wanglab/gogpt-training-data huggingface dataset:
Protein: Capping protein-inhibiting regulator of actin dynamics (Cancer-related regulator of actin dynamics) (Q6ZU35)
Organism: Homo sapiens (Human)
Function: Involved in epithelial cell integrity by acting on the maintenance of the actin cytoskeleton. Positively regulates the actin polymerization, by inhibiting the interaction of actin-capping proteins with actin.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:30361697}.
Interaction partners:
Sequence:
MGTRAFSHDSIFIPDGGAESEQTVQAMSQDNILGKVKTLQQQLGKNIKFGQRSPNAIPMNKANSGEASLEEDLFLTSPMEIVTQQDIVLSDAENKSSDTPSSLSPLNLPGAGSEMEEKVAPVKPSRPKRHFSSAGTIESVNLDAIPLAIARLDNSAAKHKLAVKPKKQRVSKKHRRLAQDPQHEQGGLESRPCLDQNGHPGEDKPTWHEEEPNPLDSEEERRRQEDYWRELEAKCKRQKAEAAEKRRLEEQRLQALERRLWEENRRQELLEEEGEGQEPPLEAERAPREEQQRSLEAPGWEDAERREREERERLEAEEERRRLQAQAQAEERRRLEEDARLEERRRQEEEEGRCAEELKRQEEEEAEGWEELEQQEAEVQGPPEALEETGEGRRGAEEEDLGEEEEEGQAHLEDWRGQLSELLNDFEERLEDQERLKPEGQREHSEEPGICEEQNPEAERRREQQGRSGDFQGADRPGPEEKREEGDTEPLLKQEGPVEAAQPPVERKEAAALEQGRKVEELRWQEVDERQTMPRPYTFQVSSGGKQILFPKVNLSPVTPAKDTGLTAAPQEPKAPKASPVQHALPSSLSVPHTAILVTGAQLCGPAVNLSQIKDTACKSLLGLEEKKHAEAPAGENPPRGPGDARAGSGKAKPRQESPSSASALAEWASIRSRILKNAESDPRSSERDQLRPGDESTPRGRCDSRGNQRKTPPVNAKFSIMPAWQKFSDGGTETSKQSTEAESIRKRPMLGPSEETAPQPPPAGVRELGKGPEKSEMHREPADTTEGCKFAKDLPSFLVPSLPYPPQKVVAHTEFTTSSDSETANGIAKPDPVMPGGEEKASPFGIKLRRTNYSLRFNCDQQAEQKKKKRHSSTGDSADAGPPAAGSARGEKEMEGVALKHGPSLPQERKQAPSTRRDSAEPSSSRSVPVAHPGPPPASSQTPAPEHDKAANKMPLAQKPALAPKPTSQTPPASPLSKLSRPYLVELLSRRAGRPDPEPSEPSKEDQESSDRRPPSPPGPEERKGQKRDEEEEATERKPASPPLPATQQEKPSQTPEAGRKEKPMLQSRHSLDGSKLTEKVETAQPLWITLALQKQKGFREQQATREERKQAREAKQAEKLSKENVSVSVQPGSSSVSRAGSLHKSTALPEEKRPETAVSRLERREQLKKANTLPTSVTVEISDSAPPAPLVKEVTKRFSTPDAAPVSTEPAWLALAKRKAKAWSDCPQIIK
Protein: CYtochrome P450 family (O16220)
Organism: Caenorhabditis elegans
Interaction partners:
- CYtochrome P450 family
- Fatty acid synthase
Sequence:
MFVILFISAILSWLIVRQYQKVSRLPPGPVSLPLIGNLPQIFYYLWTTGSIVSTLDLFRKRYGNIFTLWVGPLPHVSIADYEISHEVFVKNGSKYADKFHAPVMQDIRKDMGIMVTNGDHWQHMRRFSLQTFRNMGVGKDIMETKIMQELDARCAEIDTSAMNGVTVTQASEFFELTVGSIINSILVGKRFDATTKHEFLKIIETMDASIETASFFDMMVPVWILKTFFKHRYDNLSDAFEVSKAFSAAEAIKRVDQIKSGRYFIDENNLQDYTDAFLLKIEKEGQCQDFNMETLKTMIGDLWITGQETTTTTLISGFNQLLLHPEVMVKAREELMKVTENGSRSLSLTDRASTPYLNAMIGEIQRHASILNVNFWKINKEFTYMGGHPVDAGALVTAQLGTLHVNETVFENPLKFDPERYIRDENLLQKVIPFGVGKRSCLGESLARAELYLIFGNLLLRYKFESSSKLSTTELAPYSIGKRPFKLEMKFVKI
Protein: Vesicle transport protein GOT1B (Germ cell tumor 2) (Golgi transport 1 homolog B) (Putative NF-kappa-B-activating protein 470) (hGOT1a) (Q9Y3E0)
Organism: Homo sapiens (Human)
Function: May be involved in fusion of ER-derived transport vesicles with the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10406798}; Multi-pass membrane protein {ECO:0000269|PubMed:10406798}.
Interaction partners:
- Uridine 5'-monophosphate synthase
- Dihydropyrimidine dehydrogenase [NADP
- Dihydroorotate dehydrogenase
- Integrator complex subunit 13
- Solute carrier family 23 member 1
- Solute carrier family 23 member 2
Sequence:
MISLTDTQKIGMGLTGFGVFFLFFGMILFFDKALLAIGNVLFVAGLAFVIGLERTFRFFFQKHKMKATGFFLGGVFVVLIGWPLIGMIFEIYGFFLLFRGFFPVVVGFIRRVPVLGSLLNLPGIRSFVDKVGESNNMV
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (Q8DCK7)
Organism: Vibrio vulnificus (strain CMCP6)
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00473}.
Interaction partners:
Sequence:
MLKTINPTQTQAWNALTAHFESAQDMDLKDLFAQDAARFDKFSARFGSDILVDYSKNLINEETLKHLFALAKETELSAAIKAMFSGEAINQTEGRAVLHTALRNRSNQPVLVDGEDVMPAVNAVLEKMKSFTDRVIGGEWKGYTGKAITDIVNIGIGGSDLGPYMVTEALAPYKNHLNLHFVSNVDGTHIVETLKKVDPETTLFLIASKTFTTQETMTNAHTARDWFLATAGDQAHVAKHFAALSTNAPAVSEFGIDTDNMFEFWDWVGGRYSLWSAIGLSIALAVGYDNFIELLEGAHEMDNHFVSTELESNIPVILALIGIWYNNFHGAESEAILPYDQYMHRFAAYFQQGNMESNGKYVDRNGNPVTYQTGPIIWGEPGTNGQHAFYQLIHQGTKLIPCDFIAPAVSHNPAGDHHQKLMSNFFAQTEALAFGKNEETVKAELVKAGKNAEEVAAIAPFKVFEGNRPTNSILVKQITPRTLGNLIAMYEHKIFVQGVIWNIFSFDQWGVELGKQLANQILPELADGSEISSHDSSTNGLINAFKAFKA
Protein: Leucine-rich repeat-containing protein 49 (Centriolar satellite-associated tubulin polyglutamylase complex regulator 2) (Tubulin polyglutamylase complex subunit 4) (PGs4) (Q8IUZ0)
Organism: Homo sapiens (Human)
Function: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:34782749}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:34782749}. Note=Associated with microtubules. {ECO:0000269|PubMed:34782749}.
Interaction partners:
- Tubulin polyglutamylase complex subunit 1
- Polyglutamylase complex subunit TTLL1
- Nicolin-1
- Tubulin polyglutamylase complex subunit 2
- Centriolar satellite-associated tubulin polyglutamylase complex regulator 1
- SANT and BTB domain regulator of class switch recombination
- TBC1 domain family member 19
- Eukaryotic translation initiation factor 3 subunit F
Sequence:
MIPGKYRSVSGRAANNVNCGLHLVIQTSSLPEKNKVEFKLNKDTSSFPGRLLQHDLERNYSSRQGDHINLVSSSLSSFPILQRSSEEKILYSDRLSLERQKLTVCPIINGEDHLRLLNFQHNFITRIQNISNLQKLISLDLYDNQIEEISGLSTLRCLRVLLLGKNRIKKISNLENLKSLDVLDLHGNQITKIENINHLCELRVLNLARNFLSHVDNLNGLDSLTELNLRHNQITFVRDVDNLPCLQHLFLSFNNISSFDSVSCLADSSSLSDITFDGNPIAQESWYKHTVLQNMMQLRQLDMKRITEEERRMASVLAKKEEEKKRESHKQSLLKEKKRLTINNVARQWDLQQQRVANIATNEDRKDSDSPQDPCQIDGSTLSAFPEETGPLDSGLNNALQGLSVIDTYLVEVDGDTLSLYGSGALESLDRNWSVQTAGMITTVSFTFIEFDEIVQVLPKLKIKFPNSLHLKFKETNLVMLQQFNALAQLRRIDQLTIDPQGNPVVNFTLWKYYVLFRLSHFSMQKINGTEVTQNDMIMAERLFGILAHVASSELPQYRLISILGDARKKQFRYLLESKGKKPGIINEENNDSKRLVGENTNRATLNYTTRDFYNEKLEEIKEKKKFCKTYIEDLVKEATEINMKNEALQKLWPQMFIELVRDAVIEIRNKNSYMKLCLQQITDQK
Protein: Kynurenine formamidase (KFA) (KFase) (EC 3.5.1.9) (Arylformamidase) (N-formylkynurenine formamidase) (FKF) (Q8K4H1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:12411446}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03014, ECO:0000269|PubMed:12411446}. Note=Predominantly cytosolic. Some fraction is nuclear.
Interaction partners:
- Kynurenine 3-monooxygenase
- Tryptophan 2,3-dioxygenase
- Kynureninase
- Indoleamine 2,3-dioxygenase 2
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine--oxoglutarate transaminase 3
- Indoleamine 2,3-dioxygenase 1
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Aromatic-L-amino-acid decarboxylase
- 3-hydroxyanthranilate 3,4-dioxygenase
Sequence:
MAFPSLSAGQNPWRNLSSEELEKQYSPSRWVIHTKPEEVVGNFVQIGSQATQKARATRRNQLDVPYGDGEGEKLDIYFPDEDSKAFPLFLFLHGGYWQSGSKDDSAFMVNPLTAQGIVVVIVAYDIAPKGTLDQMVDQVTRSVVFLQRRYPSNEGIYLCGHSAGAHLAAMVLLARWTKHGVTPNLQGFLLVSGIYDLEPLIATSQNDPLRMTLEDAQRNSPQRHLDVVPAQPVAPACPVLVLVGQHDSPEFHRQSKEFYETLLRVGWKASFQQLRGVDHFDIIENLTREDDVLTQIILKTVFQKL
Protein: Sequence-variable mosaic (SVM) signal sequence domain-containing protein (Q2NJQ2)
Organism: Aster yellows witches'-broom phytoplasma (strain AYWB)
Interaction partners:
Sequence:
MFKIKNNLLLLLNVFVFAFLGLFLINNNQQVMGMDKDIASTSNNNPNITNYSIEENIINLKYKIRENAVKKINIENEIQQLSNNEPRKNTLLTLKKNLENLINNQKEQLKTYQILLKTLNDENN
Protein: Winged helix-turn-helix domain-containing protein (Q8YF33)
Organism: Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M)
Interaction partners:
Sequence:
MNIHASNLDIEKFRKVYALVTGGATDGERVAAQARARKIAERAGMSLNDAVSQLDSQPKPKPANFFEGFADWMEEKEPGYKAKRAREVVEREQRYASRRAEILKQFGTAKAFLDPTPNERLILKAAEPFIAELGEPYEDACGTWRRPISSFAGVHSHFFNLDDVDPEAIMAIKAAIPFPETICGAFEELKVWDKLNDDRAHFYGHHEYYYELPVELRIELLREVMRTQPVTSWGDLEARFHYKSYAWQRQWIDPKDFDDPEWSRLFDDVRILRALAEKPFREPVQNGRRTNAEKRSAVLSMLDTNPELSDREICRRVGVSPKTVGNWRRRRNDRLSQP
Protein: Protein KRE1 (Killer toxin-resistance protein 1) (P17260)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in a late stage of cell wall 1,6-beta-glucan synthesis and assembly. Has a structural, rather than enzymic, function within cell wall 1,6-beta-glucan assembly and architecture, possibly by being involved in covalently cross-linking 1,6-beta-glucans to other cell wall components such as 1,3-beta-glucan, chitin and certain mannoproteins. Acts as the plasma membrane receptor for the yeast K1 viral toxin.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor. Secreted, cell wall. Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as component of the cell wall. Concentrated at the surface of mother cells.
Interaction partners:
- Glucosidase 2 subunit alpha
- Cell wall synthesis protein KRE9
- Beta-glucan synthesis-associated protein KRE6
- Trafficking protein particle complex II-specific subunit 65
- Mannan endo-1,6-alpha-mannosidase DFG5
- Mannosyl-oligosaccharide glucosidase
- Pheromone-processing carboxypeptidase KEX1
- Killer toxin-resistance protein 5
- Cell wall synthesis protein KNH1
- Flavin carrier protein 2
Sequence:
MMRRTLLHSFATLLLSLSLWSAAVMAAVTTQVTVVTNVAGALVTETTIWDPATAAAAATTTAQTGFFTTVFTTTNDVGTTVTLTQTVNRATMLPTTTTSTSSTGKTTTTVPTATSSLSSGLYLSTVTTTNDLGTTVTLTQTFTHSSTSATSSASSSVSSSVSSSGSSSSVKTTTSTGSAVAETGTRPDPSTDFTEPPVSAVTSLSIDSYITITEGTTSTYTTTRAPTSMWVTVVRQGNTITVQTTFVQRFSSQYVTVASPSVGSIGMGTLTGTVGVIKSAIKKTVSHNEAQHLGMSSFTSILGGLLTVLIWFL
Protein: Exocyst complex component 6 (Exocyst complex component Sec15A) (SEC15-like protein 1) (Q8R313)
Organism: Mus musculus (Mouse)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O54923}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O54923}. Cell projection, growth cone {ECO:0000250|UniProtKB:O54923}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q8TAG9}. Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). {ECO:0000250|UniProtKB:O54923, ECO:0000250|UniProtKB:Q8TAG9}.
Interaction partners:
- Exocyst complex component 5
- Exocyst complex component 3
- Exocyst complex component 8
- Exocyst complex component 2
- Exocyst complex component 7
- Exocyst complex component 1
- Exocyst complex component 4
- Ras-related protein Rab-11A
- Rab-3A-interacting protein
- Ras-related protein Rab-8A
Sequence:
MAESCEALGTVPEHERILQEIESTDTACVGPTLRSVYDDQPNAHKKFMEKLDACIRNHDKEIEKMCNFHHQGFVDAITELLKVRADAEKLKVTDTNRRFQDAGKEVIIQTEDIIRCRIQQRNITTVVEKLQLCLPVLEMYSKLKEQMSMKRYYSALKTMEQLENVYFPRVSQYRFCQLMMETLPKLREDMMNYCMSDLTYGLESIRKHSDKIGEAAMKQAQQQKSFSVALQKQNNMRFGKNMHVNNDRILEEKSDVIPKHALEEEAENDEEVLTVQDLVDFSPVYRCLHIYSALGDEETFENYYRKQRKKQARLVLQPQSSVHETVDGYRRYFTQIVGFFVVEDHILHVTQGLVTRVYTEELWNMALSKIIAVLRAHSSYCTDPDLVLELKNLIVIFADTLQGYGFPVNRLFDLLFEIRDQYNETLLKKWAGIFRDIFEEDNYSPIPIGSEEEYKVVISRFPFQDPDLEKQSFPKKFPMSQSVPLIYIQVKEFIYASLKFSESLHRSSTEIDDMLRKSTNLLLTRILSSCLLNLIRKPHIGLTELVQIIINTTHLEQACKYLEDFITNITNISQETVHTTRLYGLSTFKDARHAAEGEIYTKLNQKIDEFVQLADYDWTMAESDGRASGYLMDLINFLRSIFQVFTHLPGKVAQTACMSACQHLSTSLMQMLLDSELKQISMGAVQQFNLDVIQCELFASSEPVPGFQGDTLQLAFIDLRQLLDLFMVWDWSTYLADYGQPASKYLRVNPHAALTLLEKMKDTSKKNNIFAQFRKNDRDRQKLIETVVRQLRGLVTGMSQHT
Protein: Probable E3 ubiquitin-protein ligase DTX2 (EC 2.3.2.27) (Protein deltex-2) (Deltex2) (hDTX2) (RING finger protein 58) (RING-type E3 ubiquitin transferase DTX2) (Q86UW9)
Organism: Homo sapiens (Human)
Function: Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Probably acts both as a positive and negative regulator of Notch, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Functions as a ubiquitin ligase protein in vitro, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11564735}. Nucleus {ECO:0000269|PubMed:11564735}. Note=Predominantly cytoplasmic. Partially nuclear. {ECO:0000269|PubMed:11564735}.
Interaction partners:
- DNA-binding protein RFX6
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Calcium-responsive transactivator
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Transcription factor RFX3
- Cyclin-K
- Ankyrin-2
- Ankyrin-3
Sequence:
MAMAPSPSLVQVYTSPAAVAVWEWQDGLGTWHPYSATVCSFIEQQFVQQKGQRFGLGSLAHSIPLGQADPSLAPYIIDLPSWTQFRQDTGTMRAVRRHLFPQHSAPGRGVVWEWLSDDGSWTAYEASVCDYLEQQVARGNQLVDLAPLGYNYTVNYTTHTQTNKTSSFCRSVRRQAGPPYPVTTIIAPPGHTGVACSCHQCLSGSRTGPVSGRYRHSMTNLPAYPVPQHPPHRTASVFGTHQAFAPYNKPSLSGARSAPRLNTTNAWGAAPPSLGSQPLYRSSLSHLGPQHLPPGSSTSGAVSASLPSGPSSSPGSVPATVPMQMPKPSRVQQALAGMTSVLMSAIGLPVCLSRAPQPTSPPASRLASKSHGSVKRLRKMSVKGATPKPEPEPEQVIKNYTEELKVPPDEDCIICMEKLSTASGYSDVTDSKAIGSLAVGHLTKCSHAFHLLCLLAMYCNGNKDGSLQCPSCKTIYGEKTGTQPQGKMEVLRFQMSLPGHEDCGTILIVYSIPHGIQGPEHPNPGKPFTARGFPRQCYLPDNAQGRKVLELLKVAWKRRLIFTVGTSSTTGETDTVVWNEIHHKTEMDRNITGHGYPDPNYLQNVLAELAAQGVTEDCLEQQ
Protein: (2S)-flavanone 2-hydroxylase (EC 1.14.14.162) (CYP GE-5) (Cytochrome P450 93B1) (Flavone synthase II) (Licodione synthase) (P93149)
Organism: Glycyrrhiza echinata (Licorice)
Function: Catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively. Can also convert eriodictyol to luteolin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEPQLVAVSVLVSALICYFFFRPYFHRYGKNLPPSPFFRLPIIGHMHMLGPLLHQSFHNLSHRYGPLFSLNFGSVLCVVASTPHFAKQLLQTNELAFNCRIESTAVKKLTYESSLAFAPYGDYWRFIKKLSMNELLGSRSINNFQHLRAQETHQLLRLLSNRARAFEAVNITEELLKLTNNVISIMMVGEAEEARDVVRDVTEIFGEFNVSDFIWLFKKMDLQGFGKRIEDLFQRFDTLVERIISKREQTRKDRRRNGKKGEQGSGDGIRDFLDILLDCTEDENSEIKIQRVHIKALIMDFFTAGTDTTAISTEWALVELVKKPSVLQKVREEIDNVVGKDRLVEESDCPNLPYLQAILKETFRLHPPVPMVTRRCVAECTVENYVIPEDSLLFVNVWSIGRNPKFWDNPLEFRPERFLKLEGDSSGVVDVRGSHFQLLPFGSGRRMCPGVSLAMQEVPALLGAIIQCFDFHVVGPKGEILKGDDIVINVDERPGLTAPRAHNLVCVPVDRTSGGGPLKIIEC
Protein: Haloacid dehalogenase-like hydrolase domain-containing protein Sgpp (EC 3.1.3.-) (Subclass I phosphosugar phosphatase) (AtSgpp) (Q9ZVJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a phosphosugar phosphatase on a broad range of sugar phosphate substrates with preferential activity on D-ribose-5-phosphate, 2-deoxy-D-ribose-5-phosphate, 2-deoxy-D-glucose-6-phosphate, and D-mannose-6-phosphate and with a lower activity on D-fructose-1-phosphate, D-glucose-6-phosphate, DL-glycerol-3-phosphate, and D-fructose-6-phosphate.
Interaction partners:
- Haloacid dehalogenase-like hydrolase domain-containing protein At2g33255
- Alkaline-phosphatase-like family protein
- 
- Alkaline-phosphatase-like family protein
- Alkaline-phosphatase-like family protein
- GPI ethanolamine phosphate transferase 2
- Transcription factor ALC
- GPI ethanolamine phosphate transferase 3
- Catalytic/ hydrolase
- 
Sequence:
MNGFSDLNPSESKPSLSQLAPLEAILFDVDGTLCDSDPIHLIAFQELLQEIGFNNGVPIDEKFFVENIAGKHNSEIALLLFPDDVSRGLKFCDEKEALYRKIVAEKIKPLDGLIKLTKWIEDRGLKRAAVTNAPKENAELMISKLGLTDFFQAVILGSECEFPKPHPGPYLKALEVLNVSKEHTLVFEDSISGIKAGVAAGMPVIGLTTGNPASLLMQAKPAFLIENYADPKLWAVLEELDNKS
Protein: Interleukin-22 (IL-22) (Cytokine Zcyto18) (IL-10-related T-cell-derived-inducible factor) (IL-TIF) (Q9GZX6)
Organism: Homo sapiens (Human)
Function: Cytokine that plays a critical role in modulating tissue responses during inflammation. Plays an essential role in the regeneration of epithelial cells to maintain barrier function after injury and for the prevention of further tissue damage. Unlike most of the cytokines, has no effect on immune cells. Signals through a heterodimeric receptor composed of two subunits, the specific receptor IL22RA1 which is present on non-immune cells in many organs and the shared subunit IL10RB. Ligation of IL22RA1 with IL22 induces activation of the tyrosine kinases JAK1 and TYK2, which in turn activates STAT3. In turn, promotes cell survival and proliferation through STAT3, ERK1/2 and PI3K/AKT pathways.
Subcellular location: Secreted.
Interaction partners:
- Interleukin-22 receptor subunit alpha-2
- Interleukin-22 receptor subunit alpha-1
- Interleukin-10 receptor subunit beta
- Interleukin-17A
- Interleukin-17F
- Interleukin-20 receptor subunit alpha
- Interleukin-23 receptor
- Interleukin-10
- Interferon gamma
- Interleukin-10 receptor subunit alpha
Sequence:
MAALQKSVSSFLMGTLATSCLLLLALLVQGGAAAPISSHCRLDKSNFQQPYITNRTFMLAKEASLADNNTDVRLIGEKLFHGVSMSERCYLMKQVLNFTLEEVLFPQSDRFQPYMQEVVPFLARLSNRLSTCHIEGDDLHIQRNVQKLKDTVKKLGESGEIKAIGELDLLFMSLRNACI
Protein: DNA repair protein XRCC4 (X-ray repair cross-complementing protein 4) [Cleaved into: Protein XRCC4, C-terminus (XRCC4/C)] (Q924T3)
Organism: Mus musculus (Mouse)
Function: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination. Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other. The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors. Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed. XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity. Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends. Promotes displacement of PNKP from processed strand break termini (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q13426}. Chromosome {ECO:0000250|UniProtKB:Q13426}. Note=Localizes to site of double-strand breaks. {ECO:0000250|UniProtKB:Q13426}.; SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm {ECO:0000250|UniProtKB:Q13426}. Note=Translocates from the nucleus to the cytoplasm following cleavage by caspase-3 (CASP3). {ECO:0000250|UniProtKB:Q13426}.
Interaction partners:
- Non-homologous end-joining factor 1
- DNA ligase 4
- DNA-dependent protein kinase catalytic subunit
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
- Protein PAXX
- Aprataxin and PNK-like factor
- Aprataxin
- TP53-binding protein 1
- Bifunctional polynucleotide phosphatase/kinase
Sequence:
MERKVSRIYLASEPNVPYFLQVSWERAIGSGFVITLTDGHSAWTATVSELEISQEADDMAMEKGKYIDELRKALVPGSGAAGTYKFLFSKESQHFSLEKELKDVSFRLGSFNLDKVSNSAEVIRELICYCLDTITEKQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALEADLYQRFILVLNEKKTKIRSLHKLLNEVQQLEESTKPERENPCSDKTPEEHGLYDGSTDEESGAPVQAAETLHKDDSIFSSPDVTDIAPSRKRRHRMQKNLGTEPKMAPQELPLQEKERLASSLPQTLKEESTSAENMSLETLRNSSPEDLFD
Protein: Conserved protein (O69686)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty acid methyltransferase Rv3720
Sequence:
MQGQLSRTRVYTVPVPGSAQSAYACGVERLLASYRSIPATASIRLAKPTSNLFRARVKHDARGLDASGLTGVIGIDPEARTADVAGMCTYEDLIAATLHYGLSPLVVPQLRTITLGGAVTGLGIESASFRNGLPHESVLEMDILTGAGELLTVSPGQHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFVALRHIRFSSLTAMVAAMERIIDTGGLDGESVDYLDGVVFSADESYLCIGMQTSVPGPVSDYTGQDIYYRSIQHEAGIKEDRLTIHDYFWRWDTDWFWCSRSFGAQNPRLRRWWPRRYRRSSVYWRLMALDQRFGIADRFENSRGRPARERVVQDIEVPIERTCEFLEWFGENVPISPIWLCPLRLRDHAGWPLYPIRPDRSYVNIGFWSSVPVGATEGATNRKIENKVSALDGHKSLYSDSFYTREEFDELYGGETYNTVKKAYDPDSRLLDLYAKAVQRR
Protein: N-lysine methyltransferase KMT5A (EC 2.1.1.-) (H4-K20-HMTase KMT5A) (Histone-lysine N-methyltransferase KMT5A) (EC 2.1.1.361) (Lysine N-methyltransferase 5A) (Lysine-specific methylase 5A) (PR/SET domain-containing protein 07) (PR-Set7) (PR/SET07) (SET domain-containing protein 8) (Q9NQR1)
Organism: Homo sapiens (Human)
Function: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.
Subcellular location: Nucleus {ECO:0000269|PubMed:12086618}. Chromosome {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12208845, ECO:0000269|PubMed:23468428}. Note=Specifically localizes to mitotic chromosomes (PubMed:12208845). Colocalized with SIRT2 at mitotic foci (PubMed:23468428). Associates with chromosomes during mitosis; association is increased in a H(2)O(2)-induced oxidative stress-dependent manner (PubMed:23468428). Associates with silent chromatin on euchromatic arms (PubMed:12086618). Not associated with constitutive heterochromatin (PubMed:12086618). {ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:12208845, ECO:0000269|PubMed:23468428}.
Interaction partners:
- Histone H4
- Histone H3.1
- Histone H3.2
- Histone H2B type 1-K
- Histone H2B type 1-J
- Lethal
- Histone H2A type 1-C
- Histone H2A type 1-B/E
- Histone H4-like protein type G
- Histone H2A type 1
Sequence:
MGEGGAAAALVAAAAAAAAAAAAVVAGQRRRRLGRRARCHGPGRAAGGKMSKPCAVEAAAAAVAATAPGPEMVERRGPGRPRTDGENVFTGQSKIYSYMSPNKCSGMRFPLQEENSVTHHEVKCQGKPLAGIYRKREEKRNAGNAVRSAMKSEEQKIKDARKGPLVPFPNQKSEAAEPPKTPPSSCDSTNAAIAKQALKKPIKGKQAPRKKAQGKTQQNRKLTDFYPVRRSSRKSKAELQSEERKRIDELIESGKEEGMKIDLIDGKGRGVIATKQFSRGDFVVEYHGDLIEITDAKKREALYAQDPSTGCYMYYFQYLSKTYCVDATRETNRLGRLINHSKCGNCQTKLHDIDGVPHLILIASRDIAAGEELLYDYGDRSKASIEAHPWLKH
Protein: Rab GDP dissociation inhibitor beta (Rab GDI beta) (GDI-3) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) (Q61598)
Organism: Mus musculus (Mouse)
Function: GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking. Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P50395}.
Interaction partners:
- Ras-related protein Rab-1A
- Ras-related protein Rab-6A
- Ras-related protein Rab-10
- Ras-related protein Rab-1B
- Ras-related protein Rab-7a
- Cell division control protein 42 homolog
- Ras-related protein Rab-8A
- Ras-related protein Rab-6B
- Ras-related protein Rab-5A
- Ras-related protein Rab-11A
Sequence:
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDQNPYYGGESASITPLEDLYKRFKLPGQPPASMGRGRDWNVDLIPKFLMANGQLVKMLLFTEVTRYMDFKVIEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGVDPKKTSMRDVYKKFDLGQDVIDFTGHSLALYRTDDYLDQPCCETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVVGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLFVPKDLGTDSQIFISRAYDATTHFETTCDDIKDIYKRMTGSEFDFEEMKRKKNDIYGED