wanglab/gogpt-training-data huggingface dataset:
Protein: Wilms tumor protein 1-interacting protein (WT1-interacting protein) (Q7TQJ8)
Organism: Mus musculus (Mouse)
Function: Adapter or scaffold protein which participates in the assembly of numerous protein complexes and is involved in several cellular processes such as cell fate determination, cytoskeletal organization, repression of gene transcription, cell-cell adhesion, cell differentiation, proliferation and migration. Positively regulates microRNA (miRNA)-mediated gene silencing. Negatively regulates Hippo signaling pathway and antagonizes phosphorylation of YAP1. Acts as a transcriptional corepressor for SNAI1 and SNAI2/SLUG-dependent repression of E-cadherin transcription. Acts as a hypoxic regulator by bridging an association between the prolyl hydroxylases and VHL enabling efficient degradation of HIF1A. In podocytes, may play a role in the regulation of actin dynamics and/or foot process cytoarchitecture. In the course of podocyte injury, shuttles into the nucleus and acts as a transcription regulator that represses WT1-dependent transcription regulation, thereby translating changes in slit diaphragm structure into altered gene expression and a less differentiated phenotype. Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity).
Subcellular location: Cell junction, focal adhesion. Cell junction, adherens junction. Nucleus. Cytoplasm, cytosol. Cell membrane. Note=In adherent but isolated podocytes, targets to focal adhesions and then shifts to adherens junctions after cells make homotypic contacts. Following podocyte injury, caused by treatment with LPS, puromycin aminonucleoside, ultraviolet or hydrogen peroxide, translocates from sites of cell-cell contacts into the cytosol and nucleus. Maximal nuclear localization is achieved 6 hours after LPS treatment. Nuclear translocation requires dynein motor activity and intact microtubule network (By similarity). Returns to cell-cell contacts several hours after LPS stimulation. In the presence of ROR2, localizes to the plasma membrane. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Protein salvador homolog 1
- Serine/threonine-protein kinase LATS2
- LIM domain-containing protein ajuba
- LIM domain-containing protein 1
Sequence:
MQRSRTAADDAALLLAGLGLRESEPTAGSPGRVRRGPRAVDEAAPASGRRGKGGCGGPEAAPDVPSRPERGPRASLAGSDGGSARSSGISLGYDQRHGPGPGPPSGGSARSSVSSLGSRGSAGACADLLPPGVGPAPARSPEPAQFPFPLPSLPLPPGREGGPSAAERRLEALTRELERALEARTARDYFGICIKCGLGIYGARQACQAMGSLYHTDCFICDSCGRRLRGKAFYNVGEKVYCQEDFLYSGFQQTADKCSVCGHLIMEMILQALGKSYHPGCFRCSVCNECLDGVPFTVDVDNNIYCVRDYHTVFAPKCASCARPILPAQGCETTIRVVSMDRDYHVECYHCEDCGLQLSGEEGRRCYPLEGHLLCRRCHLRRLGQGPLPSPAVHVTEL
Protein: DEK protein (Dek, isoform D) (Q8IFW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDANKAAETAAKENAADKVSDVENASVTAGVAKAVGAQPERGSKDAAESPAAVDASASAATDDVADKKAKGDSTAVSNTESDAAAADKKEKSPSPVIKKSNNKDAKKEDNSEKDEENSEDGDEPEDEADEKASDEESEKKKPKLDAEDKIKDATDESKPKSGADKPKKPEPKAKNGKVAKEEDDDEEDEDDEDAEDDDGDENDGLDKNNEVAEDDENVVALAEIDRINENINKTRVDGLQTLHAICFGAQGKNNVVKKNLRSFAGFEFAKDSAEYNKKLEAIKKVDNKGLRSICEILTLDRKGSKNETVLRVLKFLMEPDESLCLEQGDEEEEEDAEDEDLDEDEEDPPSEEDKKRKSGKSSGGAGRGSARNSTGRPRRATAGKKMSAYVDFSSSDDSEQKVAVPKRRRNDDSESGSDYNPSANSDSDGGRGGGAGAAGRKVPSRGGRGRPARKSRRRNSDSEEEEESEVSDADSDVPKRKRGSVGKRGRPAAPASAGRRGRGRGAASRKRKDSDSEDEEVSEDEEEEDVSDFASDQSEEERPKKSKKPITPAKNSKANNKSKPAGKADSRSKKSKKESSEEDDDVDDKDESDEDEPLTKKGKQAFPTVGSQ
Protein: IP15483p (Metabotropic GABA-B receptor subtype 3, isoform C) (Q058U9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRIIQPVQGTRYGPWPAVGLRLVLALAWATSAAAAMESSAELQALGYEAIRPGAASISTSSPSSSPPGESASTVTAGGTPIPPRSDWKYKRTKVKRRQQRLNSHSNLPGSTNASHAHHLLNLPPRQRYLKVNQVFESERRMSPAEMQRNHGKIVLLGLFELSTSRGPRPDGLSELGAATMAVEHINRKRLLPGYTLELVTNDTQCDPGVGVDRFFHAIYTQPSTRMVMLLGSACSEVTESLAKVVPYWNIVQVSFGSTSPALSDRREFPYFYRTVAPDSSHNPARIAFIRKFGWGTVTTFSQNEEVHSLAVNNLVTELEAANISCAATITFAATDFKEQLLLLRETDTRIIIGSFSQELAPQILCEAYRLRMFGADYAWILHESMGAPWWPDQRTACSNHELQLAVENLIVVSTHNSIVGNNVSYSGLNNHMFNSQLRKQSAQFHGQDGFGSGYGSRISIAATQSDSRRRRRRGVGGTSGGHLFPEAISQYAPQTYDAVWAIALALRAAEEHWRRNEEQSKLDGFDYTRSDMAWEFLQQMGKLHFLGVSGPVSFSGPDRVGTTAFYQIQRGLLEPVALYYPATDALDFRCPRCRPVKWHSGQVPIAKRVFKLRVATIAPLAFYTIATLSSVGIALAIAFLAFNLHFRKLK
Protein: RE61424p (Q7JWH6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNPCTSSPPQMPRGSGSVENCNLESDGLQLLEMAGKEDYEELRDLLQSWDVADLLPHLQDEAINVDELQMIKRHHLSELLRNFRFGTRIRFEHHLERWRRWLNVPLQGAQGQGSSHCSGCRCPEILGQSQCQEQSPLHMEQPSEQEELHKPEDLVKTIPAESLVALSDPREMSVPFPLPLVHPPAQITDDIMMVKQELMPMQQTRKPEAVLAAGSSGGTSGNKEDATATPDQEVSILGILRSSGMKAQSLLERIGQNDPLDAVQRLLLIQLVCSYYEENQMHLTLQRSHLLEREILQLFPQEQLSYYRTERRGKIYVRFTNMKRSKRLSSSRQELKRRRSELIRSIPTVQGHDASASVNFAGDQISSPDRSD
Protein: Transcription elongation factor A protein 2 (Protein S-II-T1) (Testis-specific S-II) (Transcription elongation factor S-II protein 2) (Transcription elongation factor TFIIS.l) (Q63799)
Organism: Rattus norvegicus (Rat)
Function: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- Transcription initiation factor IIB
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit RPB3
- Transcription elongation factor SPT5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- RNA polymerase II subunit J
- DNA-directed RNA polymerase II subunit RPB4
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MGKEEEIARIARRLDKMVTRKNAEGAMDLLRELKNMPITLHLLQSTRVGMSVNALRKQSSDEELIALAKSLIKSWKKLLDVSDGKSRDQGRGTPLPTSSSKDASGTTDLSCKKPDPPRTSSTPRITTFPQVPITCDAVRNKCREMLTLALQTDHDHVAVGVSCEHLSSQIEECIFLDVGNTDMKYKNRVRSRISNLKDAKNPGLRRNVLCGAITPQQIAVMTSEEMASDELKEIRKAMTKEAIREHQMARTGGTQTDLFTCNKCRKKNCTYTQVQTRSSDEPMTTYVVCNECGNRWKFC
Protein: Bromodomain testis-specific protein (Cancer/testis antigen 9) (CT9) (RING3-like protein) (Q58F21)
Organism: Homo sapiens (Human)
Function: Testis-specific chromatin protein that specifically binds histone H4 acetylated at 'Lys-5' and 'Lys-8' (H4K5ac and H4K8ac, respectively) and plays a key role in spermatogenesis. Required in late pachytene spermatocytes: plays a role in meiotic and post-meiotic cells by binding to acetylated histones at the promoter of specific meiotic and post-meiotic genes, facilitating their activation at the appropriate time. In the post-meiotic phase of spermatogenesis, binds to hyperacetylated histones and participates in their general removal from DNA. Also recognizes and binds a subset of butyrylated histones: able to bind histone H4 butyrylated at 'Lys-8' (H4K8ac), while it is not able to bind H4 butyrylated at 'Lys-5' (H4K5ac) (By similarity). Also acts as a component of the splicing machinery in pachytene spermatocytes and round spermatids and participates in 3'-UTR truncation of specific mRNAs in post-meiotic spermatids (By similarity). Required for chromocenter organization, a structure comprised of peri-centromeric heterochromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:20538714, ECO:0000269|PubMed:22901802, ECO:0000269|PubMed:22971749, ECO:0000269|PubMed:25593309}. Note=Detected on chromatin. {ECO:0000250|UniProtKB:Q91Y44}.
Interaction partners:
- Histone H4-like protein type G
- Histone H4
- Bromodomain-containing protein 2
- Beta-defensin 1
- Bromodomain-containing protein 4
- Bromodomain-containing protein 3
- Cyclin-dependent kinase 9
- Cyclin-T1
- Histone H3.3C
- Histone H3.1
Sequence:
MSLPSRQTAIIVNPPPPEYINTKKNGRLTNQLQYLQKVVLKDLWKHSFSWPFQRPVDAVKLQLPDYYTIIKNPMDLNTIKKRLENKYYAKASECIEDFNTMFSNCYLYNKPGDDIVLMAQALEKLFMQKLSQMPQEEQVVGVKERIKKGTQQNIAVSSAKEKSSPSATEKVFKQQEIPSVFPKTSISPLNVVQGASVNSSSQTAAQVTKGVKRKADTTTPATSAVKASSEFSPTFTEKSVALPPIKENMPKNVLPDSQQQYNVVKTVKVTEQLRHCSEILKEMLAKKHFSYAWPFYNPVDVNALGLHNYYDVVKNPMDLGTIKEKMDNQEYKDAYKFAADVRLMFMNCYKYNPPDHEVVTMARMLQDVFETHFSKIPIEPVESMPLCYIKTDITETTGRENTNEASSEGNSSDDSEDERVKRLAKLQEQLKAVHQQLQVLSQVPFRKLNKKKEKSKKEKKKEKVNNSNENPRKMCEQMRLKEKSKRNQPKKRKQQFIGLKSEDEDNAKPMNYDEKRQLSLNINKLPGDKLGRVVHIIQSREPSLSNSNPDEIEIDFETLKASTLRELEKYVSACLRKRPLKPPAKKIMMSKEELHSQKKQELEKRLLDVNNQLNSRKRQTKSDKTQPSKAVENVSRLSESSSSSSSSSESESSSSDLSSSDSSDSESEMFPKFTEVKPNDSPSKENVKKMKNECIPPEGRTGVTQIGYCVQDTTSANTTLVHQTTPSHVMPPNHHQLAFNYQELEHLQTVKNISPLQILPPSGDSEQLSNGITVMHPSGDSDTTMLESECQAPVQKDIKIKNADSWKSLGKPVKPSGVMKSSDELFNQFRKAAIEKEVKARTQELIRKHLEQNTKELKASQENQRDLGNGLTVESFSNKIQNKCSGEEQKEHQQSSEAQDKSKLWLLKDRDLARQKEQERRRREAMVGTIDMTLQSDIMTMFENNFD
Protein: Integrator complex assembly factor BRAT1 (BRCA1-associated ATM activator 1) (BRCA1-associated protein required for ATM activation protein 1) (Q8C3R1)
Organism: Mus musculus (Mouse)
Function: Involved in DNA damage response; activates kinases ATM, SMC1A and PRKDC by modulating their phosphorylation status following ionizing radiation (IR) stress. Plays a role in regulating mitochondrial function and cell proliferation (By similarity). Required for protein stability of MTOR and MTOR-related proteins, and cell cycle progress by growth factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:25631046}. Cytoplasm {ECO:0000269|PubMed:25631046}. Note=Present at double strand breaks (DSBs) following ionizing radiation treatment (By similarity). The ubiquitinated form localizes in the nucleus in a NDFIP1-dependent manner. {ECO:0000250|UniProtKB:Q6PJG6, ECO:0000269|PubMed:25631046}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
Sequence:
MDPECSRLLPALCAVLADPRQLVADDTCLEKLLDWFKTVTEAESSLQLLQDHPCLMELLSHVLKPQDVSPRVLSFALRLVGVFAAQEDCFEYLQQGELLLGLFGESGAPGWAAWSIPSVRSGWIQGLCYLAHHPSALHFLADSGAVDTLFSLQGDPSLFVASAASQLLVHILALSMQGGAPGSPVPEAAAWPMCAQKIVNHVDESLHAKATPQVTQALNVLTTTFGRCHNPWTGVLWERLSPPVARLFERDPIPAVHALMDLLLSVARSPVLNFAACGLWEMLAQTLSRLSPIQAGPLALGTLKLQHCPQELRTQAFGVLLQPLACILKATTQAPGPPGLLDGTVGSLLTVDILLASKSACVGLLCQTLAHLEELQMLPQCPSPWPQVHLLQAALTILHLCDGSADPSSSAGGRLCGTLGGCVRVQRAALDFLGTLSQGTSPLELVLEVFAVLLKTLESPESSPMVLKKAFQATLRWLQNPHKTPSSSDLSSDALLFLGELFPILQKRLCSPCWEVRDSALEFLTHLIRHWGGQADFREALRSSEVPTLALQLLQDPESYVRASAVGAAGQLSSQGLQAAPASPENSQAQQGLLMDLMHILSTDSEGFPRRAVLRVFTDWLRDGHADVVRDTEWFVATVLQAVSRDLDWEVRVQGLELARVFLTQALGQPSLHCPYTVGLPRASSPRPHPEFLQTLCRLPLFEFAFCALLDCDRPVAQKACDLLLFLRDKTVPCSSPREAGDSPNSASVEAALQRWREGEQAQPLGDLDPEAMLAILRALDLEGLQGRLAKSSDHVEKSPQSLLQDMLATVGVLEENEADCY
Protein: At1g14330/F14L17_7 (F14L17.10 protein) (Galactose oxidase/kelch repeat superfamily protein) (Q9M9S9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- BTB/POZ domain-containing protein At2g30600
- Probable aspartyl protease At4g16563
- U-box domain-containing protein 45
- F-box protein PP2-A14
- U-box domain-containing protein 29
- Probable CCR4-associated factor 1 homolog 5
- Kelch repeat-containing protein At3g27220
- RING-H2 finger protein ATL79
- RNA-binding protein BRN2
- E3 ubiquitin-protein ligase SGR9, amyloplastic
Sequence:
MVEDRTYLMSRIFSSSRLSESKWPYMYPQPEDSSESNLINGKRALENDVDELRQSKSPRLMGFSIHGNEAIEEDEQEQDQSDSNNNGNSDGDSLINDIGRDNSISCLIRCSRSGYGSIASLNRSFRSLVKTGEIYRLRRQNQIVEHWVYFSCQLLEWVAFNPFERRWMNLPTMPSGVTFMCADKESLAVGTDLLVLGKDDYSSHVIYRYSLLTNSWSSGMRMNSPRCLFGSASLGEIAIFAGGFDSFGKISDSAEMYNSELQTWTTLPKMNKPRKMCSGVFMDGKFYVIGGIGGNDSKVLTCGEEFDLETKKWTEIPEMSPPRSREMPAAAEAPPLVAVVNNELYAADHADMEVRKYDKESKKWFTLGRLPERADSVNGWGLAFRACGERLIVIGGPRSSGGGYIELNSWIPSSDRSPPLWTLLGRKHSSNFVYNCAVMGC
Protein: Sticks and stones, isoform A (A1Z7J1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MALQQQHQRHQQHQQHQQQQQQQQQQQHIKWQQHATKRRRCRQHWIKHLQLLRLLAVIVLASAPVPSHAQQQKFRTTPHDLQVLEGAEAMMRCEVANVAGAVQWTKDGFALGFSAVIPGFPRYSVLGDRKQGIYNLRISNASINDDADYQCQVGPARLNSAIRANAKLTVISPPASIEIKGYSHNSKVEVRENQDLQLKCIVANAKPAAQIVWYRGNVEYKPEKREDTVEESTAKRFTTTSSLKLKPGPDDDYTEYTCQARHKALSPDMPMRATVQLSVLYPPGPPYIEGYSAGETLRRGQTVELMCRSRGGNPPAQLIWYKNGSQIRMAYRTSGRLSENIYTFTAEAGDNKARFRCEASNVMSQNPLKAEVELSVLFAPTHVTVMGPTEARVGDIVPLTCTTAPSNPPAEIKWMVGGRQVRNATSKTIVSPEGGWTTTSNITAVVEPNKRSLVVICHGLNMQLTENVVSTHTINVLYPPAPPLISGYMEGQIIPAGSVQKLLCVSSGGNPLATLTWYKNDKRINSVIRAADKSVSAEITILANVSDNQAQYRCEASNSATEIPLFQSTTLSVHFAPETVKIRIEPEELRPGMEATIICDSSSSNPPAKLSWWKDGIPIEGINNTSKPGLWGGTVSTLEFRVNVTQEMNGQVYTCQSANEALQRSAHEAVSLDVLYRPKFVPPPSSTAVGVEGESLQVSLQTRANPTPVTYKWTKDGTTIPQDGDHRIFADGGSLNFTRLHRDDAGIYSCSASNSQGGATLNITVVVEYGTTIKSVSENIVVNPGEDAMLSCTVEGKPLTEEHVKWERVGYDMTVKTSTTFANGTSYLHIKDAKREDVGNFRCVADNRVDNPTNRDILLIVKFAPEIAKTPTLLRAASGTGERGRLPCRAQGSPKPQFIWRQDKKDLPINRTYKYEVEERKIDSLTYESTLIVDKVAPADYGAYECVARNELGEAVETVRLEITSQPDPPLSLNILNVTHDTVTLAWTPGFDGGLKASYRVRYRMADREQYKYIDGLPNSHKLTIGGLRMNTLYLFSVMSWNELGQSSYLPDLARAETKGLELMPAELTEDSSNTPNLVIIGISLAAFGFLLVNASLVAWFFVHQRRKKVAETTNQPAKTATIEMYAPSSYNDTVTGETLSSVSEKSESYSNEGSSQPEYIDEVRKKAASTYLVEGSDMPPPRYQKDGTLPVIYPNNVVNACTLPHPRHNNGSAAIHMTRDDQMLISKGVYIPSPSPAPPPDGSYYNMNSDRYLSYPPMEYPAALDFTAQPMPMAHLQPMTVTSLATNGGPTLIGNGSVAAVAGGSGTLRRGILRGVVGVPQPDVTHHTSTVGGSPMQMLHDLHPVNLSASTLTTSTTLNGSLPTATATLPRQPHGILKDPNRNKQQQQQQQQQQQQQQLQHQQQLLNASLVGVGVPVSAPLGSLQILNLPPASGGLGNNLLMTTNAFDPTTVGLSSFGAVSQAGGIPVAYTDADGHLV
Protein: Homeobox protein SIX5 (DM locus-associated homeodomain protein) (Sine oculis homeobox homolog 5) (Q8N196)
Organism: Homo sapiens (Human)
Function: Transcription factor that is thought to be involved in regulation of organogenesis. May be involved in determination and maintenance of retina formation. Binds a 5'-GGTGTCAG-3' motif present in the ARE regulatory element of ATP1A1. Binds a 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the myogenin promoter, and in the IGFBP5 promoter (By similarity). Thought to be regulated by association with Dach and Eya proteins, and seems to be coactivated by EYA1, EYA2 and EYA3 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12500905}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12500905}.
Interaction partners:
- Protein phosphatase EYA1
- Zinc finger protein 143
- Dystrophia myotonica WD repeat-containing protein
- Transcriptional repressor CTCF
- Myotonin-protein kinase
- Protein phosphatase EYA3
- Muscleblind-like protein 1
Sequence:
MATLPAEPSAGPAAGGEAVAAAAATEEEEEEARQLLQTLQAAEGEAAAAAGAGAGAAAAGAEGPGSPGVPGSPPEAASEPPTGLRFSPEQVACVCEALLQAGHAGRLSRFLGALPPAERLRGSDPVLRARALVAFQRGEYAELYRLLESRPFPAAHHAFLQDLYLRARYHEAERARGRALGAVDKYRLRKKFPLPKTIWDGEETVYCFKERSRAALKACYRGNRYPTPDEKRRLATLTGLSLTQVSNWFKNRRQRDRTGAGGGAPCKSESDGNPTTEDESSRSPEDLERGAAPVSAEAAAQGSIFLAGTGPPAPCPASSSILVNGSFLAASGSPAVLLNGGPVIINGLALGEASSLGPLLLTGGGGAPPPQPSPQGASETKTSLVLDPQTGEVRLEEAQSEAPETKGAQVAAPGPALGEEVLGPLAQVVPGPPTAATFPLPPGPVPAVAAPQVVPLSPPPGYPTGLSPTSPLLNLPQVVPTSQVVTLPQAVGPLQLLAAGPGSPVKVAAAAGPANVHLINSGVGVTALQLPSATAPGNFLLANPVSGSPIVTGVALQQGKIILTATFPTSMLVSQVLPPAPGLALPLKPETAISVPEGGLPVAPSPALPEAHALGTLSAQQPPPAAATTSSTSLPFSPDSPGLLPNFPAPPPEGLMLSPAAVPVWSAGLELSAGTEGLLEAEKGLGTQAPHTVLRLPDPDPEGLLLGATAGGEVDEGLEAEAKVLTQLQSVPVEEPLEL
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha1 (EC 3.1.1.47) (PAF acetylhydrolase 29 kDa subunit) (PAF-AH 29 kDa subunit) (PAF-AH subunit gamma) (PAFAH subunit gamma) (Q15102)
Organism: Homo sapiens (Human)
Function: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. Both alpha1/alpha1 homodimer (PAFAH1B3/PAFAH1B3 homodimer) and alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B2 heterodimer) hydrolyze 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) more efficiently than PAF, but they have little hydrolytic activity towards 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE). Plays an important role during the development of brain.
Subcellular location: Cytoplasm.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit beta
- Platelet-activating factor acetylhydrolase IB subunit alpha2
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Lysophosphatidylcholine acyltransferase 1
- Platelet-activating factor acetylhydrolase
- Lysophosphatidylcholine acyltransferase 2
- Lysophospholipid acyltransferase LPCAT4
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
- Dual specificity protein kinase CLK2
Sequence:
MSGEENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDGTQHVLWRLENGELEHIRPKIVVVWVGTNNHGHTAEQVTGGIKAIVQLVNERQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGHPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGAPLLEPAP
Protein: Transgelin (Q6TGT5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MANKGPSYGLSREVQSKIDKKYDPELEGRLVQWIVSQCGEAIGKPQPGKQGFQQWLKDGCILCELINSLFKDSKPVKKIQSSSMAFKQMEQISQFLTAAERYGITKSDIFQTVDLWEGKDLAAVQMTLLSLGSLAVTKDDGCYRGDPAWFPKKSHENRREFSEEQMKEGHSVIGLHMGTNIGASQAGMTGYGRPRQILNNQ
Protein: RB-related protein RBF2 (Q9NIS1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METCEVEGEAETLVRRFSVSCEQLELEARIQQSALSTYHRLDAVNGLSTSEADAQEWLCCAVYSELQRSKMRDIRESINEANDSVAKNCCWNVSLTRLLRSFKMNVSQFLRRMEHWNWLTQNENTFQLEVEELRCRLGITSTLLRHYKHIFRSLFVHPGKGADPGAANHYQALYEFGWLLFLVIRNELPGFAITNLINGCQVLVCTMDLLFVNALEVPRSVVIRREFSGVPKNWDTEDFNPILLNKYSVLEALGELIPELPAKGVVQMKNAFFHKALIMLYMDHSLVGDDTHMREIIKEGMLDINLENLNRKYTNQVADISEMDERVLLSVQGAIETKGDSPKSPQFAFQTSSSPSHRKLSTHDLPASLPLSIIKAFPKKEDADKIVNYLDQTLEEMNQTFTMAVKDFLDAELSGKRFRQARGLYYKYLQKILGPELVQKPQLKIGQLMKQRKLTAALLACCLELALHVHHKLVEGLRFPFVLHCFSLDAYDFQKILELVVRYDHGFLGRELIKHLDVVEEMCLESLIFRKSSQLWWELNQRLPRYKEVDAETEDKENFSTGSSICLRKFYGLANRRLLLLCKSLCLVDSFPQIWHLAEHSFTLESSRLLRNRHLDQLLLCAIHLHVRLEKLHLTFSMIIQHYRRQPHFRRSAYREVSLGNGQTADIITFYNSVYVQSMGNYGRHLECAQTRKSLEESQSNVGILTETTSNELSMRANISISSPPPPRVCQSGSCSSHPPSSPAASPLSLQSSPNVKRAASSNDLREIKRPNILRRRQLSVI
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (P0DOB6)
Organism: Lactococcus lactis subsp. lactis (Streptococcus lactis)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
Interaction partners:
Sequence:
MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGIEVYGINHGYAGMVAGDIFPLTSASVGDKIGRGGTFLYSARYPEFAQVEGQLAGIEQLKKFGIEGVVVIGGDGSYHGAMRLTEHGFPAVGLPGTIDNDIVGTDFTIGFDTAVSTVVDALDKIRDTSSSHNRTFVVEVMGRNAGDIALNAGIAAGADDISIPELEFKFENVVNNINKGYEKGKNHHIIIVAEGVMTGEEFATKLKEAGYKGDLRVSVLGHIQRGGSPTARDRVLASRMGARAVELLRDGIGGVAVGIRNEELVESPILGTAEEGALFSLTTEGGIKVNNPHKAGLELYRLNSALNNLNLN
Protein: Hmr (Hybrid male rescue) (Q86CW5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD09786p
- GST-containing FLYWCH zinc-finger protein
- CG2124
- Rab at 9D
- Heterochromatin protein 1
Sequence:
MEEEPVAIENDCQIIVSDTIGQKTNGVDDDKAPNPFSRCTYPGSRDGGILQTYRAERLLIALVRRQPLLYDARHPKFRDVAQREKQWKKIASRLATNATNCKRSWSALRYKYQRHVRRLRNFHRSAIQKDRAALRWRPCMEYEEEMRFMYTHVARFPLIVDKIPTEILEKEHVDESETRPDVEVIENPPMDIIDLDVEEDPTYNYRCNRLQRRLIEAVSAYPLLYDSTCTGYQNTRHRFLIWSAISNEVHDKATKLMKCWLKLQTRYEWELIHRPRHIGTSELCRLMDFMEPHVQRMRGTVCKSSKYLQNGWHEPIENFHTVMALITTMRNMPELVQLTEDSLHNKVKPPRYDEFWQKVGMEVMCSHEHCEVTWLVLRAFYHELQAVRSSGYQLQDKWFFEGSMGLALTPVTSRSTARPALKRTANGAIPVAGEPPAKTPVPVRMPLAIVYPSTSKGSSTSMTNSASTATSIGPTFTNVRRSSGPVINNTSTAAAATNSVSSSVSPDQALPKFVIPKITSAISVGSGYMIPLKFVPNVRILPKPAATMGTGVSPIATTNQMAGPNAKPPEVRPQITQGPGLQVKLHTKPQMASRPQMAPVVPRTVIRTTNPTNPAQTQDRVSGGPMSTLGELLRPQNPSQIRSPAPQQTLPNFVPITTSNITAKSNLPTPTAAPMVRIHQPGLKSAWDGKSNSAPFSKPIRSLLTTSSPAAAPIVATAEPARAKIIPPKPKLPATTLVNPKKYQPIVPVAVLPTAATRMAKPATEPATELPVTTPPIATGQTTRVIRKTPLFPTSATQAASDSYATIQGTLASQAKAVGAAISAPVVRPAKLPTVAKATTASQSDIKATAAASATLGSQPENLPLGNITVCLHESDTTGNELQVWCGNQGTRFNLNMIRTTTLIREVMAVPQLHKEDPQLAAKCVEFWHFIAKKFHMPEEALRACWKFLAANMSVFPKIAPMSELMRPFKYSEKVWEKSNRLFGKFDEIALKYQWLNHKNVLPEVIRFFAKYEYLYCDLRRPRPGEDAQAPPQLTNQEKQEVWREARLKFPNLNHRDIWSMFKFAFRTYLDDLERGIDNPWPQNWWQALEQLRFLVNVRYHPLEPYYYIVHNRMSEEVKRCKMHEALTSSDHIDKTKFTPSKLLTGFSKEPKPWETEEAKRLLTGKLNSVRSTETLTQIAPAPALALAPDAQPIPVPDGVSVSKKTSESKPASNANVKSHKDKNISTAQKRPTPARSVTCNNLSPIEAFELCKKLRSQPNSFERASTLDKRAAWVRVSKELHATVTECRLGLQYALREMRNLKIADPSNQCTMGHKYLHHMSEIYKQVKPNAQLTVRTPQQLNQLNESLAKNTQEVSPQEFLPEINLSTCSPDLVVKNWAYAVGNLSTASQDTLLGKMTQLFSKYAKVNPPPP
Protein: Brevinin-2SN1 (E7EKH3)
Organism: Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa)
Function: Antimicrobial peptide. Active against some Gram-negative and a variety of Gram-positive bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 10231. Shows hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000305|PubMed:24055160}.
Interaction partners:
Sequence:
MFTMKKPLLFLFFLGTISLSFCEEERGADEDDEVEMTEEEKRGLRDKIKNVAIDVAKGAGTGVLKALLCQLDKSC
Protein: Cytosolic leucyl aminopeptidase, putative (EC 3.4.11.1) (Q57W67)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Glutathione synthetase
- glutathione-specific gamma-glutamylcyclotransferase
- Glutamate--cysteine ligase
- Aspartate aminotransferase
- aspartate transaminase
- Peptidase, putative
- Kynurenine aminotransferase, putative
- CAAX prenyl protease
Sequence:
MLKRVIARASLPKSLDVLPLFSFSKKGKGGIEKVAGDSQVKSLVSHPKCVSAHFCNPKDHSEALREDDDGGDVDKHDAVDVPFGFRDAPGNILLDPERRRLFAGIGEKPTVRDYRLAVTAAVREASKLKASALVMRSLPNVLYSVGDLFQPASALPAEDVAEKTVTYAVAAAYRYDRFLSKAKGGLPPPSRGRRNKAVAEGSHEQLNLIIDCGDKTSIASGNIIGHCINDARNLGNLREDEGTPQFYCEWIHQELAPLGIKVQNVLHGEQLEKAGLNLIYNVGKGSKHTPYLVVFEYVGDKRSNKATALVGKGVTFDCGGLNIKPFGSMETMHMDMMGAATVMATMKAIAELQLPVNVVAAVGLAENAIGPSSYHPSCILTSRKGLSVEVLNTDAEGRLVLADTLTYLQKDAKLVKKADTIIDIATLTGAIVVGLGSRRAGLFGNDIALVQQLMASGRSSGEEVWPMPIGDEHQRAIKGNIADLVNVPSVREGGSCTAAAFLSNFVEKDVKWAHLDIAGSGMGTDKPRGFQPAGAPGFGVELLVDYFRQHVMASSKGVSTGKDGSHGDAEESTQEEGANAEVSEENTKRSKTSAGGKKLTKNAEPKEGKGKEAKPNVKGTKGGRKVGEKGTEGKGKAASPAEKKRVKKAPAAKQGRRAVKGNPKGKKRSGN
Protein: 6-carboxy-5,6,7,8-tetrahydropterin synthase (CPH4 synthase) (EC 4.1.2.50) (Queuosine biosynthesis protein QueD) (P65870)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP.
Interaction partners:
- 7-carboxy-7-deazaguanine synthase
- GTP cyclohydrolase 1
- 7-cyano-7-deazaguanine synthase
- NADPH-dependent 7-cyano-7-deazaguanine reductase
- Dihydroneopterin triphosphate 2'-epimerase
- Epoxyqueuosine reductase
- Dihydroneopterin triphosphate diphosphatase
- Alkaline phosphatase
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreT
- S-adenosylmethionine:tRNA ribosyltransferase-isomerase
Sequence:
MMSTTLFKDFTFEAAHRLPHVPEGHKCGRLHGHSFMVRLEITGEVDPHTGWIIDFAELKAAFKPTYERLDHHYLNDIPGLENPTSEVLAKWIWDQVKPVVPLLSAVMVKETCTAGCIYRGE