wanglab/gogpt-training-data huggingface dataset:
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (P0A6P9)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000305|PubMed:4942326}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17242352, ECO:0000269|PubMed:18337249}. Secreted {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462}. Cell surface {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other (PubMed:17242352). When covalently bound to the substrate at Lys-342, the inactive enolase is secreted (PubMed:15003462). {ECO:0000269|PubMed:15003462, ECO:0000269|PubMed:17242352}.
Interaction partners:
- Ribonuclease E
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Pyruvate kinase I
- Glucose-6-phosphate isomerase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
- Pyruvate kinase II
- Glyceraldehyde-3-phosphate dehydrogenase A
- Fructose-bisphosphate aldolase class 2
Sequence:
MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFLGKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAKAAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVKEAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKDITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDGFAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAKDAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGEKAPYNGRKEIKGQA
Protein: Intermembrane transport lipoprotein PqiC (P0AB10)
Organism: Escherichia coli (strain K12)
Function: Component of a transport pathway that contributes to membrane integrity.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:27795327}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}; Periplasmic side {ECO:0000269|PubMed:27795327}.
Interaction partners:
- Intermembrane transport protein PqiA
- Intermembrane transport protein PqiB
- Lipophilic envelope-spanning tunnel protein A
- Lipophilic envelope-spanning tunnel protein B
- Uncharacterized lipoprotein YbfP
- Uncharacterized lipoprotein YsaB
- Uncharacterized protein YtcA
Sequence:
MKKWLVTIAALWLAGCSSGEINKNYYQLPVVQSGTQSTASQGNRLLWVEQVTVPDYLAGNGVVYQTSDVKYVIANNNLWASPLDQQLRNTLVANLSTQLPGWVVASQPLGSAQDTLNVTVTEFNGRYDGKVIVSGEWLLNHQGQLIKRPFRLEGVQTQDGYDEMVKVLAGVWSQEAASIAQEIKRLP
Protein: SR-related and CTD-associated factor 8 (CDC5L complex-associated protein 7) (RNA-binding motif protein 16) (Q9UPN6)
Organism: Homo sapiens (Human)
Function: Anti-terminator protein required to prevent early mRNA termination during transcription. Together with SCAF4, acts by suppressing the use of early, alternative poly(A) sites, thereby preventing the accumulation of non-functional truncated proteins. Mechanistically, associates with the phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit (POLR2A), and subsequently binds nascent RNA upstream of early polyadenylation sites to prevent premature mRNA transcript cleavage and polyadenylation. Independently of SCAF4, also acts as a positive regulator of transcript elongation.
Subcellular location: Nucleus {ECO:0000269|PubMed:11101529, ECO:0000269|PubMed:31104839, ECO:0000269|PubMed:9528809}. Nucleus matrix {ECO:0000269|PubMed:9528809}. Note=Detected in granular nuclear foci which correspond to sites of active transcription. {ECO:0000269|PubMed:31104839, ECO:0000269|PubMed:9528809}.
Interaction partners:
- Pre-mRNA cleavage complex 2 protein Pcf11
- Probable helicase senataxin
- DNA-directed RNA polymerase II subunit RPB1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Cleavage and polyadenylation specificity factor subunit 3
- Inner nuclear membrane protein Man1
- pre-mRNA 3' end processing protein WDR33
- Regulation of nuclear pre-mRNA domain-containing protein 2
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 7
Sequence:
MEAVKTFNSELYSLNDYKPPISKAKMTQITKAAIKAIKFYKHVVQSVEKFIQKCKPEYKVPGLYVIDSIVRQSRHQFGQEKDVFAPRFSNNIISTFQNLYRCPGDDKSKIVRVLNLWQKNNVFKSEIIQPLLDMAAGIPPPVVTPVLASTTTAMSNTPGTPVTPVTPANVVQGLPDPWVSQITNTDTLAAVAQILQSPQGQQLQQLIQTLQIQQQKPQPSILQALDAGLVVQLQALTAQLTAAAAAANTLTPLEQGVSFNKKLMDRFDFGEDSEHSEEPKKEIPASQLSHVSESVNNSIFHQIAEQLQQQNLEHLRQQLLEQQQPQKATPQDSQEGTFGSEHSASPSQGSSQQHFLEPEVNLDDSIDIQQQDMDIDEGQDGVEEEVFEQEAKKVAVRSRSRTHSRSRSRSPRKRRSRSRSGSRKRKHRKRSRSRSRERKRKSSRSYSSERRAREREKERQKKGLPPIRSKTLSVCSTTLWVGQVDKKATQQDLTNLFEEFGQIESINMIPPRGCAYVCMVHRQDAFRALQKLSSGSYKIGSKVIKIAWALNKGVKTEYKQFWDVDLGVTYIPWEKVKVDDLEGFAEGGMIDQETVNTEWETVKSSEPVKETVQTTQSPTPVEKETVVTTQAEVFPPPVAMLQIPVAPAVPTVSLVPPAFPVSMPVPPPGFSPIPPPPFLRASFNPSQPPPGFMPPPVPPPVVPPPTIPPVVPTSLVQPSLSMTPETVKDVGFGSLVIPGGSVASNLATSALPAGNVFNAPTKQAEPEEKVPHLIDHQISSGENTRSVIPNDISSNAAILGGQPPNVTSNSGILGVQRPNVSSNSEILGVRPSNVSSSSGIIAAQPPNILNNSGILGIQPPSVSNSSGLLGVLPPNIPNNSGLVGVQPPNVPNTPGLLGTQPPAGPQNLPPLSIPNQRMPTMPMLDIRPGLIPQAPGPRFPLIQPGIPPQRGIPPPSVLDSALHPPPRGPFPPGDIFSQPERPFLAPGRQSVDNVTNPEKRIPLGNDNIQQEGDRDYRFPPIETRESISRPPPVDVRDVVGRPIDPREGPGRPPLDGRDHFGRPPVDIRENLVRPGIDHLGRRDHFGFNPEKPWGHRGDFDEREHRVLPVYGGPKGLHEERGRFRSGNYRFDPRSGPWNRGFGQEVHRDFDDRRRPWERQRDRDDRDFDFCREMNGNRLGRDRIQNTWVPPPHARVFDYFEGATSQRKGDNVPQVNGENTERHAQPPPIPVQNDPELYEKLTSSNEINKEKSDTVADIESEPVVESTETEGT
Protein: G protein-coupled receptor kinase 6 (EC 2.7.11.16) (G protein-coupled receptor kinase GRK6) (P43250)
Organism: Homo sapiens (Human)
Function: Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine receptors in striatum and chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (By similarity). Phosphorylates rhodopsin (RHO) (in vitro) and a non G-protein-coupled receptor: LRP6 during Wnt signaling (in vitro).
Subcellular location: Membrane; Lipid-anchor.
Interaction partners:
- ARF GTPase-activating protein GIT1
- Beta-arrestin-2
- Beta-arrestin-1
- Mu-type opioid receptor
- ARF GTPase-activating protein GIT2
- Beta-2 adrenergic receptor
- C-X-C chemokine receptor type 2
- C-X-C chemokine receptor type 4
- C-X-C chemokine receptor type 1
- Rho guanine nucleotide exchange factor 6
Sequence:
MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELSRCVAFLDGVAEYEVTPDDKRKACGRQLTQNFLSHTGPDLIPEVPRQLVTNCTQRLEQGPCKDLFQELTRLTHEYLSVAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEYSERFSPQARSLCSQLLCKDPAERLGCRGGSAREVKEHPLFKKLNFKRLGAGMLEPPFKPDPQAIYCKDVLDIEQFSTVKGVELEPTDQDFYQKFATGSVPIPWQNEMVETECFQELNVFGLDGSVPPDLDWKGQPPAPPKKGLLQRLFSRQDCCGNCSDSEEELPTRL
Protein: Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10 (pTAC10) (Plastid-encoded RNA polymerase-associated protein 3) (PEP-associated protein 3) (Protein PIGMENT DEFECTIVE 312) (F4JF21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Plastid transcriptionally active 3
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Thioredoxin-like protein CITRX, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Fructokinase-like 2, chloroplastic
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- Fructokinase-like 1, chloroplastic
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
Sequence:
MQICQTKLNFTFPNPTNPNFCKPKALQWSPPRRISLLPCRGFSSDEFPVDETFLEKFGPKDKDTEDEARRRNWIERGWAPWEEILTPEADFARKSLNEGEEVPLQSPEAIEAFKMLRPSYRKKKIKEMGITEDEWYAKQFEIRGDKPPPLETSWAGPMVLRQIPPRDWPPRGWEVDRKELEFIREAHKLMAERVWLEDLDKDLRVGEDATVDKMCLERFKVFLKQYKEWVEDNKDRLEEESYKLDQDFYPGRRKRGKDYEDGMYELPFYYPGMVCEGTVTTLHLYQGAFVDIGGVHEGWVPIKGNDWFWIRHFIKVGMHVIVEITAKRDPYRFRFPLELRFVHPNIDHMIFNKFDFPPIFHRDGDTNPDEIRRDCGRPPEPRKDPGSKPEEEGLLSDHPYVDKLWQIHVAEQMILGDYEANPAKYEGKKLSELSDDEDFDEQKDIEYGEAYYKKTKLPKVILKTSVKELDLEAALTERQHHNKLMMEAKARGEGYKIDKLRRNIEMDEYDFLHWRRSLEEREALLRDISSRQALGLPLEEPGRYKPGSFFGKDQYDPTSALYQYDYWGEPKNSEISKQERMKDAHNKSIVGKGNVWYDMSYDDAIKQTIEKRKEGSTLASQEEETESEEEEEDDDDFDDFDYSILSDESSIGYSEQQPLVNGTQVLTD
Protein: Protein E7 (Q80901)
Organism: Human papillomavirus 37
Function: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000255|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MIGKEATIPEIVLELQELVQPTADLHCYEELSEEETEEERPHIPYKIVAPCCFCGSKLRLIVVATPIGIRSQEELLLGEVQLVCPNCRGKLRHD
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 9 (ADAM-TS 9) (ADAM-TS9) (ADAMTS-9) (EC 3.4.24.-) (Q9P2N4)
Organism: Homo sapiens (Human)
Function: Cleaves the large aggregating proteoglycans, aggrecan (at the '1838-Glu-|-Ala-1839' site) and versican (at the '1428-Glu-|-Ala-1429' site). Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:12514189}. Endoplasmic reticulum {ECO:0000269|PubMed:22419820}.
Interaction partners:
- Aggrecan core protein
- Threonylcarbamoyladenosine tRNA methylthiotransferase
- Beta-1,3-glucosyltransferase
- Translation initiation factor eIF2 assembly protein
Sequence:
MQFVSWATLLTLLVRDLAEMGSPDAAAAVRKDRLHPRQVKLLETLSEYEIVSPIRVNALGEPFPTNVHFKRTRRSINSATDPWPAFASSSSSSTSSQAHYRLSAFGQQFLFNLTANAGFIAPLFTVTLLGTPGVNQTKFYSEEEAELKHCFYKGYVNTNSEHTAVISLCSGMLGTFRSHDGDYFIEPLQSMDEQEDEEEQNKPHIIYRRSAPQREPSTGRHACDTSEHKNRHSKDKKKTRARKWGERINLAGDVAALNSGLATEAFSAYGNKTDNTREKRTHRRTKRFLSYPRFVEVLVVADNRMVSYHGENLQHYILTLMSIVASIYKDPSIGNLINIVIVNLIVIHNEQDGPSISFNAQTTLKNFCQWQHSKNSPGGIHHDTAVLLTRQDICRAHDKCDTLGLAELGTICDPYRSCSISEDSGLSTAFTIAHELGHVFNMPHDDNNKCKEEGVKSPQHVMAPTLNFYTNPWMWSKCSRKYITEFLDTGYGECLLNEPESRPYPLPVQLPGILYNVNKQCELIFGPGSQVCPYMMQCRRLWCNNVNGVHKGCRTQHTPWADGTECEPGKHCKYGFCVPKEMDVPVTDGSWGSWSPFGTCSRTCGGGIKTAIRECNRPEPKNGGKYCVGRRMKFKSCNTEPCLKQKRDFRDEQCAHFDGKHFNINGLLPNVRWVPKYSGILMKDRCKLFCRVAGNTAYYQLRDRVIDGTPCGQDTNDICVQGLCRQAGCDHVLNSKARRDKCGVCGGDNSSCKTVAGTFNTVHYGYNTVVRIPAGATNIDVRQHSFSGETDDDNYLALSSSKGEFLLNGNFVVTMAKREIRIGNAVVEYSGSETAVERINSTDRIEQELLLQVLSVGKLYNPDVRYSFNIPIEDKPQQFYWNSHGPWQACSKPCQGERKRKLVCTRESDQLTVSDQRCDRLPQPGHITEPCGTDCDLRWHVASRSECSAQCGLGYRTLDIYCAKYSRLDGKTEKVDDGFCSSHPKPSNREKCSGECNTGGWRYSAWTECSKSCDGGTQRRRAICVNTRNDVLDDSKCTHQEKVTIQRCSEFPCPQWKSGDWSECLVTCGKGHKHRQVWCQFGEDRLNDRMCDPETKPTSMQTCQQPECASWQAGPWGQCSVTCGQGYQLRAVKCIIGTYMSVVDDNDCNAATRPTDTQDCELPSCHPPPAAPETRRSTYSAPRTQWRFGSWTPCSATCGKGTRMRYVSCRDENGSVADESACATLPRPVAKEECSVTPCGQWKALDWSSCSVTCGQGRATRQVMCVNYSDHVIDRSECDQDYIPETDQDCSMSPCPQRTPDSGLAQHPFQNEDYRPRSASPSRTHVLGGNQWRTGPWGACSSTCAGGSQRRVVVCQDENGYTANDCVERIKPDEQRACESGPCPQWAYGNWGECTKLCGGGIRTRLVVCQRSNGERFPDLSCEILDKPPDREQCNTHACPHDAAWSTGPWSSCSVSCGRGHKQRNVYCMAKDGSHLESDYCKHLAKPHGHRKCRGGRCPKWKAGAWSQCSVSCGRGVQQRHVGCQIGTHKIARETECNPYTRPESERDCQGPRCPLYTWRAEEWQECTKTCGEGSRYRKVVCVDDNKNEVHGARCDVSKRPVDRESCSLQPCEYVWITGEWSECSVTCGKGYKQRLVSCSEIYTGKENYEYSYQTTINCPGTQPPSVHPCYLRDCPVSATWRVGNWGSCSVSCGVGVMQRSVQCLTNEDQPSHLCHTDLKPEERKTCRNVYNCELPQNCKEVKRLKGASEDGEYFLMIRGKLLKIFCAGMHSDHPKEYVTLVHGDSENFSEVYGHRLHNPTECPYNGSRRDDCQCRKDYTAAGFSSFQKIRIDLTSMQIITTDLQFARTSEGHPVPFATAGDCYSAAKCPQGRFSINLYGTGLSLTESARWISQGNYAVSDIKKSPDGTRVVGKCGGYCGKCTPSSGTGLEVRVL
Protein: Glycosylation-dependent cell adhesion molecule 1 (GlyCAM-1) (Lactophorin) (Proteose-peptone component 3) (PP3) (Whey protein) (P15522)
Organism: Camelus dromedarius (Dromedary) (Arabian camel)
Interaction partners:
- Alpha-lactalbumin
- Beta-casein
- L-selectin
- Kappa-casein
Sequence:
MKFFAVLLLASLAATSLASLNEPKDEIYMESQPTDTSAQVIMSNHQVSSEDLSMEPSISREDLVSKDDVVIKSARRHQNQNPKLLHPVPQESSFRNTATQSEETKELTPGAATTLEGKLVELTHKIIKNLENTMRETMDFLKSLFPHASEVVKPQ
Protein: Deoxycytidylate deaminase (EC 3.5.4.12) (dCMP deaminase) (O43012)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Supplies the nucleotide substrate for thymidylate synthetase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable thymidylate synthase
- Thymidylate kinase
- Probable deoxyuridine 5'-triphosphate nucleotidohydrolase
- Uridylate kinase
- BRCT-containing protein 1
- Imidazole glycerol phosphate synthase hisHF
Sequence:
MPTVGLTGPLCSGKDAVVEYLETKHGFNAIFRLPQLNEDGEYIYRTGDLVLGSVDDLISYLTPRWRERFVINGIHSPRLLSALLKRPFFLLVYIDAPIMLRFNRYKTYSSLANTTLEEFCSIQDAAAFQSDNAGTRHRALANLLINNDSNIKLHLWEKLQKADLLNPNRFRPSWDSYFMEMASLAAKRSNCMKRRVGCVLVRGNRVIATGYNGTPRGATNCNEGGCPRCNSASSCGKELDTCLCLHAEENALLEAGRERVGNNAILYCDTCPCLTCSVKITQLGIKEVVYHTSYNMDSHTASLLQAAGVQLRQYIPPENSIF
Protein: microtubule-severing ATPase (EC 5.6.1.1) (A0A2R8YCL5)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}.
Interaction partners:
Sequence:
MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRVPDFYVLQN
Protein: HECT-type E3 ubiquitin transferase (EC 2.3.2.26) (Q6P778)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
IGRVAGLAVFHGKLLDGFFIRPFYKMMLGKQITLNDMESVDSEYYNSLKWILENDPTELDLMFCIDEENFGQTYQVDLKPNGSEIMVTNENKREYIDLVIQWRFVNRVQKQMNAFLEGFTELLPIDLIKIFDENELELLMCGLGDVDVNDWRQHSIYKNGYCPNHPVIQWFWKAVLLMDAEKRIRLLQFVTGTSRVPMNGFAELYGSNGPQLFTIEQWGSPEKLPRAHTCFNRLDLPPYETFEDLREKLLMAVENAQGFEGVD
Protein: Uncharacterized protein (Q381Z7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYENFAAHAHDRALASGNIKPPPPASYLLIWSLPLLASFFVFGIARPLVADREVTPSLTHIGSGRSKRWWVVRLHLCVSTWLLFYCNFCVCAYLLLPTRVLLRLRMLPLSNNTTYGWCMRELRRALSFGIHLYDWDDKIYTGRISVVKSVESLASSDGPVRDELAPVVPLTNSEMWKYRAVVLAALVVTLFTLYFLASMIFRLSLGLPPCGEHRSNLALPQGSEEEEHDEDDDKNDEFDISFFSVDSEWWNMGNPDDACVDSPEAQAEEERLRSREQKRQNRQLPEKKTQSVRSVVWECWPLFASVCYSALYAISGGVAPFMWWVFPSSVVIVIVGSVLV
Protein: Ig heavy chain V region 1-72 (Ig heavy chain V region VH558 B4) (P06328)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGWSCIMLFLAATATGVHSQVQLQQPGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKYNEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCAR
Protein: ESAT-6-like protein EsxG (Conserved protein TB9.8) (O53692)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: EsxG, in complex with EsxH, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery. EsxG stabilizes EsxH in the host cytosol.
Subcellular location: Secreted {ECO:0000305|PubMed:21730061}. Note=Secreted via the ESX-3 / type VII secretion system (T7SS). {ECO:0000305|PubMed:21730061}.
Interaction partners:
- ESAT-6-like protein EsxH
- ESX-3 secretion-associated protein EspG3
- ESAT-6-like protein EsxR
- ESX-3 secretion system protein EccD3
- PPE family protein PPE4
- ESAT-6-like protein EsxB
- ESAT-6-like protein EsxQ
- PE family immunomodulator PE5
- 6 kDa early secretory antigenic target
- ESX-3 secretion system protein EccE3
Sequence:
MSLLDAHIPQLVASQSAFAAKAGLMRHTIGQAEQAAMSAQAFHQGESSAAFQAAHARFVAAAAKVNTLLDVAQANLGEAAGTYVAADAAAASTYTGF
Protein: Phosphatidate phosphatase PAH1 (EC 3.1.3.4) (Phosphatidic acid phosphohydrolase 1) (AtPAH1) (Q9SF47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Magnesium-dependent phosphatidate phosphatase which catalyzes the dephosphorylation of phosphatidate to yield diacylglycerol. Acts redundantly with PAH2 to repress phospholipid biosynthesis at the endoplasmic reticulum (ER). May function indirectly as repressor of multiple enzymes involved in phospholipid biosynthesis. Is involved in the pathway of galactolipid synthesis in the ER, which is required for the membrane lipid remodeling, an essential adaptation mechanism to cope with phosphate starvation.
Subcellular location: Cytoplasm, cytosol.
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 1
- Lipid phosphate phosphatase 1
- Putative lipid phosphate phosphatase 3, chloroplastic
- Lipid phosphate phosphatase 2
- Phospholipid:diacylglycerol acyltransferase 1
- Diacylglycerol O-acyltransferase 3
- Triacylglycerol lipase SDP1
- Triacylglycerol lipase SDP1L
- Probable lipid phosphate phosphatase 4
Sequence:
MSLVGRVGSLISQGVYSVATPFHPFGGAIDVIVVQQQDGSFRSTPWYVRFGKFQGVLKGAEKFVRISVNGTEADFHMYLDNSGEAYFIREVDPAANDTNNLISGSENNNGNQNNGVTYRLEHSLSDSGTGELREGFDPLSRLERTESDCNRRFYDFQDDPPSPTSEYGSARFDNLNVESYGDSQGSDSEVVLVSIDGHILTAPVSVAEQEAENLRLNTPQFHLAPGDGTEFCEGNTEFASSETPWDTEYIDKVEESSDTANIASDKVDAINDERNDLDSHSRDNAEKDSHDAERDLLGSCLEQSELTKTSENVKSEEPGPTFEDRNLKEGEFPLRTIMENDRSEDEVTIESIDTLVDSFESSTTQITIEEVKTTEGSRISVDSNADSECKDEQTSAETAILFNNQESSISVDSNADSECKDEQPRISAETAILINNQEGGIIESEDQDSERVSIDSTREEVDKDNEDRKTVVSVGVTSSVDEGEPDTDQRYELSLCKDELRQGMGLSAAAEVFDAHMISKEEYINSATSILESENLVVRIRETYMPWTKAARIVLGKAVFDLDLDIQPDDVISVEENESPKPKDDETTITPSSSGTRWRLWPIPFRRVKTVEHTGSNSSSEEDLFVDSEPGLQNSPETQSTTESRHESPRRQLVRTNVPTNEQIASLNLKDGQNMITFSFSTRVLGTQQVDAHIYRWRWDTKIVISDVDGTITKSDVLGQFMPFIGKDWTQSGVAKLFSAIKENGYQLLFLSARAIVQAYLTRNFLNNLKQDGKALPTGPVVISPDGLFPALYREVIRRAPHEFKIACLEDIRKLFPTDYNPFYAGFGNRDTDELSYRKLGIPKGKIFIINPKGEVATGHRIDVKKSYTSLHTLVNDMFPPTSLVEQEDYNPWNFWKLPIEEVE
Protein: At1g28540 (F1K23.22) (Transmembrane protein) (Q9SHP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Deneddylase
- Protein LHCP TRANSLOCATION DEFECT
- GTP-binding protein OBGC, chloroplastic
Sequence:
MAEKSQIPDNNNNTSSSAKKPTPEIGSGSGKRYYNPPESVNPDQATLREQWKFAIRQYSKWYSHAWGTAILAGGFFFGLGWIIKGSNPLPSLQSSSKPRDEEK
Protein: Lysophospholipid acyltransferase LPCAT4 (1-acylglycerol-3-phosphate O-acyltransferase 7) (1-AGP acyltransferase 7) (1-AGPAT 7) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (1-alkenylglycerophosphoethanolamine O-acyltransferase) (EC 2.3.1.121) (1-alkylglycerophosphocholine O-acetyltransferase) (EC 2.3.1.67) (Acyltransferase-like 3) (Lysophosphatidylcholine acyltransferase 4) (Lysophosphatidylethanolamine acyltransferase 2) (EC 2.3.1.n7) (Plasmalogen synthase) (Q643R3)
Organism: Homo sapiens (Human)
Function: Displays acyl-CoA-dependent lysophospholipid acyltransferase activity with a subset of lysophospholipids as substrates; converts lysophosphatidylethanolamine to phosphatidylethanolamine, lysophosphatidylcholine to phosphatidycholine, 1-alkenyl-lysophatidylethanolamine to 1-alkenyl-phosphatidylethanolamine, lysophosphatidylglycerol and alkyl-lysophosphatidylcholine to phosphatidylglycerol and alkyl-phosphatidylcholine, respectively. In contrast, has no lysophosphatidylinositol, glycerol-3-phosphate, diacylglycerol or lysophosphatidic acid acyltransferase activity. Prefers long chain acyl-CoAs (C16, C18) as acyl donors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16243729, ECO:0000269|PubMed:18458083}; Multi-pass membrane protein {ECO:0000269|PubMed:16243729, ECO:0000269|PubMed:18458083}.
Interaction partners:
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysocardiolipin acyltransferase 1
- Lysophospholipid acyltransferase 5
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Lysophosphatidylcholine acyltransferase 2
- Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
- Lysoplasmalogenase TMEM86B
- Cholinephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Ethanolaminephosphotransferase 1
Sequence:
MSQGSPGDWAPLDPTPGPPASPNPFVHELHLSRLQRVKFCLLGALLAPIRVLLAFIVLFLLWPFAWLQVAGLSEEQLQEPITGWRKTVCHNGVLGLSRLLFFLLGFLRIRVRGQRASRLQAPVLVAAPHSTFFDPIVLLPCDLPKVVSRAENLSVPVIGALLRFNQAILVSRHDPASRRRVVEEVRRRATSGGKWPQVLFFPEGTCSNKKALLKFKPGAFIAGVPVQPVLIRYPNSLDTTSWAWRGPGVLKVLWLTASQPCSIVDVEFLPVYHPSPEESRDPTLYANNVQRVMAQALGIPATECEFVGSLPVIVVGRLKVALEPQLWELGKVLRKAGLSAGYVDAGAEPGRSRMISQEEFARQLQLSDPQTVAGAFGYFQQDTKGLVDFRDVALALAALDGGRSLEELTRLAFELFAEEQAEGPNRLLYKDGFSTILHLLLGSPHPAATALHAELCQAGSSQGLSLCQFQNFSLHDPLYGKLFSTYLRPPHTSRGTSQTPNASSPGNPTALANGTVQAPKQKGD