wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase subunit gamma-1 (EC 2.7.7.7) (3'-5' exodeoxyribonuclease) (EC 3.1.11.-) (5'-deoxyribose-phosphate lyase) (EC 4.2.99.-) (Mitochondrial DNA polymerase catalytic subunit) (PolG-alpha) (PolgA) (P54099)
Organism: Mus musculus (Mouse)
Function: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P54098}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:P54098}.
Interaction partners:
- DNA polymerase subunit gamma-2
- Twinkle mtDNA helicase
- Single-stranded DNA-binding protein, mitochondrial
- Transcription factor A, mitochondrial
- DNA polymerase epsilon catalytic subunit A
- DNA-directed RNA polymerase, mitochondrial
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA primase small subunit
- DNA polymerase zeta catalytic subunit
- Ribonuclease H1
Sequence:
MSRLLWKKVAGAKVASGPVPATARWVASSVLDPVPSDGRPPSQMPSSENGQLRLNPLLIQMLSRGLHEQIFGCGGEMPDEAAVQRSVEHLQKHGLWGQPATPLPDVELRLPRLFGGNLDQHFRLLAQKQSLPYLEAAASLLEAQLPPEPKSWAWAEGWTRYGPEGEAEPVAIPEERALVFDVEVCLAEGTCPTLAVAISPSAWYSWCSRRLVEERYSWTSQLSPADLIPLGGSTSASSSTKQDGQEQLVVGHNVSFDRAHIREQYLIQDSRMRFLDTMSMHMAISGLSSFQRSLWMGAKQGKHKNPAAHKARAEVPEESQWSSESSSWDWMDISSANNLADVHNLYVGGPPLEKEPRELFVKGSMRDIRENFQDLMQYCARDVWATFEVFQQQLPLFLERCPHPVTLAGMLEMGVSYLPVNQNWERYLTEAQNTYEELQREMKKSLMDLANDACQLLSGERYKEDPWLWDLEWDLQEFKQKKAKKVKKPASASKLPIEGAGPFGDPMDQEDPGPPSEEEELQRSVTAHNRLQQLRSTTDLLPKRPQHLPGHPGWYRQLCPRLDDPAWAPGPSLLSLQMRVTPKLMALTWDGFPLHYSDSHGWGYLVPGRRDNLTEPPVSPTVESAAVTCPYRAIESLYRKHCLEQGKQQLEPQEVDLAEEFLLTDNSAMWQTVEELGCLDVEAEAKMENSGLSQPLVLPAACAPKSSQPTYHHGNGPYNDVNIPGCWFFKLPHKDGNNYNVGSPFAKDFLPKMEDGTLQAGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRVVTRHPAFDEEGHYGAILPQVVTAGTITRRAVEPTWLTASNARPDRVGSELKAMVQAPPGYVLVGADVDSQELWIAAVLGDAHFAGMHGCTAFGWMTLQGRKSRGTDLHSKTAATVGISREHAKIFNYGRIYGAGQSFAERLLMQFNHRLTRQEAAEKAQQMYAVTKGLRRYRLSADGEWLVKQLNLPVDRTEDGWVSLQDLRMIRREASRKSRWKKWEVAAERAWTGGTESEMFNKLESIAMSDTPRTPVLGCCISRALEPSVVQGEFITSRVNWVVQSSAVDYLHLMLVAMKWLFEEFAIDGRFCISIHDEVRYLVREEDRYRAALALQITNLLTRCMFAYKLGLNDLPQSVAFFSAVDIDQCLRKEVTMDCKTPSNPTGMERRYGIPQGEALDIYQIIELTKGSLEKRSQPGP
Protein: Putative glutamate--cysteine ligase 2 (EC 6.3.2.2) (Gamma-glutamylcysteine synthetase 2) (GCS 2) (Gamma-GCS 2) (P77213)
Organism: Escherichia coli (strain K12)
Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate.
Interaction partners:
- Glutamate--cysteine ligase
- Glutathione synthetase
- Glutathione hydrolase proenzyme
- 5-oxoprolinase subunit B
- Cytosol aminopeptidase
- Aminopeptidase N
- Cytosol non-specific dipeptidase
- 5-oxoprolinase subunit C
- 5-oxoprolinase subunit A
- Peptidase B
Sequence:
MPLPDFHVSEPFTLGIELEMQVVNPPGYDLSQDSSMLIDAVKNKITAGEVKHDITESMLELATDVCRDINQAAGQFSAMQKVVLQAATDHHLEICGGGTHPFQKWQRQEVCDNERYQRTLENFGYLIQQATVFGQHVHVGCASGDDAIYLLHGLSRFVPHFIALSAASPYMQGTDTRFASSRPNIFSAFPDNGPMPWVSNWQQFEALFRCLSYTTMIDSIKDLHWDIRPSPHFGTVEVRVMDTPLTLSHAVNMAGLIQATAHWLLTERPFKHQEKDYLLYKFNRFQACRYGLEGVITDPHTGDRRPLTEDTLRLLEKIAPSAHKIGASSAIEALHRQVVSGLNEAQLMRDFVADGGSLIGLVKKHCEIWAGD
Protein: Coiled-coil domain-containing protein 93 (Q567U6)
Organism: Homo sapiens (Human)
Function: Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes and is dependent on its interaction with WASHC2C.
Subcellular location: Early endosome {ECO:0000305|PubMed:25355947}.
Interaction partners:
- Coiled-coil domain-containing protein 22
- VPS35 endosomal protein-sorting factor-like
- COMM domain-containing protein 1
- Vacuolar protein sorting-associated protein 26C
- COMM domain-containing protein 10
- COMM domain-containing protein 9
- COMM domain-containing protein 6
- Vacuolar protein sorting-associated protein 29
- COMM domain-containing protein 2
- COMM domain-containing protein 5
Sequence:
MGLPRGPEGQGLPEVETREDEEQNVKLTEILELLVAAGYFRARIKGLSPFDKVVGGMTWCITTCNFDVDVDLLFQENSTIGQKIALSEKIVSVLPRMKCPHQLEPHQIQGMDFIHIFPVVQWLVKRAIETKEEMGDYIRSYSVSQFQKTYSLPEDDDFIKRKEKAIKTVVDLSEVYKPRRKYKRHQGAEELLDEESRIHATLLEYGRRYGFSRQSKMEKAEDKKTALPAGLSATEKADAHEEDELRAAEEQRIQSLMTKMTAMANEESRLTASSVGQIVGLCSAEIKQIVSEYAEKQSELSAEESPEKLGTSQLHRRKVISLNKQIAQKTKHLEELRASHTSLQARYNEAKKTLTELKTYSEKLDKEQAALEKIESKADPSILQNLRALVAMNENLKSQEQEFKAHCREEMTRLQQEIENLKAERAPRGDEKTLSSGEPPGTLTSAMTHDEDLDRRYNMEKEKLYKIRLLQARRNREIAILHRKIDEVPSRAELIQYQKRFIELYRQISAVHKETKQFFTLYNTLDDKKVYLEKEISLLNSIHENFSQAMASPAARDQFLRQMEQIVEGIKQSRMKMEKKKQENKMRRDQLNDQYLELLEKQRLYFKTVKEFKEEGRKNEMLLSKVKAKAS
Protein: Sodium/hydrogen exchanger 6 (Na(+)/H(+) exchanger 6) (NHE-6) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 6) (A1L3P4)
Organism: Mus musculus (Mouse)
Function: Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo. Plays a critical role during neurodevelopment by regulating synaptic development and plasticity. Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH (By similarity). Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q92581}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:23303939, ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:24035762}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17005858}; Multi-pass membrane protein {ECO:0000255}. Note=Present predominantly in the recycling compartments including early and recycling endosomes, but undergoes plasma membrane localization during vesicular recycling, which is enhanced upon certain stimuli, such as hypoxia. {ECO:0000250|UniProtKB:Q92581}.
Interaction partners:
- Sodium/hydrogen exchanger 7
- Sodium/hydrogen exchanger 9B2
Sequence:
MAGARRGWRLAPVRRGVCGPRARPLMRPLWLLFAVSFFGWTGALDGSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTALVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFIAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGNSSEDALDRELTFGDHELVIRGTRLVLPMDDSEPALNSLDDTRHSPA
Protein: Ribosome biogenesis protein 15 (Nucleolar protein 15) (P53927)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the biogenesis of the 60S ribosomal subunit. Required for pre-rRNA processing and cytokinesis. Associates with the precursors of the 25S and 5.8S rRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11583614}. Nucleus, nucleolus {ECO:0000269|PubMed:10953080, ECO:0000269|PubMed:11583614}.
Interaction partners:
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein RPF2
- ATP-dependent rRNA helicase SPB4
- ATP-dependent RNA helicase HAS1
- Protein MAK16
- Pescadillo homolog
- 25S rRNA
- Nucleolar complex protein 2
- rRNA-processing protein EBP2
- Ribosome biogenesis protein BRX1
Sequence:
MVKSTSKTSTKETVTKQPTEEKPIQEKEELALETSSSSSDEEDEKDEDEIEGLAASDDEQSGTHKIKRLNPKKQANEKKSKDKKTLEEYSGIIYVSRLPHGFHEKELSKYFAQFGDLKEVRLARNKKTGNSRHYGFLEFVNKEDAMIAQESMNNYLLMGHLLQVRVLPKGAKIEKLYKYKKRVLVEKGITKPVKQLKDNMKQKHEERIKKLAKSGIEFKW
Protein: Oleosin 21.2 kDa (Oleosin type 2) (Q39165)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth (By similarity).
Subcellular location: Lipid droplet {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface (By similarity). {ECO:0000250}.
Interaction partners:
- 12S seed storage protein CRC
- 12S seed storage protein CRB
- 2S seed storage protein 3
- Peroxygenase 2
- Peroxygenase 1
- Glycine-rich protein family
- 12S seed storage protein CRA1
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Zinc finger CCCH domain-containing protein 17
- Late embryogenesis abundant protein
Sequence:
MADTHRVDRTDRHFQFQSPYEGGRGQGQYEGDRGYGGGGYKSMMPESGPSSTQVLSLLIGVPVVGSLLALAGLLLAGSVIGLMVALPLFLLFSPVIVPAALTIGLAMTGFLASGMFGLTGLSSISWVMNYLRGTRRTVPEQLEYAKRRMADAVGYAGQKGKEMGQHVQNKAQDVKQYDISKPHDTTTKGHETQGRTTAA
Protein: Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase) (P25704)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9931306}. Note=Localized to the Z line (By similarity). Some colocalization with CKM at M-band. {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase
- phosphoglycerate mutase
- Pyruvate kinase
- Fructose-bisphosphate aldolase A
- Bisphosphoglycerate mutase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Phosphoenolpyruvate carboxykinase, mitochondrial
- Phosphoenolpyruvate carboxykinase, cytosolic
- Phosphoglycerate kinase
Sequence:
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVEHINKTLGPALLEKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNHDLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFHRNGKYDLDFKSPDDPARHITGQKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVDIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAVFAGRKFRNPKAK
Protein: Phosphofructokinase-P (O14943)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAGMNAGVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITEKLKEARGRGKKFTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQPWSV
Protein: Vasoactive intestinal peptide (VIP) (Vasoactive intestinal polypeptide) (P63289)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: VIP causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder.
Subcellular location: Secreted.
Interaction partners:
Sequence:
HSDAVFTDNYTRLRKQMAVKKYLNSILN
Protein: Histone chaperone ASF1A (Anti-silencing function protein 1 homolog A) (hAsf1) (hAsf1a) (CCG1-interacting factor A) (CIA) (hCIA) (Q9Y294)
Organism: Homo sapiens (Human)
Function: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks: acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51. Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.
Subcellular location: Nucleus {ECO:0000269|PubMed:11897662, ECO:0000269|PubMed:12842904}. Chromosome {ECO:0000269|PubMed:29478807}.
Interaction partners:
- Ubinuclein-1
- Protein HIRA
- Histone H3.3
- Histone H3.1
- Calcineurin-binding protein cabin-1
- Serine/threonine-protein kinase tousled-like 2
- Histone H3.1t
- Histone H3.2
- Histone H4
- Nuclear autoantigenic sperm protein
Sequence:
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
Protein: DNA helicase II (EC 5.6.2.4) (DNA 3'-5' helicase II) (Q02322)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: May process damage occurring in non-replicating regions of DNA to produce recombinational intermediates for sister strand recombinational exchange.
Interaction partners:
- ATP-dependent DNA helicase RecQ
- DNA mismatch repair protein MutL
- UvrABC system protein B
- Beta sliding clamp
- Protein RecA
- DNA polymerase I
- UvrABC system protein A
Sequence:
MMDISELLDGLNDKQRERVAAPLGNHLVLAGAGSGKTRVLTHRIAWLIAVENISEGSIMAVTFTNKAAAEMRHRIQSTLAKHAQHQLFGMWIGTFHSIAHRLLRAHHLDVGLPQDFQILDSEDQLRLIKRLLKLHNFDEKAFPPKQACWYINNKKDEGLRPNDIEDFNDRQEREWIKIYQIYQDTCDRAGLVDFAELLIRVYELFEKKPLILQRYQQRFQHILVDEFQDTNKIQYKWIKILAGKTGQVMIVGDDDQSIYGWRGAQIENIQKFLKDFKAETIRLEQNYRSTANILNSANELIANNSDRLGKNLWTEGEKGDPVGIYSAFNELDEAKFVASQIQDWVEHGGKLDDCAVLYRSNSQSRVIEEALIRCQIPYRIYGGMRFFERQEIKDALAYLRLINNRQDDAAFERVINTPTRGIGDRTLDILRNLTRERQITLWQAVQVATQENMLAGRASTALLRFQELINSLQLDTAEMPLFAQTDFVIKHSGLYEMYQQEKGEKGEVRIENLEELVTATREFIKPDNAEEMTELTAFLTHASLEAGEEQASPHQSCVEMMTLHSAKGLEFPRVFMVGVEEGLFPSFRSFEEPGRLEEERRLAYVGITRAKKKLTISYAESRRLYAKEERHLPSRFIAELPRECIQEIRLRGTVTRAMNLAKVGSLSNTSAVENEWKMGQKVKHEKFGFGTVINVEGSENNTRLQIAFQAQGIKWLIAHLAKLEKVR
Protein: Protein ecdysoneless homolog (Q9LSM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AAR2 protein family
- Pre-mRNA-processing-splicing factor 8B
- Pre-mRNA-processing-splicing factor 8A
- At5g08320
- Paired amphipathic helix SIN3-like protein
- DnaJ protein ERDJ2B
- HIT-type Zinc finger family protein
- DExH-box ATP-dependent RNA helicase DExH12
- DnaJ protein ERDJ2A
- DExH-box ATP-dependent RNA helicase DExH13
Sequence:
MSKPSSSPFFSETTSRLQDETVFFSLFPDSSLSSAALQSLHLEIIDFVSPFTSPYIWQHEPFSLSIALSSSCACTNTAIPHLHGKLKYGDNLEDEWFAVFLLFRISAAFPSNSIRVWDTDGEFLLIEAAFHLPRWLNPETSLNRVFIRGGDLHIVPRSRLPDPSLVASLRFLIERGNESRASDSVQSALKNRISDYPERAWRNMHRVRVRVPVSVAQVIRHEPFLISLAVEGFYDRDMDSMKHAAKMEKFLSKGREEKLVLVLVKMSRAMYGQLVQQKFQAPNCYPMPSVSDRDAFSEAELGMKIACGMEMMYQQRKKEGEDGKGISWSKYKDNLEKYGYFEGLLSGSKEYKRLMENAEEYHQKSSSFSRTRDIMSAPVRRIDEILALPYSEDDFKGQEVPASDNDSWLYDGEDELNSVLQERQKEMEFYNSKKERKNKGKEKQEAGSSSDANMNNFDLGDISKSMQQFMHKVSSYKGAEVPENRDFKEVSIDVDRFMKDIESMLGSQGRDEQADDDSDGSEGSSMDMDFDDVEDDSEGEESNEDAKESFEESYYGAMNEELKNSTLEKSFENVNQQHSSKQNEESSKTRDEKDDEFTPVDADFNLVKNLLESYSSQQGLPGPASNLLGLMGLQLPKDSGDKN
Protein: Palmitoyl-protein thioesterase 1 (EC 3.1.2.22) (Palmitoyl-protein hydrolase 1) (Q9LY31)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Oleoyl-acyl carrier protein thioesterase 2, chloroplastic
- Probable acyl-activating enzyme 16, chloroplastic
- Long chain acyl-CoA synthetase 5
- Long-chain-fatty-acid--[acyl-carrier-protein] ligase AEE15, chloroplastic
- Probable enoyl-CoA hydratase 1, peroxisomal
- Long chain acyl-CoA synthetase 8
- Long chain acyl-CoA synthetase 3
- Long chain acyl-CoA synthetase 6, peroxisomal
- Long chain acyl-CoA synthetase 9, chloroplastic
Sequence:
MDFLKATIIVALICNFASLASSVPFIVLHGIGDKCSNAGVTQFTELLSDWSGSQGYCLEIGNGSWDSWTMPLLDQTSVVCEKVKSMPELSDGYSIVGLSQGNMIGRALIEFCDGAPPVKSFVSVAGPHAGTASIPFCGATWICIMLDSMIKAEIYSDYMQEHLAPSGFLKIPTDIAGYMEGCRFLPKLNNELPVKNSTYKERFSSLENLVLIMFEHDTILIPKETSWFGYYPDGSFKTILPPQETKLYTEDWIGLRTLDEAGKVKFVNVSGNHLQISHTDMKKHIVPYLCDKSSSSSSTTMAVSGSSSSHQWLPSVGNIIMDLIGPEVDQLQLVLRHV
Protein: Uncharacterized protein (Q381Z6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Intraflagellar transport protein 27 homolog
- Small GTP-binding protein Rab11
- Small GTPase
Sequence:
MNGVEINERDAPIIWKEKAVGVVCRNFDEDMQNAVRTLKTGDEQSVERMLRSYNNVNWKSSDGNTLLHWAATLGHMCAVRLLLDAGANCDSPNVVGATPLHCAAFGGSVAVIDELLLRGANAMAKNRKGHTMFDFLKDLWGGDLYKRYEGLERLLTALSGSCYDLPSPVTKPGEPPEGTLASQRSFRGKIASCFLQNMHERQSVPFENFQYEERDEDNDDGLLQKYHLLEVKELLMDESAKRNELVREHLTWAVDVMTQLRNLAYPVRCVEEVVEVLAKKDSPEGDRWLLLRAKGASEGSEVWVRLKDLCECYPTRTDEQGHIPSLRHSPAPTNLTKRCHAYNQSNVDVYRNSVVQRVMRLLKDASARSLRYQRKPFSNSLPRFLEVSEDESERVLRRVVSSPWHSQTPKSDRGSDASFSTGVRSVKESVMKSRRNSGIVSAGRDLWGGVSQSPKSVLHSFSPSISPVCREKFDLSTRSYDPFRAPDYCAPTESSRQRAGDGGKIERLRRIYASQYLKRRFDISKKS
Protein: Suppressor of cytokine signaling 7 (SOCS-7) (Nck, Ash and phospholipase C gamma-binding protein) (Nck-associated protein 4) (NAP-4) (O14512)
Organism: Homo sapiens (Human)
Function: Regulates signaling cascades probably through protein ubiquitination and/or sequestration. Functions in insulin signaling and glucose homeostasis through IRS1 ubiquitination and subsequent proteasomal degradation. Inhibits also prolactin, growth hormone and leptin signaling by preventing STAT3 and STAT5 activation, sequestering them in the cytoplasm and reducing their binding to DNA. May be a substrate recognition component of a SCF-like E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15242778, ECO:0000269|PubMed:17803907}. Nucleus {ECO:0000269|PubMed:17803907}. Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000269|PubMed:15242778}. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus (PubMed:17803907). Rapidly relocalizes to the nucleus after UV irradiation (PubMed:17803907). Cytoplasmic location depends upon SEPT7 presence (PubMed:17803907). {ECO:0000269|PubMed:17803907}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Cullin-5
- SH2/SH3 adapter protein NCK1
- Signal transducer and activator of transcription 3
- Septin-6
- Signal transducer and activator of transcription 5A
- Elongin-C
- Signal transducer and activator of transcription 5B
- Tyrosine-protein kinase JAK1
- Signal transducer and activator of transcription 1-alpha/beta
Sequence:
MVFRNVGRPPEEEDVEAAPEPGPSELLCPRHRCALDPKALPPGLALERTWGPAAGLEAQLAALGLGQPAGPGVKTVGGGCCPCPCPPQPPPPQPQPPAAAPQAGEDPTETSDALLVLEGLESEAESLETNSCSEEELSSPGRGGGGGGRLLLQPPGPELPPVPFPLQDLVPLGRLSRGEQQQQQQQQPPPPPPPPGPLRPLAGPSRKGSFKIRLSRLFRTKSCNGGSGGGDGTGKRPSGELAASAASLTDMGGSAGRELDAGRKPKLTRTQSAFSPVSFSPLFTGETVSLVDVDISQRGLTSPHPPTPPPPPRRSLSLLDDISGTLPTSVLVAPMGSSLQSFPLPPPPPPHAPDAFPRIAPIRAAESLHSQPPQHLQCPLYRPDSSSFAASLRELEKCGWYWGPMNWEDAEMKLKGKPDGSFLVRDSSDPRYILSLSFRSQGITHHTRMEHYRGTFSLWCHPKFEDRCQSVVEFIKRAIMHSKNGKFLYFLRSRVPGLPPTPVQLLYPVSRFSNVKSLQHLCRFRIRQLVRIDHIPDLPLPKPLISYIRKFYYYDPQEEVYLSLKEAQLISKQKQEVEPST
Protein: Endothelin-converting enzyme 1 (ECE-1) (EC 3.4.24.71) (P42891)
Organism: Bos taurus (Bovine)
Function: Converts big endothelin-1 to endothelin-1.
Subcellular location: Cell membrane; Single-pass type II membrane protein.
Interaction partners:
- Endothelin-1
- EEF1A lysine methyltransferase 4
- Insulin-degrading enzyme
- Endothelin receptor type B
- Endothelin-1 receptor
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
Sequence:
MMSTYKRATLDEEDLVDSLSESDVYPNHLQVNFRGPRNGQRCWAARTPVEKRLVVLVALLAAALVACLAVLGIQYQTRTPSVCLSEACISVTSSILSSMDPTVDPCQDFFTYACGGWIKANPVPDGHSRWGTFSNLWEHNQAIIKHLLENSTASVSEAERKAQVYYRACMNETRIEELKAKPLMELIEKLGGWNITGPWDKDNFQDTLQVVTSHYHTSPFFSVYVSADSKNSNSNVIQVDQSGLGLPSRDYYLNKTENEKVLTGYLNYMVQLGKLLGGGAEDTIRPQMQQILDFETALANITIPQEKRRDEELIYHKVTAAELQTLAPAINWLPFLNTIFYPVEINESEPIVIYDKEYLSKVSTLINSTDKCLLNNYMIWNLVRKTSSFLDQRFQDADEKFMEVMYGTKKTCLPRWKFCVSDTENTLGFALGPMFVKATFAEDSKNIASEIILEIKKAFEESLSTLKWMDEDTRKSAKEKADAIYNMIGYPNFIMDPKELDKVFNDYTAVPDLYFENAMRFFNFSWRVTADQLRKAPNRDQWSMTPPMVNAYYSPTKNEIVFPAGILQAPFYTRSSPNALNFGGIGVVVGHELTHAFDDQGREYDKDGNLRPWWKNSSVEAFKQQTACMVEQYGNYSVNGEPVNGRHTLGENIADNGGLKAAYRAYQNWVKKNGAEQTLPTLGLTNNQLFFLSFAQVWCSVRTPESSHEGLITDPHSPSRFRVIGSISNSKEFSEHFHCPPGSPMNPHHKCEVW
Protein: IQ motif and Sec7 domain ArfGEF 2 (A0A0G2JZX5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
KIPPWNHPVLYLASSHTLHQYCCPTQVLDSMKLTPSGRLAESSVEGDAPGSDLSTAVDSPGSQPPYRLSQLPPTSSHMGGPPAGVGLPWSQRARLQPASVALRKQEEEEIKRSKALSDSYELSTDLQDKKVEMLERKYGGSFLSRRAARTIQTAFRQYRMNKNFERLRSSASESRMSRRIILSNMRMQFSFEEYEKAQNPAYFEGKPASLDEGAMAGARSHRLERGLPYGGSCGGGIDGGGSSVTTSGEFSNDITELEDSFSKQVKSLAESIDEALNCHPSGPMSEEPGSAQLEKRESKEQQEDSSATSFSDLPLYLDDPVPPPSPERLPSTEPPPQGRPEFWAPAPLPPVPPPMPPGTREDGSREEGTRRGPGCLECRDFRLRAAHLPLLTIEPPSDSSVDLSDRSDRGSVHRQLVYEADGCSPHGTLKHKGPPGRAPIPHRHYPAPEGPAPAPPGPLPPAPNSGTGPSGVAGGRRLGKCEAAGENSDGGDNESLESSSNSNETINCSSGSSSRDSLREPPATGLCKQTYQRETRHSWDSPAFNNDVVQRRHYRIGLNLFNKKPEKGIQYLIERGFLSDTPVGVAHFILERKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSSMDLDDALRKFQSHIRVQGEAQKVERLIEAFSQRYCVCNPALVRQFRNPDTIFILAFAIILLNTDMYSPSVKAERKMKLDDFIKNLRGVDNGEDIPRDLLVGIYQRIQGRELRTNDDHVSQVQAVERMIVGKKPVLSLPHRRLVCCCQLYEVPDPNRPQRLGLHQREVFLFNDLLVVTKIFQKKKILVTYSFRQSFPLVEMHMQLFQNSYYQFGIKLLSAVPGGERKVLIIFNAPSLQDRLRFTSDLRESIAEVQEMEKYRVESELEKQKGMMRPNASQPGGAKDSVNGTLARSSLEDTYGAGDGLKRGALSSSLRDLSDAGKCSGPLSWLGRCGTRCPLCLLSLAVSLPPAHTHTHTHTHTHTHTHTHTMPQGAW
Protein: Dual specificity protein phosphatase 18 (EC 3.1.3.16) (EC 3.1.3.48) (Q6AXW7)
Organism: Rattus norvegicus (Rat)
Function: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8VE01}. Nucleus {ECO:0000250|UniProtKB:Q8NEJ0}. Mitochondrion inner membrane {ECO:0000269|PubMed:18385140}; Peripheral membrane protein {ECO:0000269|PubMed:18385140}; Intermembrane side {ECO:0000269|PubMed:18385140}. Note=Translocates to cytoplasm in response to apoptotic stimuli such as staurosporine treatment. {ECO:0000250|UniProtKB:Q8VE01}.
Interaction partners:
- Haloacid dehalogenase-like hydrolase domain-containing 5
Sequence:
MTSPWSACPVQFPQPSISGLSQITKSLFISNGAAANDKLLLSSNQITTVINVSVEVANTFYEDIQYVQVPVVDAPIARLSDFFDPIADHIHSVEMKQGRTLLHCAAGVSRSAALCLAYLMKYHVMSLLDAHAWTKSRRPIIRPNSGFWEQLIHYEFQLFGKNTMQMVNSPMGLIPDIYEKETRMMIPLSTPDGAFHKGKEKALL