wanglab/gogpt-training-data huggingface dataset:
Protein: Choline kinase alpha (CK) (EC 2.7.1.32) (CHETK-alpha) (Ethanolamine kinase) (EK) (EC 2.7.1.82) (O54804)
Organism: Mus musculus (Mouse)
Function: Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35790}.; SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet {ECO:0000250|UniProtKB:P35790}. Note=Isoform 1 localizes to lipid droplets following phosphorylation by AMPK. {ECO:0000250|UniProtKB:P35790}.
Interaction partners:
- Ethanolamine-phosphate cytidylyltransferase
- Choline-phosphate cytidylyltransferase A
- Choline-phosphate cytidylyltransferase B
- Glycerophosphocholine phosphodiesterase GPCPD1
- Choline O-acetyltransferase
- Ethanolamine-phosphate phospho-lyase
- Phosphoethanolamine/phosphocholine phosphatase
- Choline/ethanolamine kinase
- Acetylcholinesterase
- Choline/ethanolaminephosphotransferase 1
Sequence:
MKTKFCTGGEAEPSPLGLLLSCGGNAAPTPGVGQQRDAAGELESKQLGGRTQPLALPPPPPPPLPLPPPPSPPLADEQPEPRTRRRAYLWCKEFLPGAWRGLREDQFHISVIRGGLSNMLFQCSLPDSIASVGDEPRKVLLRLYGAILKMRSCNKEGSEQAQNENEFQGAEAMVLESVMFAILAERSLGPKLFGIFPQGRLEQFIPSRRLDTEELRLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLNQVLRLKFSREARVQQLHKILSYNLPLELENLRSLLQYTRSPVVFCHNDCQEGNILLLEGQENSERRKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYTYEKYPFFRANIQKYPSRKQQLHFISSYLTTFQNDFESLSSEEQFATKEDMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMEYAQARFEAYFDQKRKLGV
Protein: Heat stress transcription factor A-1a (AtHsfA1a) (AtHsf-13) (Heat shock factor protein 1) (HSF 1) (Heat shock transcription factor 1) (HSTF 1) (P41151)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock factor-binding protein
- CDPK-related kinase 1
- Heat shock protein 90-1
- Chaperone protein ClpB1
- Autophagy-related protein 18f
- 18.1 kDa class I heat shock protein
- Dehydration-responsive element-binding protein 2A
- Multiprotein-bridging factor 1c
- Ubiquitin-like-conjugating enzyme ATG10
Sequence:
MFVNFKYFSFFIRTKMDGVTGGGTNIGEAVTAPPPRNPHPATLLNANSLPPPFLSKTYDMVEDPATDAIVSWSPTNNSFIVWDPPEFSRDLLPKYFKHNNFSSFVRQLNTYGFRKVDPDRWEFANEGFLRGQKHLLKKISRRKSVQGHGSSSSNPQSQQLSQGQGSMAALSSCVEVGKFGLEEEVEQLKRDKNVLMQELVKLRQQQQTTDNKLQVLVKHLQVMEQRQQQIMSFLAKAVQNPTFLSQFIQKQTDSNMHVTEANKKRRLREDSTAATESNSHSHSLEASDGQIVKYQPLRNDSMMWNMMKTDDKYPFLDGFSSPNQVSGVTLQEVLPITSGQSQAYASVPSGQPLSYLPSTSTSLPDTIMPETSQIPQLTRESINDFPTENFMDTEKNVPEAFISPSPFLDGGSVPIQLEGIPEDPEIDELMSNFEFLEEYMPESPVFGDATTLENNNNNNNNNNNNNNNNNNNNTNGRHMDKLIEELGLLTSETEH
Protein: Oxidoreductase, putative (EC 1.6.5.5) (Q38EM5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MRRSATFLGLTALRSVAATGWRYHKQGAPERVLQYERYRIPFDRSGSQAVVKMLAAPVHRHDRAMIGGYCGPLRPTAFPQVAGVEGVGVVEEVGKGASLLLQEGDLVWVNNPTVGTWATHVVTDVENLDVVPNRADVDIEYLASLSLFHTAYHLTNSFVSLQPNDVVLQTGASSSIAQICQGYIRARGAKLFQTMQLGRTEHAHLLAFFKMRGAFAVVPYNYVRTNYMRRLLSDVPPPKLLLNHTCGNFASSLVNLLGDNGVCVTYGNTGGKPLQIANMDVIARGIKFKGFFLPHWIKSHTREARMRVHQNVVESMTISQGHGIFRAQRFKMDGDSIFAFSNAWDAPLGSRKPVLRMVGEYGEWRRPRSDQAAWNIGRAVWDDLLQQMWESAGTTENPQSMKYYTPFNDIYSQFHDGKQSKEMGHREVFFRRPNAPRHNAAESTH
Protein: Mycinamicin VI 2''-O-methyltransferase (EC 2.1.1.238) (Mycinamicin biosynthesis protein E) (Q83WF2)
Organism: Micromonospora griseorubida
Function: O-methyltransferase that catalyzes the conversion of mycinamicin VI to mycinamicin III in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic.
Interaction partners:
Sequence:
MTAQTEFDEATVQDVVRLAGGHDSELRELTQKYDPAMISRLLVAEILSRCPPPSNDTPVLVELAIVHGSERFRHFLRVVRDSPIRPVGADEGFVGMLVEYELTELLRELFGVTHERPAGVRGTKLFPYLTDDEEAVEQIGTYLLAAQQGTEAVLAGCGSRKPDLSELSSRYFTPKFGFLHWFTPHYDRHFRDYRNQQVRVLEIGVGGYKHPEWGGGSLRMWKSFFPRGQIYGLDIMDKSHVDELRIRTIQGDQNDAEFLDRIARRYGPFDIVIDDGSHINAHVRTSFAALFPHVRPGGLYVIEDMWTAYWPGFGGQADPQECSGTSLGLLKSLIDAIQHQELPSDPNRSPGYVDRNIVGLHVYHNVAFVEKGRNDEGGIPTWIPRDFESLVQASSGGAT
Protein: Ankyrin 2 (A0A5F9ZH03)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Jerky protein homolog (O75564)
Organism: Homo sapiens (Human)
Function: May bind DNA.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00583}.
Interaction partners:
- NAD-dependent malic enzyme, mitochondrial
Sequence:
MASKPAAGKSRGEKRKRVVLTLKEKIDICTRLEKGESRKALMQEYNVGMSTLYDIRAHKAQLLRFFASSDSNKALEQRRTLHTPKLEHLDRVLYEWFLGKRSEGVPVSGPMLIEKAKDFYEQMQLTEPCVFSGGWLWRFKARHGIKKLDASSEKQSADHQAAEQFCAFFRSLAAEHGLSAEQVYNADETGLFWRCLPNPTPEGGAVPGPKQGKDRLTVLMCANATGSHRLKPLAIGKCSGPRAFKGIQHLPVAYKAQGNAWVDKEIFSDWFHHIFVPSVREHFRTIGLPEDSKAVLLLDSSRAHPQEAELVSSNVFTIFLPASVASLVQPMEQGIRRDFMRNFINPPVPLQGPHARYNMNDAIFSVACAWNAVPSHVFRRAWRKLWPSVAFAEGSSSEEELEAECFPVKPHNKSFAHILELVKEGSSCPGQLRQRQAASWGVAGREAEGGRPPAATSPAEVVWSSEKTPKADQDGRGDPGEGEEVAWEQAAVAFDAVLRFAERQPCFSAQEVGQLRALRAVFRSQQQETVGLEDVVVTSPEELAIPKCCLEASTET
Protein: Tctex1 domain-containing protein 2 (Q18917)
Organism: Caenorhabditis elegans
Interaction partners:
- DYnein Light chain
- DYnein Light chain
- Dynein light chain roadblock
- WD_REPEATS_REGION domain-containing protein
- Cytoplasmic dynein 2 light intermediate chain 1
- DYnein Light chain, Axonemal p28 type
- Probable dynein light chain 2
- Cytoplasmic dynein 2 heavy chain 1
- WD_REPEATS_REGION domain-containing protein
- Dynein light chain
Sequence:
MEDANDRNFVLRPTPGQKFRPKAVAGMIQEILGEKLGALTIYNVDEAELVSKDISASIRERLKGLQLPRYKYVIQTMIAEQCGNGATTAVQCVWDEDCDGYLTQRYVTGSIWCEVLVFAIFHY
Protein: Septum site-determining protein DivIVA (Cell division initiation protein DivIVA) (Minicell-associated protein DivIVA) (P71021)
Organism: Bacillus subtilis (strain 168)
Function: May act as a pilot protein, directing MinCD to the polar septation sites or by inhibiting MinCD at the midcell site of division. Required for polar localization of the chromosome during sporulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16885474, ECO:0000269|PubMed:9219999}. Note=Localized at the cell division site and found exclusively at the cell pole during sporulation.
Interaction partners:
- Chromosome-anchoring protein RacA
- Cell division topological determinant MinJ
- Cell division protein FtsZ
- Septum site-determining protein MinC
- Cell division protein SepF
- Cell division protein FtsA
- Cell cycle protein GpsB
- Stage 0 sporulation protein J
- Septation ring formation regulator EzrA
- Pyridoxal phosphate homeostasis protein
Sequence:
MPLTPNDIHNKTFTKSFRGYDEDEVNEFLAQVRKDYEIVLRKKTELEAKVNELDERIGHFANIEETLNKSILVAQEAAEDVKRNSQKEAKLIVREAEKNADRIINESLSKSRKIAMEIEELKKQSKVFRTRFQMLIEAQLDLLKNDDWDHLLEYEVDAVFEEKE
Protein: Major prion protein (PrP) (PrP27-30) (PrP33-35C) (CD antigen CD230) (P04925)
Organism: Mus musculus (Mouse)
Function: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:9837873}; Lipid-anchor, GPI-anchor. Golgi apparatus {ECO:0000269|PubMed:11756421}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to. vesicles in para- and perinuclear regions, where both proteins undergo internalization. Heparin displaces PRNP from lipid rafts and promotes endocytosis. {ECO:0000269|PubMed:11571277, ECO:0000269|PubMed:12732622, ECO:0000269|PubMed:16923158, ECO:0000269|PubMed:9837873}.
Interaction partners:
- Neural cell adhesion molecule 1
- Stress-induced-phosphoprotein 1
- Amyloid-beta precursor protein
- Tyrosine-protein kinase Fyn
- Caveolin-1
- Neural cell adhesion molecule 2
- Alpha-synuclein
- Endoplasmic reticulum chaperone BiP
- Glycogen synthase kinase-3 beta
- Casein kinase II subunit alpha'
Sequence:
MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAMSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG
Protein: Reaction center protein M chain (Photosynthetic reaction center M subunit) (A8ASG6)
Organism: Thermochromatium tepidum (Chromatium tepidum)
Subcellular location: Cellular chromatophore membrane {ECO:0000256|RuleBase:RU364137}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU364137}. Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MPEYQNIFTAVQVRAPAYPGVPLPKGNLPRIGRPIFSYWLGKIGDAQIGPIYLGLTGTLSIFFGLVAISIIGFNMLASVHWDVFQFLKHFFWLGLEPPPPQYGLRIPPLSEGGWWLMAGLFLTLSILLWWVRTYKRAEALGMSQHLSWAFAAAIFFYLVLGFIRPVMMGSWAKAVPFGIFPHLDWTAAFSIRYGNLYYNPFHMLSIAFLYGSALLFAMHGATILSVSRFGGDREIDQITHRGTAAERAALFWRWTMGFNVTMESIHRWAWWCAVLTVITAGIGILLSGTVVDNWYLWAVKHGMAPAYPEVVTAVNPYETAAEVMQ
Protein: UBE2S protein (Q6NXQ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNSNVENLPPHIIRLVYKEVTTLTADPPDGIKVFPNEEDLTDLQVTIEGPEGTPYAGGLFRMKLLLGKDFPASPPKGYFLTKIFHLNVGANGEICVNVLKRDWTAELGIRHVLLTIRCLLIHPNPESALNEEAGRLLLENSEEYAARARLLTEIHGGAGGPSGRAEAGRALASGTAASSTDPGAPGGLGGAEGPMAKKHAGERDKKLAAKKKTDKKRALRRL
Protein: Armadillo repeat-containing protein 8 (B7Z637)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKNAVIGNNKQKANLIVLGAVPRLLYLLQQETSSTELKTECAVVLGSLAMGTENNVKSLLDCHIIPALLQGLLSPDLKFIEACLRCLRTIFTSPVTPEELLYTGPDHQTILFNHGAVQNIAHLLTSLSYKVRMQALKCFSVLAFENPQVSMTLVNVLVDGELLPQIFVKMLQRDKPIEMQLTSAKCLTYMCRAGAIRTDDNCIVLKTLPCLVRMCSKERLLEERVEGAETLAYLIEPDVELQRIASITDHLIAMLADYFKYPSSVSAITDIKRLDHDLKHAHELRQAAFKLYASLGANDEDIRKKIIETENMMDRIVTGLSESSVKVRLAAVRCLHSLSRSVQQLRTSFQDHAVWKPLMKVLQNAPDEILVVASSMLCNLLLEFSPSKEPILESGAVELLCGLTQSENPALRVNGIWALMNMAFQAEQKIKADILRSLSTEQLFRLLSDSDLNVLMKTLGLLRNLLSTRPHIDKIMSTHGKQIMQAVTLILEGEHNIEVKEQTLCILANIADGTTAKDLIMTNDDILQKIKYYMGHSHVKLQLAAMFCISNLIWNEEEGSQERQDKLRDMGIVDILHKLSQSPDSNLCDKAKMALQQYLA
Protein: Disintegrin and metalloproteinase domain-containing protein 22 (ADAM 22) (Metalloproteinase-disintegrin ADAM22-3) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 2) (Q9P0K1)
Organism: Homo sapiens (Human)
Function: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27066583}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q9R1V6}.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Disks large homolog 4
- Disintegrin and metalloproteinase domain-containing protein 23
- Leucine-rich repeat LGI family member 4
- Voltage-dependent calcium channel gamma-2 subunit
- Leucine-rich repeat LGI family member 3
- Disks large homolog 2
- Leucine-rich repeat LGI family member 2
- Disintegrin and metalloproteinase domain-containing protein 28
- Contactin-associated protein-like 2
Sequence:
MQAAVAVSVPFLLLCVLGTCPPARCGQAGDASLMELEKRKENRFVERQSIVPLRLIYRSGGEDESRHDALDTRVRGDLGGPQLTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVKGGEHCYYQGHIRGNPDSFVALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVYKSRLFEFSLDDLPSEFQQVNITPSKFILKPRPKRSKRQLRRYPRNVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAECCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCNTYFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDIPPGVSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNLGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEDKKVNRQSARLWETSI
Protein: Ookinete maturation protein 1 (A0A509AIR7)
Organism: Plasmodium berghei (strain Anka)
Function: In the mosquito vector midgut, plays a role in ookinete development.
Interaction partners:
Sequence:
MNRTHMPNNHKIHEGINMKSSINEVKKSKRIEKELSYVTNSTKKKSKKKQTNIKKIGDVSVNIENINIPNNLNLYTDNESVVSSKYKKKKKKKKKLNIYNNNDNSKYLKPQVVKKKNSKIIFLHHNENNTSTHSGESSKFQKLKKKKKIKKGTKKKSINKISILKHKSHESFPSTQNENTPELEPKQVNLSPLEIEINKTNDIDKHGLEINKTPSTQNFNDPINNLDNNEKIKDRGLFHGIDNIYENYITNDKENMQSVIKNRHYIIDKNEQNEQAYNNDMNITNFIKNGNTNKNSNNDKSANSNDYNKNLFCELTEAIENDGIEQTCNRNINIRLKEEKEAEEEERKKNEDEHILENGKSNNEDNSFDKKDDLTNLGKSFKNNESFELNSPQKNIRKGSLDGMRKKKISEKKMKTKIKQKKKRQNNINDTTIGKKKIYIKENNNERKSSGLILGFKKMKKKLSGKRIDQKKEYKEKEIYSDKLKDVIKDKKKYKKKDIDDISFTKDIVKENVKGVDRDDDEKKRKTIGQDEEKEKIEIIIVKKNETGTEEEIKVETDENPKVKTKEKCKIENGEGCKIAIDEENSVFVEAENMKNEAKLEADVIIIEDAELRKDEEEDKSKNNEKDSKSEERDILETQMAGKEEKPVLKKKKKNKGKQRNREGKGVVEKGYDAKREKKENEEKNKANTKMEPNDSIEQKDKLSNVQNMSNIVKNNKVNKILEKYIISKKEENLKRKYMNTKKFMDILDISEKKFKIDTINFFPHTIGQVCYSDIYFFFDTYEKELKKSNTGKNTIKLMKKLFKCEYIEMNNMELILQIFDKIIDKLKKELKTESIVKIYDEEEHVIASKIMKYKNGNYDKYMYNKKKYDSNNEYSISENNLFNQNPLHHQNNLFGCNRNKLYNIIFNSSQGEYIMGSHSFLILQQWNDEYKLAMLRDKLEQIKKRKQNMNDPIAKYIKSLKYGFIDSLFSICCLYDCKKNDNDASYCDFPLPSQNTFYTNTQIHLDNMNLNSERILPMKITKAVQILASS
Protein: Chromobox homolog 4 (Pc class homolog, Drosophila), isoform CRA_a (Chromobox-like protein 4 isoform 2) (A0A0S2Z5B2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELPAVGEHVFAVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRERQEQLMGYRKRGPKPKPLVVQVPTFARRSNVLTGLQDSSTDNRAKLDLGAQGKGQGHQYELNSKKHHQYQPHSKERAGKPPPPGKSGKYYYQLNSKKHHPYQPDPKMYDLQYQGGHKEAPSPTCPDLGAKSHPPDKWAQGAGAKGYLGAVKPLAGAAGAPGKGSEKGPPNGMMPAPKEAVTGNGIGGKMKIVKNKNKNGRIVIVMSKYMENGMQAVKIKSGEVAEGEARSPSHKKRAADERHPPADRTFKKAAGAEEKKVEAPPKRREEEVSGVSDPQPQDAGSRKLSPTKEAFGEQPLQLTTKPDLLAWDPARNTHPPSHHPHPHPHHHHHHHHHHHHAVGLNLSHVRKRCLSETHGEREPCKKRLTARSISTPTCLGGSPAAERPADLPPAAALPQPEVILLDSDLDEPIDLRCVKTRSEAGEPPSSLQVKPETPASAAVAVAAAAAPTTTAEKPPAEAQDEPAESLSEFKPFFGNIIITDVTANCLTVTFKEYVTV
Protein: Uncharacterized protein C1604.16c (O94728)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MENKGNMELSNSYGFYKNGRRVSFVKATSEQSLDEATFIEKGSAQAFYHSLFENDRDNSHTMNSKRDEAGFACEVCQIYIPNSKKINHFKSMTHLLSSQHISNKFQPHLLKPKSLGYRVLSQYGWSPQGDTAGLGLENQGRRAPVRAFRVKNDTIGLGTKIDLEKVAVNKCRKGKRQCQIQHSKDVRLKEALIKHFSSN
Protein: At2g04280 (Calcium ion-binding protein) (Expressed protein) (Q9SI07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ribonuclease E/G-like protein, chloroplastic
- Chloroplastic group IIA intron splicing facilitator CRS1, chloroplastic
- Polyribonucleotide nucleotidyltransferase 1, chloroplastic
Sequence:
MFGRSAIRGGGFRAENLGQNALTLIGNIGFSLFVFGVLIFTIIAATYEPEDPLFHPSDKITTFLTSTSNATLRSDDSVVKTGEDFMLANQTAFAEFININDVEASTNETTTEEEGNKLECDVNTPIDCKDQQVFHLMMRATIDKFKDIHFYKFGKPVTGEEGVNSCDMAWRYRPRDGKSAAFYKDYRRFVVAKSENCSVSVVGIGEYHSGLNARKRKKNQKAGFEKTGGKKDDFSLPVVGELVNDSLPMVESDSVFKTGKYLVYVGGGDRCKSMNHFLWSFLCALGEAQYLNRTLVMDLTLCLSSIYTSSGQNEEGKDFRFYFDFEHLKEAASVLDEAQFWAQWGKLRKKRRNRLNLHLVEDFRVTPMKLAAVKDTLIMRKFGSVEPDNYWYRVCEGDAESVVKRPWHLLWKSRRLMEIVSAIASRLNWDYDAVHIERGEKARNKEVWPNLEADTSPSALLSTLQDKVEEGRHLYIATNEGELSFFNPLKDKYATHFLYDYKDLWDESSEWYSETTKLNGGNPVEFDGYMRASVDTEVFLRGKKQIETFNDLTNDCKDGVGTCNAATS
Protein: Putative ATP synthase subunit g 2, mitochondrial (ATPase subunit g 2) (ATP synthase membrane subunit g-like protein) (Q7Z4Y8)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000250}.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
Sequence:
MAPFVRNLVEKTPALVNAAVTYLKPRLAAFWYYTTVELVPPTPAEIPRAIQSLKKIVSSAQTGSFKQLTVKEALLNGLVATEVSTWFYVREITGKRGIIG
Protein: Secreted frizzled-related protein 1 (FRP-1) (sFRP-1) (Secreted apoptosis-related protein 2) (SARP-2) (Q8N474)
Organism: Homo sapiens (Human)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription.
Subcellular location: Secreted. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding.
Interaction partners:
- Proto-oncogene Wnt-1
- Protein Wnt-7b
- Protein Wnt-5a
- Protein Wnt-3a
- Protein Wnt-4
- Protein Wnt-8b
- Frizzled-2
- Protein Wnt-7a
- Protein Wnt-2
- Tumor necrosis factor ligand superfamily member 11
Sequence:
MGIGRSEGGRRGAALGVLLALGAALLAVGSASEYDYVSFQSDIGPYQSGRFYTKPPQCVDIPADLRLCHNVGYKKMVLPNLLEHETMAEVKQQASSWVPLLNKNCHAGTQVFLCSLFAPVCLDRPIYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGDVCIAMTPPNATEASKPQGTTVCPPCDNELKSEAIIEHLCASEFALRMKIKEVKKENGDKKIVPKKKKPLKLGPIKKKDLKKLVLYLKNGADCPCHQLDNLSHHFLIMGRKVKSQYLLTAIHKWDKKNKEFKNFMKKMKNHECPTFQSVFK
Protein: LP02983p (Q8MS96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MITSCYVRDVTKHRELLQQDAISFIEDRLPKEKVKDFVKDESEVHKPSVLIMGLDSTSRINLRRAMPSVYKFVRQPGWFEMQGYNKVGDNTFPNLLAALTGDSEKGVGDYCDVTKPGCLDSLNFIWKRFKKANYTTAFAEDCSSISTFNYLKPGFVKQPTDYYLRPLLFAIEKQFKVTNDFGFAYCVGRHLSFSYVWDFGQQFIDRFLGRSPMFGFLWSNSFTHDYYEGATALDNLLWKYLKSFEESNLFQKSIVILMSDHGHRYNTLRRASTGYFEERMPMMFIYLPPWFRRKYPHLASNLGKNQNRLSSNYDVYMTLQHLLQLDSKSVDEFPDNLRARQCKSCQSLFFELPFNRTCQMAGIEEKWCCCQPTETITNSPHVSTIAEAIVQRMNEHLISHNLSDLCHNFTLDYVEKADRKTILSNGLRPADKNEQVYIIVFETVPKNPIFEATVRWNSRTQRLLHFDVEELSRLTSYKNDANCINRKNAKKYCICKDSLSRPS
Protein: Sp4 transcription factor (A0A8I6B4P2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFRRRGGEKGGERIIIILITYQKKEEEEEAAAAMATEGGKTSEPENNNKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPPASKENNVSQPASSSSSSSSSNNGSSSPTKTKSGNPSTPNQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINIGGVTLALPVINNVTAGGGTGQVGQPTTTTTDSGTSNGNQLVSTPTTSTAPASTMPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSSERTIEEPQTPAATESEAQSSSQLQSNGIQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDAEVQPGKRLRRVACSCPNCREGEGRGSSEPGKKKQHVCHIEGCGKVYGKTSHLRAHLRWHTGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECPECSKRFMRSDHLSKHVKTHQNKKGGGTALAIVTSGELDSSVTEVLGSPRIVTVAAISQDSNPATPNVSTNMEEF
Protein: ERAD-associated E3 ubiquitin-protein ligase HRD1B (AtHrd1B) (EC 2.3.2.27) (RING-type E3 ubiquitin transferase HRD1B) (Q6NPT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD). Targets the misfolded LRR receptor kinase BRI1. Functions redundantly with HRD3A.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein OS-9 homolog
- ERAD-associated E3 ubiquitin-protein ligase component HRD3A
- Derlin-1
- Derlin-2.1
- Ubiquitin-conjugating enzyme E2 32
- Cell division control protein 48 homolog A
- Derlin-2.2
- ERAD-associated E3 ubiquitin-protein ligase HRD1A
- Peptide-N
- ERAD-associated E3 ubiquitin-protein ligase component HRD3B
Sequence:
MIQLKVYAGLSTLATLVVIYHAFSSRGQFYPATVYLSTSKINLVVLLNMGLVLMLSLWNLVKIVFLGSLREAEVERLNEQAWRELMEILFAITIFRQDFSVGFISLVVTLLLIKGLHWMAQKRVEYIETTPSVTLLSHVRIVSFMVFLLILDCLLTYSSIQQLIQSRKASMSVFFTFEYMILATTTVSIIVKYAFYVTDMLKEGQWEGKPVYTFYLELVRDLLHLSMYLCFFLMIFMNYGLPLHLIRELYETFRNFKIRVTDYLRYRKITSNMNDRFPDATPEELSSNDATCIICREEMTSAKKLVCGHLFHVHCLRSWLERQNTCPTCRALVVPAENATSTASGNRGPHQESLQQGTGTSSSDGQGSSVSAAASENMSRHEARFQAAASAASIYGRSIVYPSSANTLVWSQGNSLLPQTEVEAQRRFLESQIEVLTNQLRLLEKPTTVDTKGKSVADTA