sequence:
MAQAQIDEQRRLQDLYVQLKKEINDGEGVAWLFQQKTYTDKDNKPTKATPPLRTTSSDLRLCDCNKQHQHNQSNCWMCGNKRSRRAT
Protein: Homeobox protein Hox-A11 (Homeobox protein Hox-1I) (P31270)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-A10
- Forkhead box protein O1
- Paired box protein Pax-2
- Homeobox protein Hox-A13
- Pre-B-cell leukemia transcription factor 1
Sequence:
MDFDERGPCSSNMYLPSCTYYVSGPDFSSLPSFLPQTPSSRPMTYSYSSNLPQVQPVREVTFREYAIEPATKWHPRGNLAHCYSAEELVHRDCLQAPSAAGVPGDVLAKSSANVYHHPTPAVSSNFYSTVGRNGVLPQAFDQFFETAYGTPENLASSDYPGDKSAEKGPPAATATSAAAAAAATGAPATSSSDSGGGGGCRETAAAAEEKERRRRPESSSSPESSSGHTEDKAGGSSGQRTRKKRCPYTKYQIRELEREFFFSVYINKEKRLQLSRMLNLTDRQVKIWFQNRRMKEKKINRDRLQYYSANPLL
Protein: Predicted protein (F2D891)
Organism: Hordeum vulgare subsp. vulgare (Domesticated barley)
Interaction partners:
Sequence:
MVAPATLSLRPCATLAPSRAAHAHAGFAHTSRPALSVSCPPTRFETLRRAATAVSDRQGSAEPSEKQEDKPRTYYFLVANAKFMLDDEEHFQEQLQEKLRLYEERSKEQDFWLVIEPKFLDRFPNVAKRLKRPAVALVSTDRNWIRFMKLRLDRVLAEQFDAETVEEALASNPAELKFDKPDKWTAPYPKYESGWWEAFLPPKSSNGTA
Protein: BS_ykrK family protein (A0A0H2UQN3)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MKTTFSYPKWAEIPNIDLYLDQVLLYVNQVCAPISPNKDKGLTASMVNNYVKNGYLTKPDKKKYQRQQIARLIAITTLKSVFSIQEIAQTLNTLQTQASSDQLYDAFVDYMNQGIDPANPIIQTSCQTVKLYHQTLDLIDHTQEEVIQ
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial (Protein FROSTBITE1) (Q9FJW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12084824, ECO:0000305|PubMed:25732537}; Peripheral membrane protein {ECO:0000269|PubMed:12084824}; Matrix side {ECO:0000269|PubMed:12084824}.
Interaction partners:
- NADH dehydrogenase subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10-A
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13-A
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
Sequence:
MALCATTQRTIRIAATLRRVARPFATDAVVESDYKRGEIGKVSGIPEEHLSRKVIIYSPARTATQSGSGKLGKWKINFVSTLKWENPLMGWTSTGDPYANVGDSALAFDSEEAAKSFAERHGWDYKVKKPNTPLLKVKSYSDNFKWKGNPQPEN
Protein: Euchromatic histone lysine methyltransferase 1 (A0A8I6AB09)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MLIAIVFCFLPLQQAVLAKQETKQDCCMKTELLREDTLMAADEGSTEKQAGETPMAADGETNGSCEKSGDISHPNAPKHTQENTRASPQEGTNRVSRVAENGVSERDTEVGKQNHVTADDFMQTSVIGSNGYFLNKPALQGQPLRTPNTLNSSLPGHAAKTLPGGASKCRTPSALPQTPTTAPTVPGEGSADTEDRKPTASGTDVRVHRARKTMPKSILGLHAASKDHREVQDHKEPKEDINRNISECGRQQLLPTFPALHQSLPQNQCYMATTKSQTACLPFVLAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGAKGEKVLDDSALHVNGESLEMDSEEEDSEELEDEEDRGAEQAAAFPTEDSRTSKESMSETDRAAKMDGDSEEEQESPDTGEDEDGGDESDLSSESSIKKKFLKRRGKTDSPWIKPARKRRRRSRKKPSSMLGSEACKSSPGSMEQAALGDSAGYMEVSLDSLDLRVRGILSSQTENEGLANGPDVLETDGLHEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEETSKAKEVTIAKADTTSTVTLAPGQEKSLAAEGRADTTTGSIAGAPEDEKSQSTVTQAPECFDPAGPAGFVRPTSGFSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDKPVAVEKTVSRDIARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQENGLPDTSSAAAADPL
Protein: Alkaline nuclease (Q87066)
Organism: Suid herpesvirus 1 (SuHV-1) (Pseudorabies virus)
Interaction partners:
Sequence:
MAALVLPNSLPEELAARTFLRFLRAAPRPAAVGARSYRLAYVHDLLVELARHGLAAPDAAAAAFGGARPPPAPATSPPRRARRILTVEAATRAQSESDLWTLLRRGLATASTVRWGADGPRFPPTWCEASTARCGTPTTRRSSLAASTSAWPGRPSRPVRRGAHAAPARGGDGRRRGRGRSEGGDVHLRRDGRAPAGSRPLLVRAAAGPAHRHGRGLAGPAGLRPRRRGRWGAPHADGDALLRDQVPRQVPVLGGRREPHGARVRLLGRPDADTLRGFLNSIARPGVEFFEGAPGPGEALATADPAWRARAQDAPVTRRRCGAFDARHVAANARQSEVWLFSDPVDGRQDIVPWASGERALRVPVFANPRHANFRQILVQSYVVAGVFPDRPARPHLATFFGRRRRPCEQNRTLDLASLCDVPPACAVPVLLIVTPVSVCEEAFEDLRARAEEAFRATRRGHGTVLLPILQQPRRDELRRRADLRRGRVRGL
Protein: Protein obstructor-E (Q9VMM6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chitin-binding protein that is important for the longitudinal contraction and lateral expansion of the larval cuticle during its conversion into the oval-shaped puparium case. Essential for survival to the second instar larval stage. Confers the orientated contractility and expandability of the larval cuticle by regulating the arrangement of chitin and the formation of supracellular ridges on the cuticle of third instar larvae. Essential for determining pupal body shape; required for the orientated shape change of the cuticle during metamorphosis which involves changes in the morphology of the supracellular ridges.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:28076349}.
Interaction partners:
- RE49895p
- Cuticular protein 67B
- HL04814p
Sequence:
MAKILISALLCVAMFGSMALGSPECPTPNGRFASGDQCDSYTECQDGTPVEKLCPDGLLFHQRTKATGECTYAPYSTCKERARLQPANGTEECPRQFGFYPNGDATKCGVYRNCAHGVASLTKCPEGLAFNEETYQCDWPDLVESCNAEAYLGFNCPAADSADDSAAAAVDVSPEGELRYYRHPQTCKKYFVCVNGHPRLYNCGKYLAFNSQTKLCDFYNKVPECYALLKEKQRLKAEKQQPQVAQPED