wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ECM21 (Extracellular mutant protein 21) (P38167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
- Protein LDB19
- Arrestin-related trafficking adapter 3
- Manganese transporter SMF1
- Arrestin-related trafficking adapter 6
- Protein ROD1
- Protein ROG3
- Arrestin-related trafficking adapter 5
- Arrestin-related trafficking adapter 10
- Ubiquitin ligase-binding protein BUL2
Sequence:
MPFITSRPVAKNSSHSLSETDLNQSKGQPFQPSPTKKLGSMQQRRRSSTIRHALSSLLGGANVHSPAVLNNTTKGGNNNGNIRSSNTDAQLLGKKQNKQPPPNARRHSTTAIQGSISDSATTTPRSSTSDTNRRTSGRLSVDQEPRISGGRYSQIEEDSTVLDFDDDHNSSAVVSSDLSSTSLTRLANSKKFNEQFLIEYLTARGLLGPKTVLSNEYLKISISTSGESVFLPTISSNDDEYLSRLNGLNDGTDDAEADFFMDGIDQQEGNTPSLATTAAATESGGSINENRDTLLRENNSGDHPGSGSELNTRSVEIDSSMVSYSIAVIVSVKKPTRFTDMQLELCSRVKVFWNTGVPPTKTFNEEFYNAASMKWNLNDENFDLFVPLSISPDDQMIENNSNDRQMRLFKNIPTEERLYLDKTKTKASLLNAIDVNKTHLYQPGDYVFLVPVVFSNHIPETIYLPSARVSYRLRLATKAINRKGFYRQDSNSPQPIVSPDSSSSLSSTTSSLKLTETESAQAHRRISNTLFSKVKNHLHMSSHQLKNEESGEEDIFAEYPIKVIRTPPPVAVSTANKPIYINRVWTDSLSYEISFAQKYVSLNSEVPIKIKLAPICKNVCVKRIHVSITERVTFVSKGYEYEYDQTDPVAKDPYNPYYLDFASKRRKERSVSLFEIRTKEKGTRALREEIVENSFNDNLLSYSPFDDDSDSKGNPKERLGITEPIIIETKLKFPKYEDLDKRTAKIIPPYGIDAYTSIPNPEHAVANGPSHRRPSVIGFLSGHKGSKSHEENEKPVYDPKFHQTIIKSNSGLPVKTHTRLNTPKRGLYLDSLHFSNVYCRHKLEIMLRISKPDPECPSKLRHYEVLIDTPIFLVSEQCNSGNMELPTYDMATMEGKGNQVPLSMNSDFFGNTCPPPPTFEEAISVPASPIVSPMGSPNIMASYDPDLLSIQQLNLSRTTSVSGPSGYSDDAGVPNVNRNSISNANAMNGSISNSAFVSGNSGQGVARARATSVNDRSRFNNLDKLLSTPSPVNRSHNSSPTNGLSQANGTVRIPNATTENSKDKQNEFFKKGYTLANVKDDEEQEGIVSSSSADSLLSHGNEPPRYDEIVPLMSDEE
Protein: Cofilin-1 (Cofilin, non-muscle isoform) (P45592)
Organism: Rattus norvegicus (Rat)
Function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (By similarity). Important for normal progress through mitosis and normal cytokinesis (By similarity). In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (By similarity). Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (By similarity). Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). Required for neural tube morphogenesis and neural crest cell migration (By similarity).
Subcellular location: Nucleus matrix {ECO:0000250|UniProtKB:P10668}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P10668}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P10668}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10668}; Cytoplasmic side {ECO:0000250|UniProtKB:P10668}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P18760}. Cell projection, growth cone {ECO:0000250|UniProtKB:P18760}. Cell projection, axon {ECO:0000250|UniProtKB:P18760}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide. {ECO:0000250|UniProtKB:P10668, ECO:0000250|UniProtKB:P23528}.
Interaction partners:
- Src substrate cortactin
- LIM domain kinase 1
- Hematopoietic lineage cell-specific protein
- LIM domain kinase 2
- Actin, cytoplasmic 1
- Protein phosphatase Slingshot homolog 1
- Actin nucleation-promoting factor WASL
- Protein phosphatase Slingshot homolog 3
- Actin, cytoplasmic 2
- protein-serine/threonine phosphatase
Sequence:
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYTTFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL
Protein: Uncharacterized protein C5orf46 (Q6UWT4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MAVSVLRLTVVLGLLVLFLTCYADDKPDKPDDKPDDSGKDPKPDFPKFLSLLGTEIIENAVEFILRSMSRSTGFMEFDDNEGKHSSK
Protein: Carnitine O-palmitoyltransferase 2, mitochondrial (EC 2.3.1.21) (Carnitine palmitoyltransferase II) (CPT II) (P23786)
Organism: Homo sapiens (Human)
Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Interaction partners:
- Mitochondrial carnitine/acylcarnitine carrier protein
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Carnitine O-palmitoyltransferase 1, liver isoform
- Peroxisomal acyl-coenzyme A oxidase 3
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Palmitoyl thioesterase CPT1C
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Beta-alanine-activating enzyme
Sequence:
MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLIIAKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELTDALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHGQLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLGGFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS
Protein: TATA box-binding protein-like 1 (TBP-like factor) (Q387R9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor TFIIIB component B'' Myb domain-containing protein
- Transcription factor, putative
- Bromo domain-containing protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- RNA polymerase-like protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-direcetd RNA polymerase II, subunit 9, putative
- General transcription factor IIH subunit 4
Sequence:
MDNDFTGNFDMDENDFFIDEDEGDMDFLQRAAGASGVYVDAAPKVVMENNEQMKGECSDRVAEVNIQELFPNADPATVPLVVGIIAQAKLGVGVDLRALSCATRNVEFTPRVRCPAATLRLHEPNAVVQVRTSGLLGIIGSTSVGEARQATELAARIIRKALNLNFSSVQFRVRSLMARFDLCHPIRLDELAKHEGVFCSYEPDRFSGCIVRLSGSSRGNQWQVCCTVFVTGKVIVLGARSREELLDAFYTVLPIIAQYAKR
Protein: U-box domain-containing protein 38 (EC 2.3.2.27) (Plant U-box protein 38) (RING-type E3 ubiquitin transferase PUB38) (Q9FJP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as an E3 ubiquitin ligase.
Interaction partners:
- Probable ubiquitin-conjugating enzyme E2 37
Sequence:
MGKNGRLRWNPFSHRSSSSTSSSSRQQQQEQQPPVEFLCPISKSVMSDPVVVSSGQTFERVCVQVCRDLNFIPKLNDDEESLPDFSNIIPNLNMKSTIDTWCDTVGVSRPQPPDYSTVERILRQQMPPPDVEIRVSEQELLRAVAHRAPMIIHHADSELMGRRDFNNSTTSSDESVIVAHSPFTPLPLTTRPACFSPSPSSSSSEIETLTHHTFFSNSTSTATEEDEVIYNKLKSSEIFDQEQGLIMMRKMTRTNDEARVSLCSPRILSLLKNMIVSRYSLVQTNALASLVNLSLDKKNKLTIVRLGFVPILIDVLKSGSREAQEHAAGTIFSLSLEDDNKMPIGVLGALQPLLHALRAAESDRTRHDSALALYHLTLNQTNRSKLVRLGAVPALFSMVRSGESASRALLVICNLACCSEGRSAMLDANAVAILVGKLREEWTEEPTEARSSSSARENCVAALFALSHESLRFKGLAKEARAVEVLKEVEERGTERAREKAKKILQLMRERVPEDDEEDGEGSIDWDRVIDSNGSIRSRFRVGGRNRVVTQNSSGF
Protein: Inactive 2'-5'-oligoadenylate synthase 1B ((2-5')oligo(A) synthase 1B) (2-5A synthase 1B) (2'-5'-oligoadenylate synthase-like protein 1) (Q60856)
Organism: Mus musculus (Mouse)
Function: Does not have 2'-5'-OAS activity, but can bind double-stranded RNA. The full-length protein displays antiviral activity against flaviviruses such as west Nile virus (WNV) via an alternative antiviral pathway independent of RNase L. The truncated form of the protein lacks antiviral activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:22623793}; Single-pass type IV membrane protein {ECO:0000305|PubMed:22623793}.
Interaction partners:
Sequence:
MEQDLRSIPASKLDKFIENHLPDTSFCADLREVIDALCALLKDRSFRGPVRRMRASKGVKGKGTTLKGRSDADLVVFLNNLTSFEDQLNQQGVLIKEIKKQLCEVQHERRCGVKFEVHSLRSPNSRALSFKLSAPDLLKEVKFDVLPAYDLLDHLNILKKPNQQFYANLISGRTPPGKEGKLSICFMGLRKYFLNCRPTKLKRLIRLVTHWYQLCKEKLGDPLPPQYALELLTVYAWEYGSRVTKFNTAQGFRTVLELVTKYKQLQIYWTVYYDFRHQEVSEYLHQQLKKDRPVILDPADPTRNIAGLNPKDWRRLAGEAAAWLQYPCFKYRDGSSVCSWEVPTEVGVPMKYLLCRIFWLLFWSLFHFIFGKTSSG
Protein: Protein tipD (O15736)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Not known; disruption of the gene for tipD results in morphological defects.
Interaction partners:
- Autophagy protein 5
- Ubiquitin-like protein atg12
- Autophagy-related protein 3
- Autophagy-related protein 18
- Ubiquitin-like modifier-activating enzyme atg7
- Serine/threonine-protein kinase atg1
- Probable serine/threonine-protein kinase DDB_G0291918
- Probable serine/threonine-protein kinase vps15
- Autophagy-related protein 9
- Phosphatidylinositol 3-kinase VPS34-like
Sequence:
MFSSQNNSYMMMMGGGGIGNINNNQFYSPIISTSAQSFNSIVEWKRDIIRQLNDRNQNQTNNYSEFMRIYTDLLKRERTLNDRTLLYEKEIVSLRNEKKTQQQPPSGSSKMDSSSSSSSSNRVSGMGSTIEEMEQKLFKLQEDLTNSYKRNADNASSILLLNDKNKDLQNELMSKEIEIERIRSTIQQDLDSIKRLEMVVIEKENVSQIIRDELSSLQTEFLHNESKVVKLEQENSSLVERWLRKKNEEASKMNEANDFYQKMVEQRDSTPAKAAVQLSESISNLVVKLPDANDVPIPIVLERGVFSSEAMLPSKAKKRWTGHNSEIYCMAFNSIGNLLATGGGDKCVKVWDVISGQQKSTLLGASQSIVSVSFSPNDESILGTSNDNSARLWNTELGRSRHTLTGHIGKVYTGKFINSNRVVTGSHDRTIKLWDLQKGYCTRTIFCFSSCNDLVILGGSGTHLASGHVDHSVRFWDSNAGEPTQVLSSIHEGQITSITNSPTNTNQILTNSRDHTLKIIDIRTFDTIRTFKDPEYRNGLNWTKASWSPDGRYIASGSIDGSICIWDATNGKTVKVLTKVHNNGSSVCCCSWSPLANIFISADKDKNIIQWE
Protein: Pituitary homeobox 1 (Homeobox protein PITX1) (Paired-like homeodomain transcription factor 1) (Q99NA7)
Organism: Rattus norvegicus (Rat)
Function: Sequence-specific transcription factor that binds gene promoters and activates their transcription. May play a role in the development of anterior structures, and in particular, the brain and facies and in specifying the identity or structure of hindlimb.
Subcellular location: Nucleus.
Interaction partners:
- Pituitary-specific positive transcription factor 1
- T-box transcription factor 19
- Steroidogenic factor 1
- LIM/homeobox protein Lhx3
- T-box transcription factor 4
Sequence:
MDAFKGGMSLERLPEGLRPPPPPPHDMGPSFHLARTADPREPLENSASESSDADLPDKERGGEAKVPEDGGAGSAGCGSAEDPAKKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSMREEIAVWTNLTEPRVRVWFKNRRAKWRKRERNQQLDLCKGGYVPQFSGLVQPYEDVYAAAGYSYNNWAAKSLAPAPLSTKSFTFFNSMSPLSSQSMFSAPSSISSMTMPSSMGPGSVPGMPNSGLNNINNLTGSSLNSAMSPGACPYGTPASPYSVYRDTCNSSLASLRLKSKQHSSFGYGGLQGPASGLNACQYNS
Protein: tRNA (guanine(6)-N(2))-methyltransferase THUMP3 (EC 2.1.1.256) (THUMP domain-containing protein 3) (tRNA(Trp) (guanine(7)-N(2))-methyltransferase THUMP3) (EC 2.1.1.-) (Q9BV44)
Organism: Homo sapiens (Human)
Function: Methyltransferase which catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates containing the characteristic 3'-CCA terminus of mature tRNAs. Also catalyzes the formation of N(2)-methylguanosine at position 7 of tRNA(Trp). Requires the methyltransferase adapter protein TRM112 for tRNA methyltransferase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:34669960, ECO:0000269|PubMed:34948388}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- Histone-lysine N-methyltransferase SETD5
Sequence:
MCDIEEATNQLLDVNLHENQKSVQVTESDLGSESELLVTIGATVPTGFEQTAADEVREKLGSSCKISRDRGKIYFVISVESLAQVHCLRSVDNLFVVVQEFQDYQFKQTKEEVLKDFEDLAGKLPWSNPLKVWKINASFKKKKAKRKKINQNSSKEKINNGQEVKIDQRNVKKEFTSHALDSHILDYYENPAIKEDVSTLIGDDLASCKDETDESSKEETEPQVLKFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNITHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEGATEWSDCFHIAGDNNPLAVNRAANNIASLLTKSQIKEGKPSWGLPIDAVQWDICNLPLRTGSVDIIVTDLPFGKRMGSKKRNWNLYPACLREMSRVCTPTTGRAVLLTQDTKCFTKALSGMRHVWRKVDTVWVNVGGLRAAVYVLIRTPQAFVHPSEQDGERGTLWQCKE
Protein: Ubiquitin-conjugating enzyme E2 G1 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme G1) (E217K) (UBC7) (Ubiquitin carrier protein G1) (Ubiquitin-protein ligase G1) [Cleaved into: Ubiquitin-conjugating enzyme E2 G1, N-terminally processed] (P62253)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like modifier-activating enzyme 1
- E3 ubiquitin-protein ligase AMFR
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-conjugating enzyme E2 J1
- Ubiquitin-conjugating enzyme E2 G2
- Ubiquitin-like modifier-activating enzyme 6
Sequence:
MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLTFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETIMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE
Protein: Intermediate capsid protein VP6 (P04509)
Organism: Rotavirus A (strain RVA/Cow/France/RF/1975/G6P6[1]) (RV-A)
Function: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (By similarity). VP6 is required for the transcription activity of the DLP.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:11285213, ECO:0000269|PubMed:12097594}. Note=Component of the intermediate capsid (PubMed:11285213). Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential). {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:11285213}.
Interaction partners:
Sequence:
MDVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIITMNGNEFQTGGIGNLPIRNWNFDFGLLGTTLLNLDANYVETARNTIDYFVDFVDNVCMDEMVRESQRNGIAPQSDSLIKLSGIKFKRINFDNSSEYIENWNLQNRRQRTGFTFHKPNIFPYSASFTLNRSQPAHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANTQQFEHIVQLRRVLTTATITLLPDAERFSFPRVITSADGATTWYFNPVILRPNNVEIEFLLNGQIINTYQARFGTIIARNFDTIRLSFQLMRPPNMTPAVAALFPNAQPFEHHATVGLTLRIESAVCESVLADASETMLANVTSVRQEYAIPVGPVFPPGMNWTDLITNYSPSREDNLQRVFTVASIRSMLVK
Protein: MAGUK p55 scaffold protein 4 (E7EUL8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIQSDKGADPPDKKDMKLSTATNPQNGLSQILRLVLQELSLFYGRDVNGVCLLYDLLHSPWLQALLKIYDCLQEFKEKKLVPATPHAQVLSYEVVELLRETPTSPEIQELRQMLQAPHFKALLSAHDTIAQKDFEPLLPPLPDNIPESEEAMRIVCLVKNQQPLGATIKRHEMTGDILVARIIHGGLAERSGLLYAGDKLVEVNGVSVEGLDPEQVIHILAMSRGTIMFKVVPVSDPPVNSQQMVYVRAMTEYWPQEDPDIPCMDAGLPFQKGDILQIVDQNDALWWQARKISDPATCAGLVPSNHLLKRKQREFWWSQPYQPHTCLKSTLSISMEEEDDMKIDEKCVEAEELSEDKEEFVGYGQKFFIAGFRRSMRLCRRKSHLSPLHASVCCTGSCYSAVGAPYEEVVRYQRRPSDKYRLIVLMGPSGVGVNELRRQLIEFNPSHFQSAVPHTTRTKKSYEMNGREYHYVSKETFENLIYSHRMLEYGEYKGHLYGTSVDAVQTVLVEGKICVMDLEPQDIQGVRTHELKPYVIFIKPSNMRCMKQSRKNAKVITDYYVDMKFKDEDLQEMENLAQRMETQFGQFFDHVIVNDSLHDACAQLLSAIQKAQEEPQWVPATWISSDTESQ
Protein: Procathepsin L (EC 3.4.22.15) (Cathepsin L1) (Major excreted protein) (MEP) [Cleaved into: Cathepsin L; Cathepsin L heavy chain; Cathepsin L light chain] (Q9GKL8)
Organism: Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Function: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:P06797}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secreted, extracellular space {ECO:0000250|UniProtKB:P06797}. Secreted {ECO:0000250|UniProtKB:P06797}. Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. {ECO:0000250|UniProtKB:P06797}.
Interaction partners:
Sequence:
MNPTFILAALCLGIASATLTFNHSLEAQWTKWKAMHNRLYGMNEEGWRRAVWEKNMKMIELHNQEYSQGKHSFTMAMNTFGDMTSEEFRQVMNGFQNRKPRKGKVFQEPLFYEAPRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSGPQGNEGCNGGLMDYAFQYVADNGGLDSEESYPYEATEESCKYNPEYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFMFYKEGIYFEPDCSSEDMDHGVLVVGYGFESTESDNSKYWLVKNSWGEEWGMGGYIKMAKDRRNHCGIASAASYPTV
Protein: Ras-related protein RABG2 (AtRABG2) (Ras-related protein Rab77) (AtRab77) (Ras-related protein Rab7a) (AtRab7a) (Q9SJ11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular vesicle trafficking and protein transport.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 B
- Geranylgeranyl transferase type-2 subunit beta 1
- Vacuolar protein sorting-associated protein 41 homolog
- Protein VACUOLELESS1
- Vacuolar protein-sorting-associated protein 33 homolog
- Vacuolar protein-sorting-associated protein 11 homolog
- Vacuolar sorting protein 18
- Vacuolar fusion protein MON1 homolog
- GPN-loop GTPase QQT1
- Geranylgeranyl transferase type-2 subunit alpha 2
Sequence:
MDSLKNRTLLKVIVLGDSGVGKTSLMNQYVYKKFNKQYKATIGADFVTKELHIDEKSVTLQIWDTAGQERFQSLGAAFYRGADCCVLVYDVNNLKSFETLNNWHTEFLKQANPMEPETFPFVLIGNKTDVDGGNSRVVSNKRAIEWCGSKGNIPYHETSAKEDTNIDEAFLSVAHIALSNERKQSNDIYPRGQYHDSVTDIIDPDQSRGCAC
Protein: Xrcc4-like factor 1 (Meiotically up-regulated gene 104 protein) (Non-homologous end-joining protein 1) (Q9P7J2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in non-homologous end joining (NHEJ) in the repair of double-strand DNA breaks (DSB). Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA ligase 4
- Non-homologous end-joining factor xrc4
- ATP-dependent DNA helicase II subunit 2
- ATP-dependent DNA helicase II subunit 1
- DNA polymerase type-X family protein pol4
Sequence:
MSWVQLRGHRFHFIQASFDAESNEAVQVIHITDLVRVWSCTCSRNQIVNQAESERCPIDPFQTFETLVDVLAEVLVNVSSESRIQLRGSNDEGSLKIFCTSKIAKDIFLEWNWTLWLTPPETIAKMVWFPLINHHLFESETDTSPGSLMSIIRDQKSLLNDKTWFKEALNERSSSSNPSTPRKRSAFADIISPKRPRTRYDFV
Protein: BMP/retinoic acid-inducible neural-specific protein 2 (Q6DFY8)
Organism: Mus musculus (Mouse)
Function: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRWPCSSWFRGLWPEAAPWAVLLALGVPGWVLAVSATVAAVVPEQHVSSAGQAPLDWLLTDRGPFHRAQEYADFMERYRQGFTTRYRIYREFARWKVNNLALERRDFFSLPLPLAPEFVRNIRLLGRRPNLQQVTENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSRKSETTGGIPVVGGTGNSSAVSLETLHQLAASYFIDRESTLRRLHHIQIATGAIKVTETRTGPLGCSNYDNLDSVSSVLVQSPENKVQLLGLQVLLPEHLRERFVAAALSYITCSSEGELVCRENDCWCKCSPTFPECNCPDADIQAMEDSLLQIQDSWATHNRQFEESEEFQTLLKRLPSDRFLNSTAISQYWTMDSNLQHRYQQLGASLKVLLKKMHRIVRRLFNLCKRCHRQPRFRLPKERSLSFWWNRIQSLLYCGESTFPGTFLEQSHSCTCPYDQSSCQGPIPCALGEGPACAHCASDNSTRCGSCNPGYVLAQGLCRPEVAESLENFLGLETDLQDLELKYLLQKRDSRIEVHSIFISNDMRLGSWFDPSWRKRMLLTLKSNKYKPGLVHVMLALSLQICLTKNSTLEPVMAIYVNPFGGSHSESWFMPVNEGNFPDWERTNVDAAAQCQNWTITLGNRWKTFFETVHVYLRSRIKSLDDSSNETIYYEPLEMTDPSKNLGYMKINTLQVFGYSLPFDPDAIRDLILQLDYPYTQGSQDSALLQLIELRDRVNQLSPPGKVRLDLFSCLLRHRLKLANNEVGRIQSSLRAFNSKLPNPVEYETGKLCS
Protein: Pawn, isoform C (A0A0B4KEW8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRKPQNLTHSIPSSRAGDRGGGGGGVGRGTSRPSAISNNRRPRDHRHLMAMVVSTLPLALLLLLVQTTAGQHESVSQISPKSSSHRSPDRQRIESTMADSVNGLAEGQSSPLDVNDNETRAERVERSASPILHDRQPIGPNDVHFPEDLEKDVSAGRYFHYNIKPTGTFDNQDEQPERTHQGIRAGKTLSQGGSSSEQSFLGRGDLRPLVSGSPIRPSPSNTATSATAASATQAPHSPRQNGNPDIQDIITGIVKLLNGNVNVHANTQGIRRPSASRINNRGPPRISEAQNLPIDYEAQKPGTSMRPPPYPFDRPERPFITGVPIPEQIVPVRPGFVSNRPPWYRNKPRPPIATSVGGNRRPLPQYKPLPAPPVQAPLQPQDPLDRKNEQEKEQNHQEQPQPTDDVVLPTDTTYDSEFSNEDANAQYIEVSDQDTDATGGEVEDELQPPPPPPSTTNNPPTTPTNPSKKKHKPKPGSEKKKLPEESPQDEGFSTIIETSSVVHTVMGMSSTYVPMSMDSSESLGLDPSTEEVIFMTANRTPTLEPSVTSSLGTSSSSNPASAIQPTSSKEHTKTTTTTTTTTSSSTSTTTSTTTPPSTESVSPNSSNANTNATPPAPYHPRPGIVLDDPEFKPGGRPRPPVQRPPAQQTLPLPAVQPTRQHLPPGYGEIFDVTLSAIQGPGPKGSGSQQTINIKPYGSYAAGGGQGDIIVSASDPPAGATTPATRLPQLPGSGSGSGSGSGTGSGGASTPGVGVSSGGGGGSGSSISPAAPANAVTQSSGGYVVPETEVVDLQGHSKPQGGAPTTNAGPTRPHYRQRPTQPPVRIDTCIVGDDSTCDQAQHERCKTDNGVSSCHCRPGYSRRKHREPCRRVISFHLGMRVDRIYEHRIVWDTKLMDKHSEPFGQLSYESIRALDSAMSMTPYSDEFMEAKVNNIYRGDPNLGGSGVYVNMTIKLDESVETLRPNLRSDVQKHLLGVLHRRNNNIGNSVLYVSSPEGAVSALQDLDECQSPELNDCHSGASCSNTWGSFRCACEAGLRDPWADQPARSGRECQACADSVCNNHGTCSYAEDGAQLCTCDSSHYGAQCEIDGEVLGVAIGASVAAIIIIVLTLVCLIMWSRRWQREQKNAMGSPVFGYMNTAPLKSAGLPQAGYQVTLEDRMRWAQIADVMAQTNHYGQAEPIGPTRPSSAMFAYPNLGAMGMGTLGGMSLQSTMQMHPSATLAPPVPLPRRLGLGPRSNGMRTLENSSSSEEEDRADLLGRNFQVPRPKSRSNGSIANQSGIYYDVDYEPSGNGIGNSSVDHLYGSQNQSVTHSSGHSHIPGPQGIPMSTYTSGRAPSSYYMK