wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-tRNA hydrolase 2 (PTH 2) (EC 3.1.1.29) (P34222)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Subcellular location: Cytoplasm.
Interaction partners:
- Peptidyl-tRNA hydrolase
- Ubiquitin domain-containing protein DSK2
- UV excision repair protein RAD23
- Increased recombination centers protein 22
Sequence:
MEKMTVSSNYTIALWATFTAISFAVGYQLGTSNASSTKKSSATLLRSKEMKEGKLHNDTDEEESESEDESDEDEDIESTSLNDIPGEVRMALVIRQDLGMTKGKIAAQCCHAALSCFRHIATNPARASYNPIMTQRWLNAGQAKITLKCPDKFTMDELYAKAISLGVNAAVIHDAGRTQIAAGSATVLGLGPAPKAVLDQITGDLKLY
Protein: Transcription factor LAF1 (Myb-related protein 18) (AtMYB18) (Protein LONG AFTER FAR-RED LIGHT 1) (Q9M0K4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that promotes photomorphogenesis in the light by participating in the transmission of phytochrome A (phyA) signals to downstream responses. Probably acts by activating expression of light-induced genes. In darkness, its degradation prevents the activation of light-induced genes.
Subcellular location: Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:11581165, ECO:0000269|PubMed:19482971}.
Interaction partners:
- Transcription factor HFR1
- Transcription factor HY5
- E3 ubiquitin-protein ligase COP1
- Transcription factor HY5-like
- Cullin-4
- Protein FAR-RED-ELONGATED HYPOCOTYL 1-LIKE
- Phytochrome A
- Protein FAR-RED ELONGATED HYPOCOTYL 1
- Protein SUPPRESSOR OF PHYA-105 1
- B-box zinc finger protein 22
Sequence:
MAKTKYGERHRKGLWSPEEDEKLRSFILSYGHSCWTTVPIKAGLQRNGKSCRLRWINYLRPGLKRDMISAEEEETILTFHSSLGNKWSQIAKFLPGRTDNEIKNYWHSHLKKKWLKSQSLQDAKSISPPSSSSSSLVACGKRNPETLISNHVFSFQRLLENKSSSPSQESNGNNSHQCSSAPEIPRLFFSEWLSSSYPHTDYSSEFTDSKHSQAPNVEETLSAYEEMGDVDQFHYNEMMINNSNWTLNDIVFGSKCKKQEHHIYREASDCNSSAEFFSPSTTT
Protein: V-myb myeloblastosis viral oncogene homologue (Avian) (V-myb myeloblastosis viral oncogene homolog (Avian), isoform CRA_d) (Q708E1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQATKAQRLFQF
Protein: Metacaspase-2 (AtMC2) (EC 3.4.22.-) (Metacaspase 1c) (AtMCP1c) (Q7XJE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a negative regulator of oxidative stress cell death and hypersensitive cell death response mediated by immune response. Acts via indirect or direct regulation of AMC1 at postranscriptional level.
Interaction partners:
- Uncharacterized protein
- Cathepsin B-like protease 1
- Cathepsin B-like protease 2
Sequence:
MLLLVDCSSCRTPLHLPPGATRIRCAICHAFTLIAPEPRLQSHASASPFPFPNSSPAPSTFIYPPPTPSPYTHAPHAPSPFNHAPPDSYPFTHAPPASSPFNHAPPGPPPPVHGQKRAVIVGVSYKNTKDELKGCINDANCMKFMLMKRFQFPESCILMLTEEEADPMRWPTKNNITMAMHWLVLSCKPGDSLVFHFSGHGNNQMDDNGDEVDGFDETLLPVDHRTSGVIVDDEINATIVRPLPYGVKLHAIVDACHSGTVMDLPYLCRMDRLGNYEWEDHRPKTGMWKGTSGGEVFSFTGCDDDQTSADTPQLSGSAWTGAMTYAFIQAIERGHGMTYGSLLNAMRSTVHEIFDKNKGRELVEVGGADFLSTLLGLLILGASPPDEEEEVNQAPQKTQEPQLSANEAFAVYEKPFSL
Protein: Extracellular calcium-sensing receptor (CaSR) (Parathyroid cell calcium-sensing receptor) (PCaR1) (RaKCaR) (P48442)
Organism: Rattus norvegicus (Rat)
Function: G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system (By similarity). The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P41180}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41180}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- G-protein coupled receptor family C group 6 member A
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
Sequence:
MASYSCCLALLALAWHSSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQDLKSRPESVECIRYNFRGFRWLQAMIFAIEEINSSPSLLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQYKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQQVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGRIWLASEAWASSSLIAMPEYFHVVGGTIGFGLKAGQIPGFREFLQKVHPRKSVHNGFAKEFWEETFNCHLQEGAKGPLPVDTFVRSHEEGGNRLLNSSTAFRPLCTGDENINSVETPYMDYEHLRISYNVYLAVYSIAHALQDIYTCLPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTNNMGEQVTFDECGDLVGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCQAGTRKGIIEGEPTCCFECVECPDGEYSGETDASACDKCPDDFWSNENHTSCIAKEIEFLAWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQILICIIWLYTAPPSSYRNHELEDEIIFITCHEGSLMALGSLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKVYIILFKPSRNTIEEVRSSTAAHAFKVAARATLRRPNISRKRSSSLGGSTGSIPSSSISSKSNSEDRFPQPERQKQQQPLSLTQQEQQQQPLTLHPQQQQQPQQPRCKQKVIFGSGTVTFSLSFDEPQKNAMAHRNSMRQNSLEAQRSNDTLGRHQALLPLQCADADSEMTIQETGLQGPMVGDHQPEMESSDEMSPALVMSTSRSFVISGGGSSVTENVLHS
Protein: N-acetylglucosamine-1-phosphotransferase subunit gamma (GlcNAc-1-phosphotransferase subunit gamma) (UDP-N-acetylglucosamine-1-phosphotransferase subunit gamma) (Q9UJJ9)
Organism: Homo sapiens (Human)
Function: Non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. Binds and presents the high mannose glycans of the acceptor to the catalytic alpha and beta subunits (GNPTAB). Enhances the rate of N-acetylglucosamine-1-phosphate transfer to the oligosaccharides of acid hydrolase acceptors.
Subcellular location: Secreted {ECO:0000269|PubMed:15532026}. Golgi apparatus {ECO:0000269|PubMed:15532026, ECO:0000269|PubMed:26108976, ECO:0000269|PubMed:27038293}.
Interaction partners:
- N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
- N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
- Neutral alpha-glucosidase AB
Sequence:
MAAGLARLLLLLGLSAGGPAPAGAAKMKVVEEPNAFGVNNPFLPQASRLQAKRDPSPVSGPVHLFRLSGKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIANNTFTGMWMRDGDACRSRSRQSKVELACGKSNRLAHVSEPSTCVYALTFETPLVCHPHALLVYPTLPEALQRQWDQVEQDLADELITPQGHEKLLRTLFEDAGYLKTPEENEPTQLEGGPDSLGFETLENCRKAHKELSKEIKRLKGLLTQHGIPYTRPTETSNLEHLGHETPRAKSPEQLRGDPGLRGSL
Protein: Transcriptional activator, putative (B9WN82)
Organism: Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast)
Interaction partners:
Sequence:
MSANLQIKLEDALDDILKSAGFMFEIINHNREQSNLIAGPNNELIQQSIVQQLNDNIQKFNDILDQTVSKFNDAKWCVAVMIENKQKLEELKIKEDGERQKRDAEAKRLKKEMKAKKKAEKEAKAAAKAREKEEKAAAKVKEEQAKAAAKVKEEQAKAAAKVKEEQAKAAAKAREEETKAAAKAREEQAKAATRAREEQARAVAIEKMKEVAAKTKAAMEREKREKEALKKKAEEEARAAARAREEKQKFDNFDDFLGIDIPDADETIDEDMLSSMNYEDLGLDNPIQASPNALQTQTIDDTPMGTDSASLDLNNILDNDESILAGLNMNLLDDANTFNDNEEFDVDSFLNQFGN
Protein: Ras-related protein Rab-5A (EC 3.6.5.2) (Q9CQD1)
Organism: Mus musculus (Mouse)
Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Active GTP-bound form is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes. Contributes to the regulation of filopodia extension. Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan (By similarity). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P18066}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000269|PubMed:25869668}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P20339}. Cell projection, ruffle {ECO:0000250|UniProtKB:P18066}. Membrane {ECO:0000250|UniProtKB:P20339}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20339}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:18425118}. Endosome membrane {ECO:0000250|UniProtKB:P20339}. Note=Enriched in stage I melanosomes. Alternates between membrane-bound and cytosolic forms. {ECO:0000250|UniProtKB:P20339}.
Interaction partners:
- Early endosome antigen 1
- Rab5 GDP/GTP exchange factor
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Ras-related protein Rab-5B
- Rabenosyn-5
- Alsin
- Ras and Rab interactor 1
- Vacuolar protein sorting-associated protein 45
- Beclin-1
- Rab GDP dissociation inhibitor alpha
Sequence:
MANRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQRQASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKKLPKNEPQNPGANSARGRGVDLTEPAQPARSQCCSN
Protein: Pre-mRNA-splicing factor CWC26 (Bud site selection protein 13) (Complexed with CEF1 protein 26) (Synthetic lethal with CLF1 protein 7) (P46947)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for efficient splicing and pre-mRNA nuclear retention. May also be involved in positioning the proximal bud pole signal.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Pre-mRNA-processing factor 19
- Pre-mRNA leakage protein 1
- Pre-mRNA-splicing factor SNT309
- Pre-mRNA-splicing factor CWC2
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing helicase BRR2
- U2 snRNP component IST3
- Pre-mRNA-splicing factor CWC22
- Pre-mRNA-processing protein 45
- Cold sensitive U2 snRNA suppressor 1
Sequence:
MALHQYLSETYGPTKPKNKTKKKKKESKSDANSDKTSLIVKERLSTLQQEQEKSGVASFSKFDKQKSKNIWKNLETNELSHAITHPSASSITGNESKNDLKEIRAQEPLVTVADKSKTRKTIYRDAQGHKIQEDSKIDDSSFSRSKYEDEKAAEREQYLKNLNMGDVQKLGINVDAHDKKKNQTASSLTIEDPAITFTHDKERTVKTSLLGRKLYDKPAPENRFAIMPGSRWDGVHRSNGFEEKWFAKQNEINEKKVQSYTLQEDY
Protein: Probable N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase (EC 3.5.1.89) (Q9HDW9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15
- N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein gpi1
- Meiotically up-regulated gene 84 protein
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GPI transamidase component gaa1
- GPI-anchor transamidase
- GPI-anchored wall transfer protein 1
- D-arabinono-1,4-lactone oxidase
Sequence:
MIWFWSTLLVTAIAVLSTANESSSGQEKLAVESILFVFAHPDDESMFFGPTIDYLGNQHSTRVHVLCLSNGNADGLGSVREKELVVAASKYQIDKTNVHVVSDPQLQDGMQAKWDPTDVAKHISQIIERYNIKTLITFDNKGISGHPNHIACYEGAMKIVKATPQVQVFVLESVNIFRKYISYLDTIPTLVQSQAGRNDTIIIHADRKSTQRIRDAMVRGHKSQMVWFRYGWIYLSKYMSNNVLKRAT
Protein: Gigaxonin (Kelch-like protein 16) (Q9H2C0)
Organism: Homo sapiens (Human)
Function: Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB. Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton.
Interaction partners:
- Cullin-3
- Microtubule-associated protein 1B
- E3 ubiquitin-protein ligase RBX1
- Kelch repeat and BTB domain-containing protein 8
- Ectoderm-neural cortex protein 1
- Kelch-like protein 3
- Kelch-like protein 9
- Kelch-like protein 12
- Kelch-like protein 41
- Kelch-like protein 42
Sequence:
MAEGSAVSDPQHAARLLRALSSFREESRFCDAHLVLDGEEIPVQKNILAAASPYIRTKLNYNPPKDDGSTYKIELEGISVMVMREILDYIFSGQIRLNEDTIQDVVQAADLLLLTDLKTLCCEFLEGCIAAENCIGIRDFALHYCLHHVHYLATEYLETHFRDVSSTEEFLELSPQKLKEVISLEKLNVGNERYVFEAVIRWIAHDTEIRKVHMKDVMSALWVSGLDSSYLREQMLNEPLVREIVKECSNIPLSQPQQGEAMLANFKPRGYSECIVTVGGEERVSRKPTAAMRCMCPLYDPNRQLWIELAPLSMPRINHGVLSAEGFLFVFGGQDENKQTLSSGEKYDPDANTWTALPPMNEARHNFGIVEIDGMLYILGGEDGEKELISMECYDIYSKTWTKQPDLTMVRKIGCYAAMKKKIYAMGGGSYGKLFESVECYDPRTQQWTAICPLKERRFGAVACGVAMELYVFGGVRSREDAQGSEMVTCKSEFYHDEFKRWIYLNDQNLCIPASSSFVYGAVPIGASIYVIGDLDTGTNYDYVREFKRSTGTWHHTKPLLPSDLRRTGCAALRIANCKLFRLQLQQGLFRIRVHSP
Protein: Globin-like protein 6 (Q18086)
Organism: Caenorhabditis elegans
Function: May play a role as physiological sensor for oxygen via redox signaling and/or electron transport.
Interaction partners:
- Globin-like protein 26
- Globin-like protein
- GLOBIN domain-containing protein
- Globin domain-containing protein
- Globin domain-containing protein
- GLoBin related
- Globin domain-containing protein
- Globin domain-containing protein
- Globin domain-containing protein
- GLOBIN domain-containing protein
Sequence:
MGNQSTKSTHGTTRVSHSKSAHHNSSRVTSDVIPRSASAISSHERFFSDSQSSSPPAVCPVSAPGKYRNFPGKDVPPICLTDEYNNSDDEVFCSTRTSKQSPLATGCPRQNLGSPGNRRSVDSTNSDLLEAVTPRSHISVKRTVSSGTEHAPDHANMQKSSSLKFTRPGVRSETKETTPSTSSNPTMFPCIHQFLHLTQPQILFVRKTWNHARNQGALEPAISIFRNSFFKNPEIRQMIMFGTKNEGHERLKKHAQLFTVLMDDLIANLDSPSATVAGLREAGEKHVWPTRNQYGCPFHAHLLDQFATAMIERTLEWGEKKDRTETTQRGWTKIVLFVTEQLKEGFQDEQKRARRIKAQIKTSAGSSSFEISTKTKQSDMKRFHTLDNM
Protein: Photosystem-II repair protein (A1YSB4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Interaction partners:
Sequence:
MATMLARRASLLPRGARPCFVASRVAPRLASRGVPVVFAAKQGSPAASKSQQYQPTSARDAIERGTEVFKNQNNLDEAVRLYRVGLEMQPNDDEARAALYNLGCALTKQKKFSEAVEAIERAINDYGLKLIVALRDDDLRLLRERREWMDALGRMKGGMSRQTKADLRTEAKAPFRLPRLILFGGLLAGAGLGLMVILTRLAKSLQGGPDAPDLNESLTNLGINVTAVAVLSWLVYRDVSSKQAELRITTREEGLGRLQVDLGKDRVLPLLKFRGQVRPVIVAGSRSFVEKAIKEAEGQYLNLRDRAVSVVPIIFEKAQAVELDPEDKLRLLKKEFAKEGAKGFGDESAKKAASEPKAKKVSVLGGLVEADKKWRLEAYDTDEWKAWILEQKEFSGLSTTEPNCYIQVQLDGTVRSSGTGSPPWDKLVEELPLLSDFRTRLTDGVGPQE
Protein: Ribonuclease J (RNase J) (EC 3.1.-.-) (A0QVT2)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: An RNase that has endonuclease and 5'-3' exonuclease activity. The 5'-exonuclease activity acts on 5'-monophosphate but not 5'-triphosphate ends. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Plays the major role in pre-23S rRNA maturation, and a minor role in processing of pre-5S and pre-16S rRNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01491}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- 4-hydroxy-tetrahydrodipicolinate synthase
- Oligoribonuclease
- Ribonuclease E
- Flavin-dependent thymidylate synthase
- 8-oxo-
- Endoribonuclease YbeY
- Ribonuclease 3
- Ribonuclease Z
- Small ribosomal subunit protein uS15
Sequence:
MSAELAPPPPLAPGGLRVTALGGISEIGRNMTVFEHLGRLLIVDCGVLFPGHDEPGVDLILPDLRHIEDRLDEIEALVVTHAHEDHIGAIPFLLKLRPDIPVVGSKFTIALVREKCREHRLKPKFVEVAERQSSQHGVFECEYFAVNHSIPGCLAVAIHTGAGTVLHTGDIKLDQLPLDGRPTDLPGMSRLGDAGVDLFLCDSTNSEHPGVSPSESEVGPTLHRLIRGAEGRVIVACFASNVDRVQQIIDAAVALGRRVSFVGRSMVRNMGIARELGYLKVDDSDILDIAAAEMMPPDRVVLITTGTQGEPMAALSRMSRGEHRSITLTSGDLIILSSSLIPGNEEAVYGVIDSLSKIGARVVTNAQARVHVSGHAYAGELLFLYNGVRPRNVMPVHGTWRHLRANAALAASTGVPPENIVLAENGVSVDLVAGRASISGAVTVGKMFVDGLITGDVGDATLGERLILSSGFVSITVVVHRGTGRPAGPAHLISRGFSEDPKALEPVAQKVERELEALAADNVTDPTRIAQAVRRTVGKWVGETYRRQPMIVPTVIEI
Protein: Activating signal cointegrator 1 complex subunit 1 (ASC-1 complex subunit p50) (Trip4 complex subunit p50) (Q8N9N2)
Organism: Homo sapiens (Human)
Function: Plays a role in DNA damage repair as component of the ASCC complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation. In cells responding to gastrin-activated paracrine signals, it is involved in the induction of SERPINB2 expression by gastrin. May also play a role in the development of neuromuscular junction.
Subcellular location: Nucleus {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:26924529}. Nucleus speckle {ECO:0000269|PubMed:29997253}. Note=Colocalizes with PRPF8 in nuclear speckles in the absence of DNA damage. {ECO:0000269|PubMed:29997253}.
Interaction partners:
- Activating signal cointegrator 1 complex subunit 2
- Activating signal cointegrator 1 complex subunit 3
- Activating signal cointegrator 1
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 3
- Small ribosomal subunit protein mS29
- Endoribonuclease YbeY
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL46
Sequence:
MEVLRPQLIRIDGRNYRKNPVQEQTYQHEEDEEDFYQGSMECADEPCDAYEVEQTPQGFRSTLRAPSLLYNLIHLNTSNDCGFQKITLDCQNIYTWKSRHIVGKRGDTRKKIEMETKTSISIPKPGQDGEIVITGQHRNGVISARTRIDVLLDTFRRKQPFTHFLAFFLNEVEVQEGFLRFQEEVLAKCSMDHGVDSSIFQNPKKLHLTIGMLVLLSEEEIQQTCEMLQQCKEEFINDISGGKPLEVEMAGIEYMNDDPGMVDVLYAKVHMKDGSNRLQELVDRVLERFQASGLIVKEWNSVKLHATVMNTLFRKDPNAEGRYNLYTAEGKYIFKERESFDGRNILKSFALLPRLEYNDAISAHCNLCLPGSSDSPASASQVAGITGVSDAYSQSLPGKS
Protein: Phosphate-specific transport system accessory protein PhoU homolog (Pst system accessory protein PhoU homolog) (Q51547)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Plays a role in the regulation of phosphate uptake.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphate transport system permease protein PstA
- Phosphate import ATP-binding protein PstB
- Phosphate-binding protein PstS
- Membrane protein component of ABC phosphate transporter
- Phosphate regulon transcriptional regulatory protein PhoB
- Phosphate regulon sensor protein PhoR
- Alkaline phosphatase L
- Exopolyphosphatase
- Phosphonates import ATP-binding protein PhnC 2
- Phosphonate transport protein PhnE
Sequence:
MINKDSLTHHISQQFNAELEDVRSHLLAMGGLVEKQVNDAVNALIDADSGLAQQVREIDDQINQMERNIDEECVRILARRQPAASDLRLIISISKSVIDLERIGDEASKVARRAIQLCEEGESPRGYVEVRHIGSQVQKMVQEALDAFARFDADLALSVAQYDKTVDREYKTALRELVTYMMEDPRAISRVLNIIWALRSLERIGDHARNIAELVIYLVRGTDVRHIGLTRMKEEVENNRGE
Protein: 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic (HTPA synthase 2) (EC 4.3.3.7) (Q9FVC8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Subcellular location: Plastid, chloroplast.
Interaction partners:
- 4-hydroxy-tetrahydrodipicolinate reductase 2, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate reductase 1, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
- aspartate-semialdehyde dehydrogenase
- Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
- Aspartokinase 1, chloroplastic
- Aspartokinase 2, chloroplastic
- Folate synthesis bifunctional protein
- Folate synthesis bifunctional protein
- Aspartokinase 3, chloroplastic
Sequence:
MAALKGYGLCSMDSALQFPCPKLFNSYKRRSSKWVSPKAAVVPNFHLPMRSLEVKNRTNTDDIKALRVITAIKTPYLPDGRFDLEAYDDLVNIQIQNGAEGVIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGSIKVIGNTGSNSTREAIHATEQGFAVGMHAALHINPYYGKTSIEGLIAHFQSVLHMGPTIIYNVPGRTGQDIPPRAIFKLSQNPNLAGVKECVGNKRVEEYTENGVVVWSGNDDECHDSRWDYGATGVISVTSNLVPGLMRKLMFEGRNSSLNSKLLPLMAWLFHEPNPIGINTALAQLGVSRPVFRLPYVPLPLSKRLEFVKLVKEIGREHFVGEKDVQALDDDDFILIGRY
Protein: Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] (P19221)
Organism: Mus musculus (Mouse)
Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).
Interaction partners:
- Fibrinogen alpha chain
- Heparin cofactor 2
- Antithrombin-III
- Thrombomodulin
- Proteinase-activated receptor 1
- Fibrinogen gamma chain
- Fibrinogen beta chain
- Platelet glycoprotein Ib alpha chain
- Proteinase-activated receptor 4
- Proteinase-activated receptor 3
Sequence:
MSHVRGLGLPGCLALAALVSLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERECVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGVNYLGTVNVTHTGIQCQLWRSRYPHKPEINSTTHPGADLKENFCRNPDSSTTGPWCYTTDPTVRREECSVPVCGQEGRTTVVMTPRSGGSKDNLSPPLGQCLTERGRLYQGNLAVTTLGSPCLPWNSLPAKTLSKYQDFDPEVKLVENFCRNPDWDEEGAWCYVAGQPGDFEYCNLNYCEEAVGEENYDVDESIAGRTTDAEFHTFFNEKTFGLGEADCGLRPLFEKKSLKDTTEKELLDSYIDGRIVEGWDAEKGIAPWQVMLFRKSPQELLCGASLISDRWVLTAAHCILYPPWDKNFTENDLLVRIGKHSRTRYERNVEKISMLEKIYVHPRYNWRENLDRDIALLKLKKPVPFSDYIHPVCLPDKQTVTSLLRAGYKGRVTGWGNLRETWTTNINEIQPSVLQVVNLPIVERPVCKASTRIRITDNMFCAGFKVNDTKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRKGKYGFYTHVFRLKRWIQKVIDQFG