wanglab/gogpt-training-data huggingface dataset:
Protein: Methylmalonic aciduria type A protein, mitochondrial (EC 3.6.-.-) (Q8IVH4)
Organism: Homo sapiens (Human)
Function: GTPase, binds and hydrolyzes GTP. Involved in intracellular vitamin B12 metabolism, mediates the transport of cobalamin (Cbl) into mitochondria for the final steps of adenosylcobalamin (AdoCbl) synthesis. Functions as a G-protein chaperone that assists AdoCbl cofactor delivery from MMAB to the methylmalonyl-CoA mutase (MMUT). Plays a dual role as both a protectase and a reactivase for MMUT. Protects MMUT from progressive inactivation by oxidation by decreasing the rate of the formation of the oxidized inactive cofactor hydroxocobalamin (OH2Cbl). Additionally acts a reactivase by promoting the replacement of OH2Cbl by the active cofactor AdoCbl, restoring the activity of MMUT in the presence and hydrolysis of GTP.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:28943303, ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:28943303}.
Interaction partners:
- Methylmalonyl-CoA mutase, mitochondrial
- Corrinoid adenosyltransferase MMAB
- Cobalamin trafficking protein CblD
- Lysosomal cobalamin transport escort protein LMBD1
- Methylmalonyl-CoA epimerase, mitochondrial
- Cyanocobalamin reductase / alkylcobalamin dealkylase
- Methionine synthase
- Methionine synthase reductase
- CD320 antigen
- E3 ubiquitin-protein ligase CBL
Sequence:
MPMLLPHPHQHFLKGLLRAPFRCYHFIFHSSTHLGSGIPCAQPFNSLGLHCTKWMLLSDGLKRKLCVQTTLKDHTEGLSDKEQRFVDKLYTGLIQGQRACLAEAITLVESTHSRKKELAQVLLQKVLLYHREQEQSNKGKPLAFRVGLSGPPGAGKSTFIEYFGKMLTERGHKLSVLAVDPSSCTSGGSLLGDKTRMTELSRDMNAYIRPSPTRGTLGGVTRTTNEAILLCEGAGYDIILIETVGVGQSEFAVADMVDMFVLLLPPAGGDELQGIKRGIIEMADLVAVTKSDGDLIVPARRIQAEYVSALKLLRKRSQVWKPKVIRISARSGEGISEMWDKMKDFQDLMLASGELTAKRRKQQKVWMWNLIQESVLEHFRTHPTVREQIPLLEQKVLIGALSPGLAADFLLKAFKSRD
Protein: 3-dehydro-D-guloside 4-epimerase (EC 5.1.3.-) (3-keto-D-guloside 4-epimerase) (P76044)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the epimerization at C4 of 3-dehydro-D-gulosides leading to 3-dehydro-D-glucosides. Probably functions in a metabolic pathway that transforms D-gulosides to D-glucosides. Can use methyl alpha-3-dehydro-D-glucoside and methyl beta-3-dehydro-D-glucoside as substrates in vitro. However, the actual specific physiological substrates for this metabolic pathway are unknown. Cannot act on D-psicose, D-fructose, D-tagatose, D-sorbose, L-xylulose, or L-ribulose.
Interaction partners:
- D-glucoside 3-dehydrogenase
- D-guloside 3-dehydrogenase
- Putative ABC transporter periplasmic-binding protein YcjN
- Inner membrane ABC transporter permease protein YcjO
- Kojibiose phosphorylase
- Inner membrane ABC transporter permease protein YcjP
- Beta-phosphoglucomutase
- Glucosylglycerate phosphorylase
- Uncharacterized HTH-type transcriptional regulator YcjW
- Outer membrane porin G
Sequence:
MKIGTQNQAFFPENILEKFRYIKEMGFDGFEIDGKLLVNNIEEVKAAIKETGLPVTTACGGYDGWIGDFIEERRLNGLKQIERILEALAEVGGKGIVVPAAWGMFTFRLPPMTSPRSLDGDRKMVSDSLRVLEQVAARTGTVVYLEPLNRYQDHMINTLADARRYIVENDLKHVQIIGDFYHMNIEEDNLAQALHDNRDLLGHVHIADNHRYQPGSGTLDFHALFEQLRADNYQGYVVYEGRIRAEDPAQAYRDSLAWLRTC
Protein: Large ribosomal subunit protein bL9m (39S ribosomal protein L9, mitochondrial) (L9mt) (MRP-L9) (Q2TBK2)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11279069}.
Interaction partners:
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL20m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL12m
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein uL13m
Sequence:
MAAAAFAVPRGVQLRVLTERLLRGGVRELLRPRLSGSTPGSERDFSLSHSRGTVIVERWWKVPLAGEGRKPRLHRRHRVYKLVEDTKHRPKENLELILTQSVDELGVRGDLVSVKKSVGRNRLLPEGLAVYASPENKKLFEEEKLLRQEGKLDKIQTKAGEATVKFLRSCHLEVGMKNNVKWELNPEIVARHFLRNLGVVVAPHALKLPEEPITQRGEYWCEVTVNGLDTVRVPMSVVNFERPKTKRYKYWLAQQAAKGMASTSFQKI
Protein: Vacuolar protein sorting-associated protein 54 (O14093)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in retrograde transport from early and late endosomes to late Golgi by linking the vesicle through the t-SNARE TGL1 to the Golgi, leading to the membrane fusion between late Golgi and endosomal vesicles. Seems also to be involved in protein transport from Golgi to the plasma membrane and is required for the integrity of the actin cytoskeleton (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}. Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 52
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 51
- t-SNARE affecting a late Golgi compartment protein 1
- Thioredoxin reductase
- t-SNARE affecting a late Golgi compartment protein 2
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 2
- Protein transport protein sec20
Sequence:
MERISSAPSISLGYPPTESSAHLAPSFSDSATSTLSFKSLLEDPVNPIRPVYTPTRTEITPVTLSPIPITPVREFQPYLHEISQEYARYSKQKRASLRRYLEKHGKLEGSMKESSINGSLLRRSSVSTILRPASESSYPNSNSETITYDIDDNVNPSSSLVDNFSISSVPSVFFQSDFNLDDPQIFDVVSEHIDITQTSDAPNSNRNLLLNNSMLQEKISWYLDTVELHLLQEIENASDSFPMIIDNLKQLKKETRDNVEETKHLLEKLTEVNVMCDRHMDAISSEELACHQLTQLKKVVQTLEDIYSEHKKVSEDVKDQRFLEAINGINSIVTQLKKKSTELNVDLLSLPSVKSLREEHKVLYHTVSQSVVQQFSKFLTSDMHKFSTILDSNELKDIYLSKNRLIPSVTKSLPSAMEFDADFLHEVDVCIDCLTLTDSLQAALTLYKTAVFEAFENLAQQYFTDGVEMRSVRKSSDLRRSLSAASLSSLSDSSRRSSSAANPFQSMSITEFAEMLTNIYFSSLECLRRIRSQIKVLIDILSKKDTKQYHLSVILNDLMATSSDVVTQQVTTINNLRFRVLDTYPPNNVIYLFSLHIIFHNELESLCGITQSSFIPTIMRQLLDWFKNFQRYSTQKLASSFERELWEAIPVEPSCQDLANRVFECSGNTPVEWTRLLSPEAEKEDENHRVHHVKVSEDCTATVSFGKQSLHIVRSSVTLLETLDDYGKLLAHFSRLAPEFQTGMLDMFRTLNSRVYQLILGAGTVRSSGLSKVLGKHIALASQTIALFQLSLNSMCRYLSRVTGTRLTNETNKLDQDFTVHHLQIHDKFVSLMRERVAISCSQIASLSWDIDSPHGYIIDLSKSLIKLYKVLHRYSQRDCVEVIPDVIRMFEDRLQLELTDIARNPSKWPGVRIDLSYFYDMMASKCGYAGDRTLLEKFERTPEQQEAA
Protein: Beta-crystallin A1 (Beta-A1-crystallin) (P02525)
Organism: Mus musculus (Mouse)
Function: Crystallins are the dominant structural components of the vertebrate eye lens.
Interaction partners:
- Alpha-crystallin A chain
- Alpha-crystallin B chain
- Filensin
- Lens fiber major intrinsic protein
- Gap junction alpha-8 protein
- Gap junction alpha-3 protein
- Beta-crystallin B1
- Phakinin
- Beta-crystallin B2
- Gamma-crystallin B
Sequence:
MLYLVLFLVPFNSIQITIYDQENFQGKRMEFTSSCPNVSERNFDNVRSLKVECGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKITIFEKENFIGRQWEICDDYPSLQAMGWFNNEVGSMKIQCGAWVCYQYPGYRGYQYILECDHHGGDYKHWPEWGSHAQTSQIQSIRRIQQ
Protein: Holocytochrome-c synthase (EC 4.4.1.17) (Cytochrome c heme lyase) (CCHL) (P06182)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q00873}. Mitochondrion intermembrane space {ECO:0000269|PubMed:22984289}.
Interaction partners:
- Cytochrome c isoform 2
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c isoform 1
- Cytochrome c lysine N-methyltransferase 1
- Holocytochrome-c1 synthase
- Threonine dehydratase, mitochondrial
- Ferrochelatase, mitochondrial
- Cytochrome c mitochondrial import factor CYC2
- Ubiquitin-conjugating enzyme E2 6
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MGWFWADQKTTGKDIGGAAVSSMSGCPVMHESSSSSPPSSECPVMQGDNDRINPLNNMPELAASKQPGQKMDLPVDRTISSIPKSPDSNEFWEYPSPQQMYNAMVRKGKIGGSGEVAEDAVESMVQVHNFLNEGCWQEVLEWEKPHTDESHVQPKLLKFMGKPGVLSPRARWMHLCGLLFPSHFSQELPFDRHDWIVLRGERKAEQQPPTFKEVRYVLDFYGGPDDENGMPTFHVDVRPALDSLDNAKDRMTRFLDRMISGPSSSSSAP
Protein: Steroid receptor seven-up, isoform A (Nuclear receptor subfamily 2 group F member 3, isoform A) (P16376)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor that is required in photoreceptors R1, R3, R4 and R6 during eye development; generation of the ganglion mother cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the transition in the expression of HB to KR in the neuroblasts (NBs).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
Interaction partners:
- Muscle-specific homeobox protein tinman
- Homeobox protein abdominal-A
- Ecdysone receptor
- Probable nuclear hormone receptor HR38
- Epidermal growth factor receptor
Sequence:
MCASPSTAPGFFNPRPQSGAELSAFDIGLSRSMGLGVPPHSAWHEPPASLGGHLHAASAGPGTTTGSVATGGGGTTPSSVASQQSAVIKQDLSCPSLNQAGSGHHPGIKEDLSSSLPSANGGSAGGHHSGSGSGSGSGVNPGHGSDMLPLIKGHGQDMLTSIKGQPTGCGSTTPSSQANSSHSQSSNSGSQIDSKQNIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYSCRGSRNCPIDQHHRNQCQYCRLKKCLKMGMRREAVQRGRVPPTQPGLAGMHGQYQIANGDPMGIAGFNGHSYLSSYISLLLRAEPYPTSRYGQCMQPNNIMGIDNICELAARLLFSAVEWAKNIPFFPELQVTDQVALLRLVWSELFVLNASQCSMPLHVAPLLAAAGLHASPMAADRVVAFMDHIRIFQEQVEKLKALHVDSAEYSCLKAIVLFTTGKLLDILYKDVPALLTKVSALLGKGSTASNDDVLAVVRDHLDELNRQEQESQAQQQAPLHLAAFMNCVAGVEAAVQQAEQAQVPTSSASASVSAPLVPSAGSAFSSCQAKSAGSEMDLLASLYAQAQATPPSSGGGDASGHNNSSGLGASLPTQSQSGSSSRNLTASPLSTSLATAPAPASASAPAPVPTSSVAQVPVPAPVPVTSSASSSSLGGGAYQTPSAAAAAAAMFHYQTPPRAAFGSAFDMFHHSTPFGVGVGHAHALAHSSGSGSASFGSPSYRYSPYSLAGSRWQL
Protein: Golgi brefeldin A resistant guanine nucleotide exchange factor 1 (A0A669KBG8)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MVDKNIYIIQGEINIVVGAIKRNARWSTHTPLDEERDPLLHSFGHLKEVLNSITELSEIEPNVFLRPFLEVIRSEDTTGPITGLALTSVNKFLSYALIDPTHEGTAEGMENMADAVTHARFVGTDPASDEVVLMKILQVLRTLLLTPVGAHLTNESVCEIMQSCFRICFEMRLSELLRKSAEHTLVDMVQLLFTRLPQFKEEPKNYVGTNMKKISPCLLNKLELSSGEQTKALNQLERVLLFKNLKLKMRAGGMSDSSKWKKQKRSPRPPRHMTKVTPGSELPTPNGTTLSSNLTGGMPFIDVPTPISSASSEAASAVVSPSTDSGLEFSSQTTSKEDLTDLEQPGSPGYSTATEPGSSELGVPEQPDLQEGTHVEKSQSASVESIPEVLEECTSPADHSDSASVHDMDYVNPRGVRFTQSSQKEGTALVPYGLPCIRELFRFLISLTNPHDRHNSEVMIHMGLHLLTVALESAPVAQCQTLLGLIKDEMCRHLFQLLSIERLNLYAASLRVCFLLFESMREHLKFQMEMYIKKLMEIITVENPKMPYEMKEMALEAIVQLWRIPSFVTELYINYDCDYYCSNLFEELTKLLSKNAFPVSGQLYTTHLLSLDALLTVIDSTEAHCQAKVLNSLTQQEKKETARPSCEIVDGTREASNTERTASDGKAVGMASDIPGLHLPGGGRLPPEHGKSGCSDLEEAVDSGADKKFARKPPRFSCLLPDPRELIEIKNKKKLLITGTEQFNQKPKKGIQFLQEKGLLTIPMDNTEVAQWLRENPRLDKKMIGEFVSDRKNIDLLESFVSTFSFQGLRLDEALRLYLEAFRLPGEAPVIQRLLEAFTERWMNCNGSPFANSDACFSLAYAVIMLNTDQHNHNVRKQNAPMTLEEFRKNLKGVNGGKDFEQDILEDMYHAIKNEEIVMPEEQTGLVRENYVWNVLLHRGATPEGIFLRVPTASYDLDLFTMTWGPTIAALSYVFDKSLEETIIQKAISGFRKCAMISAHYGLSDVFDNLIISLCKFTALSSESIENLPSVFGSNPKAHIAAKTVFHLAHRHGDILREGWKNIMEAMLQLFRAQLLPKAMIEVEDFVDPNGKISLQREETPSNRGESTVLSFVSWLTLSGPEQSSVRGPSTENQEAKRVALECIKQCDPEKMITESKFLQLESLQELMKALVSVTPDEETYDEEDAAFCLEMLLRIVLENRDRVGCVWQTVRDHLYHLCVQAQDFCFLVERAVVGLLRLAIRLLRREEISAQVLLSLRILLLMKPSVLSRVSHQVAYGLHELLKTNAANIHSGDDWATLFTLLECIGSGVKPPAALQATARADAPDAGAQSDSELPSYHQNDVSLDRGYTSDSEVYTDHGRPGKIHRSATDADVVNSGWLVVGKDDVDNSKPGPSRPGPSPLINQYSLTVGLDLGPHDTKSLLKCVESLSFIVRDAAHITPDNFELCVKTLRIFVEASLNGGCKSQEKRGKSHKYDSKGNRFKKKSKEGSMLRRPRTSSQHASRGGQSDDDEDEGVPASYHTVSLQVSQDLLDLMHTLHTRAASIYSSWAEEQRHLETGGQKIEADSRTLWAHCWCPLLQGIACLCCDARRQVRMQALTYLQRALLVHDLQKLDALEWESCFNKVLFPLLTKLLENISPADVGGMEETRMRASTLLSKVFLQHLSPLLSLSTFAALWLTILDFMDKYMHAGSSDLLSEAIPESLKNMLLVMDTAEIFHSADARGGGPSALWEITWERIDCFLPHLRDELFKQTVIQDPMPMEPQGQKPLASAHLTSAAGDTRTPGHPPPPEIPSELGACDFEKPESPRAASSSSPGSPVASSPSRLSPTPDGPPPLAQPPLILQPLASPLQVGVPPMTLPIILNPALIEATSPVPLLATPRPTDPIPTSEVN
Protein: Single-stranded-DNA-specific exonuclease RecJ (EC 3.1.-.-) (P21893)
Organism: Escherichia coli (strain K12)
Function: Single-stranded-DNA-specific exonuclease. Required for many types of recombinational events, although the stringency of the requirement for RecJ appears to vary with the type of recombinational event monitored and the other recombination gene products which are available.
Interaction partners:
- ATP-dependent DNA helicase RecQ
- Exodeoxyribonuclease I
- DNA repair protein RecO
- DNA replication and repair protein RecF
- Crossover junction endodeoxyribonuclease RuvC
- DNA helicase II
- Recombination protein RecR
- ATP-dependent DNA helicase RecG
- DNA repair protein RecN
- Protein RecA
Sequence:
MKQQIQLRRREVDETADLPAELPPLLRRLYASRGVRSAQELERSVKGMLPWQQLSGVEKAVEILYNAFREGTRIIVVGDFDADGATSTALSVLAMRSLGCSNIDYLVPNRFEDGYGLSPEVVDQAHARGAQLIVTVDNGISSHAGVEHARSLGIPVIVTDHHLPGDTLPAAEAIINPNLRDCNFPSKSLAGVGVAFYLMLALRTFLRDQGWFDERNIAIPNLAELLDLVALGTVADVVPLDANNRILTWQGMSRIRAGKCRPGIKALLEVANRDAQKLAASDLGFALGPRLNAAGRLDDMSVGVALLLCDNIGEARVLANELDALNQTRKEIEQGMQIEALTLCEKLERSRDTLPGGLAMYHPEWHQGVVGILASRIKERFHRPVIAFAPAGDGTLKGSGRSIQGLHMRDALERLDTLYPGMMLKFGGHAMAAGLSLEEDKFKLFQQRFGELVTEWLDPSLLQGEVVSDGPLSPAEMTMEVAQLLRDAGPWGQMFPEPLFDGHFRLLQQRLVGERHLKVMVEPVGGGPLLDGIAFNVDTALWPDNGVREVQLAYKLDINEFRGNRSLQIIIDNIWPI
Protein: Kininogen [Cleaved into: Bradykinin] (A0A1S3PBB7)
Organism: Salmo salar (Atlantic salmon)
Function: Inhibits papain and ficin (cysteine proteinases) but not trypsin (a serine proteinase).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12397376}. Vacuole {ECO:0000269|PubMed:12397376}.
Interaction partners:
- B1 bradykinin receptor
- B2 bradykinin receptor
- B2 bradykinin receptor
- B1 bradykinin receptor
- B1 bradykinin receptor-like
- Kininogen-1-like
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4
- Complement component 1 Q subcomponent-binding protein
- Complement component 1 Q subcomponent-binding protein
Sequence:
MKLGVRLCVLVVFSLQLWGPGQGQELEPEQVLAFCDDKDVEAAVDLALVKYNQKLPYGNQLALYQILESSKAQNDSCTQYFVEFNSRVTDCPAGGDKVWRDCDYLPTGNKVPRPCKATVHMSETDKKVLAVFCDPVEAPVVAERTTCLGCPREIDVESEDLKDPLTYSITRFNADSDSSHHFILNSVGFATRQVVAGFRYRLMFDMRKSNCSKADHKELNDECHPDPDVELAHCNSTVDVAPWRHETAEANVECAPGPLDNFDVFRRRPPGWSPLRNFNNFAEVKTTQASTASAKEESSEESQERSPSAVTMANPEPALPSVAPTTAAESPFHCPSKPWKQFVPPTTLRPAQEKSPTPLPVVEEGLSDLDLLGKK
Protein: Uncharacterized protein ycf73 (P0C311)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MTKDETLLVFTLVVSSVSVFLFGILLFMVLISATRDFRERTKSKLVKIMIWAGIVVITFAIAVRIYPIFIFLLKERIKPLVEALYDKLPWIWEVSLSRYWDRLIDFLDRYLWACAQRIQTGIRKQKGEFVVTFSCRVKKRLYARAIEVGIHLSLLSNLFWILKTTLAVGYRLLWVLYYIISFEGFLGSFRLYLVYFGFYCLLFSGKWLRTSEDRGERQAQISGILLRGMLIECAFSVLCLEEDSNLHAL
Protein: Integrin beta (Q3YAA0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
Sequence:
MDVRLLLISVLLGLSRAQQDGNECTKASAQSCGECIQAGEKCGWCTDEGFLKQGEQKSTRCDEIEALEKKGCSKASIENPRGKITIVKNQPVTNRTKNGAKLKPDQITQIQPQQLSLNLRSGEAQKFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKNLGTDLMKEMQKITSDFRIGFGSFVEKTVMPYISTTPAKLLNPCTSDQNCTSPFSYKNVLSLTDDGSQFNSLVSRQQISGNLDSPEGGFDAIMQVAVCGNQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGKCHLQDNIYTMSHYYDYPSIAHLVQKLSENNIQTIFAVTEEFQPVYQELKNLIPKSAVGTLTSDSNNVIKLIIDAYNSLSSEVILENSKLPEGVSISYVSHCKNGVSGTGDTGRKCSNISIGDEVAFEVAITAKGCPLNGKSETMKIKLLGFTEEVEVVLNFICECECHKDGIKNSPVCHFGNGTLECGACRCNEGRIGRVCECSKDEVRTEDLDANCRMDNGTDICSNNGDCVCGTCECKKRDNPEERYSGKFCECDNFNCDRSNNKLCGGHGRCDCRKCICDANYTGSACDCSLDTSTCLASNKQICNGRGNCECGACKCTDTKFQGPTCEICPTCPGVCTEHKDCVQCRAFGTGDKKDTCEEQCSYFTMKVVKKKEDLPQPNDQPIINHCKERDANDCWFFFTYATRNDSSVMVHVAEELECPSGPDIIPIVAGVVAGIVLIGLALLLIWKLLMIIHDRREFAKFEKEKMNAKWDAGENPIYKSAVTTVVNPKYEGK
Protein: Synaptotagmin-8 (Synaptotagmin VIII) (SytVIII) (Q9R0N6)
Organism: Mus musculus (Mouse)
Function: Involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation of exocytosis in insulin secreted cells.
Subcellular location: Cytoplasm. Cell membrane; Single-pass type III membrane protein. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11751263}.
Interaction partners:
Sequence:
MQADRSMKMGHALNPFSTSAPLDATAGPSLIPDLITRIPWPRWTLFIAILAAGVLLVSCLLCVICCYCHRHRHRKQPKDKETVGLGSARNSTTTHLVQPDVDCLEPCSGGDQQWGRLLLSLEYDFGSQEIRVGLRQAGNLKAEGTADPYAWVSVSTQSGRRHETKVHRGTLSPMFEETCCFLVPPAELPKATLKVQLWDFKRFSEHEPLGELQLPLGTVDLQHVLESWYQLGPPGTTEPEQMGELCFSLRYVPSSGSLTVVVLEARGLNPGLAEAYVKIQLMLNQRKWKKSKTSSKKGTTTPYFNEAFVFLVPVSQLQSVDLVLAVWARGLQLRTEPVGKVLLGSRASGQPLQHWADMLAHARRPIAQWHHLRSPREVDRVLALQPRLPLLRPRS
Protein: Muc10 protein (Q8VC95)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKNEMFILGLLALTSYFMPGESHHKSRSSQFPVRKYLEDPRYPRYPRPHYSYGFIPSSPKFPKDNQWYKMCPPGTTLMLISRRSPKFLCIPKRQIISDKTKPNATTPATTTKSTTKEPTTSPKPSTSTAIPTTTKSANSTSSTTTSTTIQTTAPTFAEVFWKFFQQIFRLKK
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 (EC 3.1.3.95) (FYVE domain-containing dual specificity protein phosphatase 1) (FYVE-DSP1) (Myotubularin-related protein 3) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Zinc finger FYVE domain-containing protein 10) (Q13615)
Organism: Homo sapiens (Human)
Function: Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11676921}. Membrane {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11676921}; Peripheral membrane protein {ECO:0000269|PubMed:10733931, ECO:0000269|PubMed:11676921}.
Interaction partners:
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4
- 1-phosphatidylinositol 3-phosphate 5-kinase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Polyphosphoinositide phosphatase
- Inositol polyphosphate 4-phosphatase type II
- Inositol polyphosphate-4-phosphatase type I A
- Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Type 2 phosphatidylinositol 4,5-bisphosphate 4-phosphatase
- Phosphatidylinositide phosphatase SAC2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
Sequence:
MDEETRHSLECIQANQIFPRKQLIREDENLQVPFLELHGESTEFVGRAEDAIIALSNYRLHIKFKESLVNVPLQLIESVECRDIFQLHLTCKDCKVIRCQFSTFEQCQEWLKRLNNAIRPPAKIEDLFSFAYHAWCMEVYASEKEQHGDLCRPGEHVTSRFKNEVERMGFDMNNAWRISNINEKYKLCGSYPQELIVPAWITDKELESVSSFRSWKRIPAVIYRHQSNGAVIARCGQPEVSWWGWRNADDEHLVQSVAKACASDSRSSGSKLSTRNTSRDFPNGGDLSDVEFDSSLSNASGAESLAIQPQKLLILDARSYAAAVANRAKGGGCECPEYYPNCEVVFMGMANIHSIRRSFQSLRLLCTQMPDPGNWLSALESTKWLHHLSVLLKSALLVVHAVDQDQRPVLVHCSDGWDRTPQIVALAKLLLDPYYRTIEGFQVLVEMEWLDFGHKFADRCGHGENSDDLNERCPVFLQWLDCVHQLQRQFPCSFEFNEAFLVKLVQHTYSCLFGTFLCNNAKERGEKHTQERTCSVWSLLRAGNKAFKNLLYSSQSEAVLYPVCHVRNLMLWSAVYLPCPSPTTPVDDSCAPYPAPGTSPDDPPLSRLPKTRSYDNLTTACDNTVPLASRRCSDPSLNEKWQEHRRSLELSSLAGPGEDPLSADSLGKPTRVPGGAELSVAAGVAEGQMENILQEATKEESGVEEPAHRAGIEIQEGKEDPLLEKESRRKTPEASAIGLHQDPELGDAALRSHLDMSWPLFSQGISEQQSGLSVLLSSLQVPPRGEDSLEVPVEQFRIEEIAEGREEAVLPIPVDAKVGYGTSQSCSLLPSQVPFETRGPNVDSSTDMLVEDKVKSVSGPQGHHRSCLVNSGKDRLPQTMEPSPSETSLVERPQVGSVVHRTSLGSTLSLTRSPCALPLAECKEGLVCNGAPETENRASEQPPGLSTLQMYPTPNGHCANGEAGRSKDSLSRQLSAMSCSSAHLHSRNLHHKWLHSHSGRPSATSSPDQPSRSHLDDDGMSVYTDTIQQRLRQIESGHQQEVETLKKQVQELKSRLESQYLTSSLHFNGDFGDEVTSIPDSESNLDQNCLSRCSTEIFSEASWEQVDKQDTEMTRWLPDHLAAHCYACDSAFWLASRKHHCRNCGNVFCSSCCNQKVPVPSQQLFEPSRVCKSCYSSLHPTSSSIDLELDKPIAATSN
Protein: WLM domain-containing protein (Q381Y4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPVTTHFSSIGVKQSEVIETATTLGWTNDHQAQDYLQKLLIIGRPILRAHNWKIHRLKEFYPRSARLLGQNFNRGEEVCVRFRVPKEKNTFFPFHEVVCTFLHELAHCKYSKHDRHFWELYTELSVECCRLDLNASLEREAAAPPDRRHTGSGRRLGGSRIVPLPREPEAMRRILSEAAERRRQSSENGQCYGCAHDKTGVGSELNDGLWTCDNCDGVIDALRGKCEFCVEVGDSTEQVEEWSCKRCSFHNHCALVQCEACGRFKSGRTADGTNTVHTVKALAASSDHLLFTMTLGRVADALAPILQEMRWSVACLEEFAPPLKRVMSRSSFKNSNECDTLSIRLRSPNNPHEPLTFTCVLAHALHQLAHLTEKNHGANFVHTWIAMIHRFLTETKAFSDDFISSQEQEDLLCLAMELELLLNGLSGRDTALCDDLLDNVPHLQRLFENCATFVKRERLFTVATTREAGVVGHSKHLELWQCRRCSVNNNGGFIIFCEVCGAPRQLSVLLRTSRTVAVRAASNETVIDISDDDGDDGSATSAGEATISPGVVFIID
Protein: Probable trehalose-phosphate phosphatase J (AtTPPJ) (EC 3.1.3.12) (Trehalose 6-phosphate phosphatase) (Q5HZ05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance (By similarity).
Interaction partners:
- Trehalase
- Alpha,alpha-trehalose-phosphate synthase 1
- Probable alpha,alpha-trehalose-phosphate synthase 4
- Probable alpha,alpha-trehalose-phosphate synthase 2
- Alpha,alpha-trehalose-phosphate synthase 5
- Alpha,alpha-trehalose-phosphate synthase 6
- Probable alpha,alpha-trehalose-phosphate synthase 10
- Probable alpha,alpha-trehalose-phosphate synthase 3
- Probable alpha,alpha-trehalose-phosphate synthase 8
- Sucrose synthase 5
Sequence:
MVSQNVVVSDAKTGIITVSTVSNSSVFTPTAQKPPTAPGYISVSKKKLLKNLEINGADQSQRLNSWVDSMRASSPTHLKSLSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKLLRGRGQGFGILVSKFPKDTSASYSLQDPPEVMNFLGRLVEWKQMQQ
Protein: Gamma-aminobutyric acid receptor subunit alpha-2 (GABA(A) receptor subunit alpha-2) (GABAAR subunit alpha-2) (P26048)
Organism: Mus musculus (Mouse)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer. The alpha2/beta2/gamma2 receptor exhibits synaptogenic activity whereas the alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:11528422}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:28978485}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P23576}. Cell projection, dendrite {ECO:0000269|PubMed:28978485}.
Interaction partners:
- Rho guanine nucleotide exchange factor 9
- Gamma-aminobutyric acid receptor subunit beta-1
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
- Gamma-aminobutyric acid receptor subunit beta-2
- Trafficking protein, kinesin binding 2
- Huntingtin-associated protein 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit gamma-1
Sequence:
MKTKLSTCNVWSLLLVLLVWDPVRLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLLGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKGSVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP
Protein: EELM2 domain-containing protein, putative (Q8IHU7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Histone deacetylase
- Heterochromatin protein 1
- Chromatin assembly factor 1 protein WD40 domain, putative
- Chromatin assembly factor 1 subunit B, putative
- Chromatin assembly factor 1 P55 subunit, putative
- Potassium channel domain-containing protein
- 3'-5' exonuclease
Sequence:
MEKKSVSMQNKVKKKCIDKSKGKDTNAIKSNGVNNNKNGTYNNNDKKINNKNLKPSDANVDIKNYSDNNENDSFCYECYHGGNLVCCDNCIRSYHLYCLSSSDKPQPNFNYWYCPLCKRRGVTVDASLKRRKKIKTIKTVEKKKDKVKQKSEGSKYTNQINVGENYQVSNVSTFFLNSHSEKYDETSKSELVYSPYLLERMKENYLSEGQYELVIKNDYELAIFIKELAKNWKCQLGWHPFTPEYAFKILHHVDYNPKKAIELLKSSEFNFLEICDPPIRKYENKWRPRDKRGQISDSPYPSSELLQSYLKRSVEFSLDEKKYHYPVNTGNKFYCEINKNNIIETNYPNERTRNSLRKEIEEDDDEEDDYEDDDLEEEEEDDKDDEEYYEEYDK