wanglab/gogpt-training-data huggingface dataset:
Protein: Arginine ADP-riboxanase OspC3 (EC 4.3.99.-) (A0A2H5DV25)
Organism: Chromobacterium sp. (strain ATCC 53434 / SC 14030)
Function: ADP-riboxanase effector that inhibits host cell pyroptosis. Acts by mediating arginine ADP-riboxanation of host CASP4/CASP11, blocking CASP4/CASP11 autoprocessing. This prevents CASP4 activation and ability to recognize and cleave GSDMD, thereby inhibiting LPS-induced pyroptosis (By similarity). ADP-riboxanation takes place in two steps: OspC3 first catalyzes ADP-ribosylation of target Arg, and then initiates a deamination to remove one N-omega group (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:A0A0H2US87}. Host cytoplasm {ECO:0000250|UniProtKB:A0A0H2US87}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:A0A0H2US87}.
Interaction partners:
Sequence:
MRVETHSPSFTNPNPAEACSGDPTEMGSRLSGVSRAPLPHAAAGRDGEAAAAGKIGAFLRKAVAAQSYGLMFANGKLFEATGDALEKREQYGFSALKRLDGLSRRNLDAVAARLGALDSAEQALKQHIMAGAWHFRHQSNAALDDGEKATIASNHLLSRQARSSGGNTFADDKALLSNHDFVFFGVEFSGRDKNDKPLNHKHSTMDFGANAYVVSDALPACRNGYLTLTDHFFNRVPGGREAEHQDFVGRFAQMGRESGRWIHEGKYRQNAPLFCYRDMKAAVALHLIEFMRNSQDEAFKAYVFDQATQSGPALDRVLNSVFQAEFHIPRLMATTDYAKHPLRPMLLKEAVDSVNLPALSDLVSNRGDAVTAMWHAINKGKDEVVAYLLGNWQFEAKDFSHAPAGFYHELNYALSESGASVYILDQFLSRGWAAVNAPFEHVNRGDTMLDNAVKYGNREMVAALIKHGADRNLLSKWHKSDLDALLA
Protein: SIN3 transcription regulator family member A (A0A0G2K3H5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
- Sin3A associated protein 30
- Histone deacetylase 1
- Methyl-CpG-binding protein 2
- Histone deacetylase 2
- Nuclear receptor corepressor 1
- Histone deacetylase 1
- SDS3 homolog, SIN3A corepressor complex component
- Nuclear receptor corepressor 2
- Inhibitor of growth protein.
- RE1-silencing transcription factor
Sequence:
MKRRLDDQESPVYAAQQRRIPGSTEAFSHQHRVLAPAPPVYEAVSETMQSATGIQYSVAPNYQVSAVPQSSGSHGPAIAAVHSSHHHPAAVQPHGGQVVQSHAHPAPSVAPVQGQQQFQRLKVEDALSYLDQVKLQFGSQPQVYNDFLDIMKEFKSQSIDTPGVISRVSQLFKGHPDLIMGFNTFLPPGYKIEVQTNDMVNVTTPGQVHQIPTHGIQPQPQPPPQHPSQPSAQSAPTPAQPAPQPTPAKVSKPSQLQAHTPASQQTPPLPPYASPRSPPVQPHTPVTISLGTAPSLQNNQPVEFNHAINYVNKIKNRFQGQPDIYKAFLEILHTYQKEQRNAKEAGGNYTPALTEQEVYAQVARLFKNQEDLLSEFGQFLPDANSSVLLSKTTAEKVDSVRNDHGGTVKKPQLNNKPQRPSQNGCQIRRHSGTGATPPVKKKPKLISLKESSMADASKHGVGTESLFFDKVRKALRSAEAYENFLRCLVIFNQEVISRAELVQLVSPFLGKFPELFNWFKNFLGYKESVHLESFPKERATEGIAMEIDYASCKRLGSSYRALPKSYQQPKCTGRTPLCKEVSSLLCSGVRPDHLLLLFFCFKLDVVLETNLATIRVLEAIQKKLSRLSAEEQAKFRLDNTLGGTSEVIHRKALQRIYADKAADIIDGLRKNPSIAVPIVLKRLKMKEEEWREAQRGFNKVWREQNEKYYLKSLDHQGINFKQNDTKVLRSKSLLNEIESIYDERQEQATEENAGVPVGPHLSLAYEDKQILEDAAALIIHHVKRQTGIQKEDKYKIKQIMHHFIPDLLFAQRGDLSDVEEEEEEEMDVDEATGAPKKHNGVGGSPPKSKLLFSNTAAQKLRGMDEVYNLFYVNNNWYIFMRLHQILCLRLLRICSQAERQIEEENREREWEREVLGIKRDKSDSPAIQLRLKEPMDVDVEDYYPAFLDMVRSLLDGNIDSSQYEDSLREMFTIHAYIAFTMDKLIQSIVRQLQHIVSDEVCVQVTDLYLAENNNGATGGQLSSQTSRSLLESTYQRKAEQLMSDENCFKLMFIQSQGQVQLTIELLDTEEENSDDPVEAERWSDYVERYMSSDTTSPELREHLAQKPVFLPRNLRRIRKCQRGREQQEKEGKEGNSKKTMENVESLDKLECRFKLNSYKMVYVIKSEDYMYRRTALLRAHQSHERVSKRLHQRFQAWVDKWTKEHVPREMAAETSKWLMGEGLEGLVPCTTTCDTETLHFVSIKKYRVKYGTVFKAP
Protein: Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform (EC 2.7.11.19) (Phosphorylase kinase subunit gamma-1) (Serine/threonine-protein kinase PHKG1) (EC 2.7.11.1, EC 2.7.11.26) (P07934)
Organism: Mus musculus (Mouse)
Function: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity).
Interaction partners:
- Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
- Phosphorylase b kinase regulatory subunit beta
- Phosphorylase b kinase regulatory subunit alpha, liver isoform
- Calmodulin-1
- Calmodulin 5
- Calmodulin-like protein 3
- Calmodulin-4
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Calmodulin-like protein 4
- Glycogen phosphorylase, muscle form
Sequence:
MTRDDALPDSHSAQTFYENYEPKEILGRGVSSVVRRCIHKPTCQEYAVKIIDITGGGSFSSEEVQELREATLKEVDILQKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLTEKETRKIMRALLEVICTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLQPGEKLREVCGTPSYLAPEIIQCSMDDGHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMDGKYQFGSPEWDDYSDTVKDLVSRFLVVQPQDRCSAEEALAHPFFQEYVVEEVRHFSPRGKFKVICLTVLASVKIYYQYRRVKPVTREIVIRDPYALRPLRRLIDAYAFRIYGHWVKKGQQQNRAALFENTPKAVLLSLAEEEDF
Protein: Probable chlorophyll(ide) b reductase NYC1, chloroplastic (EC 1.1.1.294) (Protein NON-YELLOW COLORING 1) (AtNYC1) (Q93ZA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in chlorophyll b degradation. Belongs to the chlorophyll catabolic enzymes (CCEs).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 7-hydroxymethyl chlorophyll a reductase, chloroplastic
- Chlorophyllide a oxygenase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Chlorophyllase-2
- Chlorophyllase-1
- Pheophorbide a oxygenase, chloroplastic
- Chlorophyll
- Magnesium dechelatase SGR1, chloroplastic
- Pheophytinase, chloroplastic
- Red chlorophyll catabolite reductase, chloroplastic
Sequence:
MTTLTKIQVYPQVLEHRLFFRDPIRVGSRLTCRERSNRVYVHRCEKKVERKRKVEKFKGNGSWDSLKSGFLGFSKLGFLSKDEYNQKVENLEMVFSSVAVQIARYIVTMTSTGAILLIGFQLSGGDSSMNSLVWYSWLGGIIIGTMTGANMVLEDHYRAGPRNVVITGSTRGLGKALAREFLLSGDRVIVTSRSSESVDMTVKELEQNLKEIMSNASESARKKLSDAKVVGIACDVCKPEDVEKLSNFAVKELGSINIWINNAGTNKGFRPLLEFTEEDITQIVSTNLIGSILCTRGAMDVMSRQHSGGHIFNMDGAGSGGSSTPLTAVYGSTKCGLRQFHGSIVKESQKTNVGLHTASPGMVLTELLLSGSSIKNKQMFNIICELPETVARTLVPRMRVVKGSGKAVNYLTPPRILLAIVTSWLRRGRWFDDQGRALYAAEADRLRNWAENRTRLSLTDAMEMYTENTWVSVFSLSVVCAFIILQSTTPSSFPGT
Protein: Calcipressin-3 (Down syndrome candidate region 1-like protein 2) (Myocyte-enriched calcineurin-interacting protein 3) (MCIP3) (Regulator of calcineurin 3) (Q9UKA8)
Organism: Homo sapiens (Human)
Function: Inhibits calcineurin-dependent transcriptional responses by binding to the catalytic domain of calcineurin A. Could play a role during central nervous system development (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Calcineurin subunit B type 1
- Troponin I, cardiac muscle
Sequence:
MLRDTMKSWNDSQSDLCSTDQEEEEEMIFGENEDDLDEMMDLSDLPTSLFACSVHEAVFEAREQKERFEALFTIYDDQVTFQLFKSFRRVRINFSKPEAAARARIELHETDFNGQKLKLYFAQVQMSGEVRDKSYLLPPQPVKQFLISPPASPPVGWKQSEDAMPVINYDLLCAVSKLGPGEKYELHAGTESTPSVVVHVCESETEEEEETKNPKQKIAQTRRPDPPTAALNEPQTFDCAL
Protein: Methyl-accepting chemotaxis protein CtpM (Q9I0I6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation (Probable). Directly recognizes five C4-dicarboxylic acids: L-malic, citramalic, citraconic, bromosuccinic and methylsuccinic acids. Three of the identified ligands act as chemoattractants (L-malic, D,L-bromosuccinic and L-citramalic acids) whereas two of them (L-methylsuccinic and citraconic acids) behave as antagonists by inhibiting the downstream chemotaxis signaling cascade. Antagonists compete with chemoattractants, thereby decreasing the affinity for chemoattractants and the subsequent chemotactic response. Acts through the che chemosensory pathway.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chemotaxis protein CheA
- Chemotaxis protein CheA
- Probable purine-binding chemotaxis protein
- Chemotaxis protein methyltransferase 1
- Probable chemoreceptor glutamine deamidase CheD
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
- Chemotaxis protein CheW
- Chemotaxis protein methyltransferase 2
- Protein-glutamate methylesterase/protein-glutamine glutaminase 2
- Probable chemotaxis protein
Sequence:
MMRLTLKSKVLLLAMVPVLLFALVLSGGAVLILKKQADAEVKDTRERLLGDRRAELEHYVQIAMGSIQAEYDRSANGDLNARAEAIARLSKIKYGKDGYIFGYDSQVVRLFRGDSPVDVGKSFRDRRDPSGVYLNRELVEAGRNGSHYVTYTSPLPGNESVMVPKLSYTLYLPKWDMVIGSAINLDGVEAQLVEIKQDIDERIGTLIASIVGIAGVLLVVLLVIGLAVANAMLRPLHQIRQNLDDIAAGEGDLTRRLPVTSYDELGELAGSFNRFVEKIHGLVRQIAGMTGDLKQLVEQMSAQAERSEQAMERQRHETDQVATAINEMSAAAHEVAQSAQRAAEAAQQTDHEGQAAKRVVDGSIERIHALVDEIRDSGTSLDSLQQDVQSIVSVLGVIRSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRALASRTQQSTQEIQGMIDRLQQGTNAAVDAMRRSGEAGEGTSNQANQAGDSLDAIAQLIATINAMNAQIASAAEEQTAVAEEINRSVHQIAGAVDSVADEAQQGAQTARSLAQLGQGLGRLVGQFRI
Protein: FK506-binding protein 1 (FKBP) (EC 5.2.1.8) (Peptidyl-prolyl cis-trans isomerase) (PPIase) (Rapamycin-binding protein) (O94746)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MGVTVENISAGDGKTFPQPGDNVTIHYVGTLLDGSKFDSSRDRGTPFVCRIGQGQVIRGWDEGVPQLSVGQKANLICTPDYAYGARGFPPVIPPNSTLKFEVELLKVN
Protein: Encapsulated ferritin-like protein (EncFtn) (EC 1.16.3.1) (Q2RVS1)
Organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
Function: Cargo protein of a type 1 encapsulin nanocompartment. A ferritin-like ferroxidase that mineralizes iron inside the encapsulin nanocompartment. Converts Fe(2+) to Fe(3+) that is released to the exterior of the decameric complex for deposition in the encapsulin nanocompartment. In solution the decamer binds 10-15 iron cations; in the encapsulin nanocompartment the decamer can bind up to 48 ions, perhaps via its internal channel and on its exterior. The empty encapsulin nanocompartment sequesters about 2200 Fe ions while the cargo-loaded nanocompartment can maximally sequester about 4150 Fe ions. EncFtn retains ferroxidase activity when encapsulated. Flux in the active site di-iron metal center is thought to be controlled by the 'entry site' of the protein, which both attracts metal and controls the rate of iron oxidation (Probable). Encapsulation in the nanocompartment does not alter either function of this protein.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:27529188}.
Interaction partners:
- Type 1 encapsulin shell protein
Sequence:
MAQSSNSTHEPLEVLKEETVNRHRAIVSVMEELEAVDWYDQRVDASTDPELTAILAHNRDEEKEHAAMTLEWLRRNDAKWAEHLRTYLFTEGPITAIEAADTAGEGSGGDAAKGATAQGDGSLGIGSLKGEAALARPPRL
Protein: Matrix metalloproteinase 1, isoform I (EC 3.4.24.-) (Matrix metalloproteinase 1, isoform K) (A0A0B4JD53)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTNCQSSVFIVVGTLFSIMAAAQSAPVSTTTQAEIYLSQFGYLPASARNPASSGLHDQRTWVSAIEEFQSFAGLNITGELDAETMKLMSLPRCGVRDRVGTGDSRSKRYALQGSRWRVKNLTYKISKYPKRLKRVDVDAEIGRAFAVWSEDTDLTFTRKTSGPVHIEIKFVESEHGDGDAFDGQGGTLAHAFFPVFGGDAHFDDAELWTIGSPRGTNLFQVAAHEFGHSLGLSHSDQSSALMAPFYRGFEPVFKLDEDDKAAIQSLYGRKTNQLRPTNVYPATTQRPYSPPKVPLDDSICKDSKVDTLFNSAQGETYAFKGDKYYKLTTDSVEEGYPQLISKGWPGLPGNIDAAFTYKNGKTYFFKGTQYWRYQGRQMDGVYPKEISEGFTGIPDHLDAAMVWGGNGKIYFFKGSKFWRFDPAKRPPVKASYPKPISNWEGVPNNLDAALKYTNGYTYFFKGDKYYRFHDARFAVDSATPPFPRPTAHWWFGCKNTPSSTAPQVPSLNPNPNQGILPSWMWGLTNRFF
Protein: Pentatricopeptide repeat-containing protein At1g06270 (Q9LNC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g09190
- Pentatricopeptide repeat-containing protein At2g37320
- Pentatricopeptide repeat-containing protein At4g21170
- CRS2-associated factor 1
- Pentatricopeptide repeat-containing protein At2g37310
- Tetratricopeptide repeat
- Pentatricopeptide repeat-containing protein At2g28050
- Ribosomal protein L1p/L10e family
- Pentatricopeptide repeat-containing protein At4g02750
- Small ribosomal subunit protein mS79
Sequence:
MAIRLTHLRKPLAYSRSFDVCIPFFRSISSFEAVEKAIKCAVETKEYLRIPELVVSLKEPYQNSTLFSFLSAFQRHHRIRVIDEILQSFVPVRPRSLPKIVYSSLLTYCLQSSDPLPLSFAILQRTLRSGCLPNPQTHLLLSDAWLERRRGSQSVADIINEMKLIGYSPDTGTCNYLVSSLCAVDKLDEAIKVVEEMSAAGCIPDVESYGAVINSLCLARKTTDVVKIVKEMVSKAGISPRKGMLTKVAAALRANREIWKAIEMIEFVESRDYPVEFESYEVVVEGCLEVREYILAGKVVMRMTDRGFIPYIKVRQKVVERLINIGEWKLACTVRQRVSELRS
Protein: Uncharacterized alpha-1,2-galactosyltransferase C1289.13c (EC 2.4.1.-) (O94622)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C5H10.12c
- Uncharacterized protein C4C3.09
- Meiotically up-regulated gene 136 protein
- Uncharacterized protein C1198.03c
Sequence:
MRWYSYVIPAVILSIIAISGVWWNATLGTRLDQKVQLFLNEHSSILNAVYETTTIVYTEPLHTSVSETITSTSFVTETTTVTPTVTATAQELSTLNPHPENSKIVLLMGSNAQNDPSSPLNPYIRTIIKNRRDYAERHGFKFEFLDLDEYKPSIGDKPAPWAKIPMIKNVIRKYPDAEWVWWLDHDALIMNRDLNLVDHILKHEKLNSLLLRDTEYFSGFGIDSEGFRTPKNQDPDDIHFIIAQDFNGINAGSFLIRNSEVGTWMLDFWNEPLYKEHNGVFVEQQALSHMIYSHPIVHKHVGLVTLRSINAYDSSDPAWGYEDGDLCVHFAGCFVFQTCAQNFEKYGKIITEKQGHDWFDPSEKEYIEQRLFPQP
Protein: Tectonic-1 (Q2MV58)
Organism: Homo sapiens (Human)
Function: Component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Regulator of Hedgehog (Hh), required for both activation and inhibition of the Hh pathway in the patterning of the neural tube. During neural tube development, it is required for formation of the most ventral cell types and for full Hh pathway activation. Functions in Hh signal transduction to fully activate the pathway in the presence of high Hh levels and to repress the pathway in the absence of Hh signals. Modulates Hh signal transduction downstream of SMO and RAB23 (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Secreted {ECO:0000305}. Note=Despite the presence of a signal sequence, the full-length protein might not be secreted. Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250}.
Interaction partners:
- B9 domain-containing protein 1
- Coiled-coil and C2 domain-containing protein 2A
- Tectonic-2
- B9 domain-containing protein 2
- Tectonic-like complex member MKS1
- Tectonic-3
- Transmembrane protein 216
- Transmembrane protein 231
- Meckelin
- Centrosomal protein of 290 kDa
Sequence:
MRPRGLPPLLVVLLGCWASVSAQTDATPAVTTEGLNSTEAALATFGTFPSTRPPGTPRAPGPSSGPRPTPVTDVAVLCVCDLSPAQCDINCCCDPDCSSVDFSVFSACSVPVVTGDSQFCSQKAVIYSLNFTANPPQRVFELVDQINPSIFCIHITNYKPALSFINPEVPDENNFDTLMKTSDGFTLNAESYVSFTTKLDIPTAAKYEYGVPLQTSDSFLRFPSSLTSSLCTDNNPAAFLVNQAVKCTRKINLEQCEEIEALSMAFYSSPEILRVPDSRKKVPITVQSIVIQSLNKTLTRREDTDVLQPTLVNAGHFSLCVNVVLEVKYSLTYTDAGEVTKADLSFVLGTVSSVVVPLQQKFEIHFLQENTQPVPLSGNPGYVVGLPLAAGFQPHKGSGIIQTTNRYGQLTILHSTTEQDCLALEGVRTPVLFGYTMQSGCKLRLTGALPCQLVAQKVKSLLWGQGFPDYVAPFGNSQAQDMLDWVPIHFITQSFNRKDSCQLPGALVIEVKWTKYGSLLNPQAKIVNVTANLISSSFPEANSGNERTILISTAVTFVDVSAPAEAGFRAPPAINARLPFNFFFPFV
Protein: Serine incorporator 5 (Axotomy-induced glycoprotein 3) (AIGP-3) (Q8BHJ6)
Organism: Mus musculus (Mouse)
Function: Restriction factor required to restrict infectivity of gammaretroviruses: acts by inhibiting early step of viral infection and impairing the ability of the viral particle to translocate its content to the cytoplasm (By similarity). Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q86VE9}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell membrane, where it is efficiently incorporated into budding gammaretrovirus virions and impairs subsequent virion penetration of susceptible target cells. {ECO:0000250|UniProtKB:Q86VE9}.
Interaction partners:
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
Sequence:
MSARCCAGQLACCCGSAGCSLCCGCCPKFRQSRTTRFMYLFYFILVIALCCVMMTPSVMKQVKDHIPFFEEFCKKTQAGGDACENLVGYSAVYRVCFGMACFFALFCLLTLKVNNSKSCRAYIHNGFWFFKLLLLGAMCSGAFFIPDQETFLKVWRYVGAGGSFLFICIQLLLIVQFAHKWNKNWTAGTVRNKLWYASLSLVTLIMYSVAVGGLALMAVFYTQWDDCMDNKILLGVHGGLCVLISLVAISPCVQNRQPHSGLLQSGLISCYVTYLTFSALTSKPEKKVLDEHGKNVTICAPDFGQDLHRDENMVTWLGTLLLIVCISYSCLTSTTRSSSDALQSRYGAPELEVARCCFCFGPDGEDTEEQQNVKKGPRVIYDEKKGTVYSYSYFHFVFFLASLYVMMTLTSWFHYENATIKTFFSGWSVFWVKMASCWMCVLLYLQTLVAPLCCPSRQFSV
Protein: Pentacotripeptide-repeat region of PRORP domain-containing protein (Q384U4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- REH2-associated factor 1
- RNA editing associated helicase 2
Sequence:
MTSSVTGPPSSFAAAAKVLFDSAKKVGAVKPLGTTSKLYAHQLKKIQSQSRKKGGSLGNVSYNVAEFLEAHRASQVKSSQGPIFHTRCVPLIDIPLKKTKQTGSGMQKTSSNEAPLLNLHKRQPHLAATPDMSKEAVPVGGVAGVGPQVPKLAPPKLDSVLLPKDGEAKRQPWVHHTDTHAADRTSATGGVFLAPERILHGVAPRATVVEEKPLFESPCVTEAKPLSFLDLKARQPMKEVVEVVDRPIKPSVTVPISSGGSSAASTRGGENARTETISVDVWELQRERELEQLRKDQEKAEKERLEARREEEHKTLGDEWVLSRTLATSRPLCVGAVNGALEKLYFSSDWETCFQLFKELVCAPTPPVPSVSKQAVCLMERHLRRVPGARRNELKVALSKELKERKLLDEATRFDLKHTYSEAFLQVYRSASSSVKDSLDLCTTAKAISTLVRSGSWLEAVEVFHRSQQRFSDKGGRLGLGLLAESRSLDGEARTALSEYTSKTLTAQGRFGKLHSIELVKLSKGGQKRHLLSQLIESGHVDEVIYAELLRTTKENVEDVLEEIGKRGLNVEDPAILAALCWRSFDVESPQVLFREIERQEAKIGIRPAHVLAAVAMARASKSEHTLRSTIQILKKKPNFRCKFVLRKLLPLLYERRMNSEIVELAEIYASNLPIAVALPQAVGFINSALIAQGKNPLSTHLASDLNLSGKAVVGDTGDATQLTIPRAPESVASTEAMFQCVKERDWLRALELLGAFSLHSAGDPDVGMRSVMYNCALNASMEKREIVMALYKQMIERGVQVNATTSNALLSCFIGSSEWEESIEFYKRTDSSLRDGGTYSIMLSLFGKNGMWREACEVFQDARVGLAKAPPAIFRLGINAAHSHNWEATLSIFGNFLKAHGIQNISDSVVDKVVRCLSQNNRTTELKKVEMEVSKMKGKNKGKKK
Protein: TSET complex member tstA (Protein TPLATE) (Q54NU8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MEIEIYDELNSSDSLKQINGLSKLNQFWINQGRDPTLFFTSIIKLISETDNKTTRILCYSILKSCKCTPSDWSLAIPLLVKDLNSDDNEVVISILKTLPHISSIFTELLMMGNADFGPLVRHGNPSVRKTALDTLTSLLFYRKSILQSYKSFVSTGWELIVDRILEEPIPMVYQSSFSAISSLFSEISRSVSHSDELDNSVQKRQVLSYYADWISLKLIDHFDLLLNRAQHIDINQRHSTVNTLTYLVDTISRSSGTPFWPTSFDNNNNNNNNQQINNNNNNNNNNNNNNNNNNNNNNNNNNNNNQNNLINGISSMNLSSITGTTTTTTTTGNSPITSPTSPTSIIANTASSNKTKQISSPQNIVSILVEYFLSQLDSSNDSLVFAVGKAILDLLLTQQNQHNENWINPVLTAFIGLLRREGVSLNPLPILLAIMSVLPMLGDDLLFCTLSRIFPSIKSITDSNQRVSYLIRTFELIIDRHVTSSGKSSLFTPLMTTDCLLMAFQDESSSFREEIIVSMVASHHNILSKYIEIESEKNSNNNNSSSGNSGGGSGGSVKFSTSGNLFYLHQAALNISEVCLKCITWQSERISAIEYCIRFVDWLCRVTLSSSSSSNNSGNGSESQYGIKLISLLRSDLLDQINKIPSDYICLQAVFLICTHLLRSPTNKVYEQSDAGLLISLLRRRFLFLDNQPKFTQYNGNIRDMIMGVSQFGRVSPASLHSLSGYWLGALECLYLMGLHIPSVEATVQRTLEEILATYPHNKSVYSRARFIRRMLFSSTSSALDAQSLGKYSTIRNLNSFTNYTIDFSYCIPIEQLEASNSLHSISDIFAYECKKAITGLVGVHYGSSIRDKSSRDVTLISGASDPVWIEVSHTTHPTLNTITLHVQVTNVIHFSIKNVNIMIGLSGHLDFPYPQTNCKHNIPKLLPEKSYSFEVPLNVSSLDYNLVTFKLTFNQPSGLCESENNINLNNIHTKINNYQQSSDQLLVQSIQQQQQQQQSSSQQQSQQSQQQQYQPQPISSVNSGLSSYSLNSNNSGSLNSSANSHSISTSAVGSPGTASFISSSLLSNAQSSSPTTSSPLSNVINQNIISSSSSSSSNANQITSTTTPSSTTNSNNNTTSSSSSTNPNPNPNSHTNLNSIVGSGINQPIINNQIIQSLSITTNNPSANIIQFSPIEIRCSDYIFDWNQFLIPFKYNKHQFIQQWPRFEAVFSIDVVFEGFVSVASIFDCLSALPLHNVLNSEFGNSNFHFAFSSSTWFNEQFCFTISGMEKCLSFPEDYSIYYTSPNGQSLPKYKVYHARFEFRSSSSSLLASFESIIDQWINKLPRPTSDQFIARLLAPDEKSLFSITNITQDYQAPKNHQSLANTPLSNIVDDEIALLNQWKDFKKSQEQTKKLFSQLALDQDFY
Protein: Histone-binding protein pcf3 (Chromatin assembly factor 1 subunit C) (CAF-1 subunit C) (Pombe CAF-1 first subunit) (Q9Y825)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:18761674}. Note=Localizes to replicating chromatin. {ECO:0000269|PubMed:18761674}.
Interaction partners:
- Chromatin assembly factor 1 subunit B
- Chromatin assembly factor 1 subunit A
- Histone chaperone cia1
- Histone acetyltransferase type B catalytic subunit
- Histone deacetylase clr6
- NASP-related protein sim3
- Histone H4
- Chromatin remodeling factor mit1
- Proliferating cell nuclear antigen
Sequence:
MNTELDMQNFEHIKFLENQISEDHFRWKKNSKHLYNLLITRTLTWPSLSIQWLSAMESITEKAVLKNRLLLGTHAAEGMPNFLQLADLDLPDFNQTILDPVKHYNEDTGELGGYSMQHSCKFQISQRILHNGDVNRVRHMPQNPNIIATMSSCGNAYIFDRTKYTSMPAEEFLPNISLIGHKKEGFGLSWNRQQNCRLVTAANDSKILEWDLNNFSRDTRCLTPVKDFHYDDSPVNDVEYHPHHTNLYIAVNDNGIAFICDNRLQQTCSKTVKASNPLFSVRHNPSIATLFALGSEQDLQLWDLRNLNKSVFNTSEDLSDNRLKVPSRLTLGGTSLSWSWRHSGRIVSACQEYCYVWNFNKANPLEFVHAGHKGTVNEVDFDPFEAQCIASVADDNELHIWKPNVIVN
Protein: Collagen alpha-2(XI) chain (Q32S24)
Organism: Bos taurus (Bovine)
Function: May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen type V alpha 2 chain.
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
- Collagen alpha-3
- Collagen type III alpha 1 chain
Sequence:
MERCSRCHHLLLLVLLLLWLSAAPAWAGTAPVDVLRALRFPALPDGVRRARGICPADVAYRVSRPAQLSAPTRQLFPGGFPKDFSLLTAVRARPGLQAPLLTLYSAQGVRQLGLELGRPVRFLYEDQTGRPQPPAQPVFRGLSLADGKWHRVAVAVKGQSVTLIIDCKKRVTRPLPRSARPVLDTRGVIIFGARILDEEVFEGDIQELSIIPGVQAAYESCDQKELECEGGWRERPQRQPSHRTQRSPKQQPPRLHRPQNQEPQAQSTESLYYDYEPPYYDVMTTGTTPDYQDPTPGEEEGILESSPLPPPEEEQTDLQVPPTADRFLTEEYGEGGTEPPAGPYDYTYAYGDDYHEETELGPALSAETARSEAAARGPRGLKGEKGEPAVLEPGMLVEGPPGPEGPAGFPGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGAPGPPGTSLMLPFRFGSGGGDKGPVVAAQEAQAQAILQQARVALRGPPGPMGYTGRPGPLGQPGSPGMKGESGDLGPQGPRGPQGLMGPPGKAGRRGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGHRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPRGKPGLPGMPGSDGPPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGIKGVDGIRGLKGHKGEKGEDGFPGFKGDMGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPPGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPPGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGETGPMGERGHPGPPGPPGEQGLTGTAGKEGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGSAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGAKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPSGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGETGQAGEAGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEVGPRGQDGAKGDRGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDTGAKGEKGHPGLIGLIGPPGEQGEKGDRGLPGPQGSTGQKGETGIPGASGPIGPGGPPGLPGPAGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSRLMQEDEAVPTGGAPGSPGGLEEIFGSLDSLREEIEQMRRPMGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGAPVGVVQLTFLRLLSVSARQNISYPCSGEAQDSPLKLRGANEDELSPETSPYIKEIRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSELGAPPRRGGVLLGPVCFMG
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (E5KP26)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPLVSRLSRLWAIMRKPRAAVGSGHRKQAASQEGRQKHAKNNSQAKPSACDGMIAECPGAPAGLARQPEEVVLQASVSSYHLFRDVAEVTAFRGSLLSWYDQEKRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINYYTGWMQKWPTLQDLASASLEEVNQLWAGLGYYSRGRRLQEGARKVVEELGGHMPRTAETLQQLLPGVGRYTAGAIASIAFGQATGVVDGNVARVLCRVRAIGADPSSTLVSQQLWGLAQQLVDPARPGDFNQAAMELGATVCTPQRPLCSQCPVESLCRARQRVEQEQLLASGSLSGSPDVEECAPNTGQCHLCLPPSEPWDQTLGVVNFPRKASRKPPREESSATCVLEQPGALGAQILLVQRPNSGLLAGLWEFPSVTWEPSEQLQRKALLQELQRWAGPLPATHLRHLGEVVHTFSHIKLTYQVYGLALEGQTPVTTVPPGARWLTQEEFHTAAVSTAMKKVFRVYQGQQPGTCMGSKRSQVSSPCSRKKPRMGQQVLDNFFRSHISTDAHSLNSAAQ