wanglab/gogpt-training-data huggingface dataset:
Protein: Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)] (Q07258)
Organism: Rattus norvegicus (Rat)
Function: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively.
Subcellular location: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}.
Interaction partners:
- TGF-beta receptor type-2
- TGF-beta receptor type-1
- Endoglin.
- Latent-transforming growth factor beta-binding protein 1
- Transforming growth factor beta receptor type 3
- Activin receptor type-1-like
- Transforming growth factor beta-1 proprotein
- Receptor protein serine/threonine kinase
- Decorin
- Fibromodulin
Sequence:
MKMHLQRALVVLALLNLATVSLSLSTCTTLDFGHIKKKRVEAIRGQILSKLRLTSPPEPSVMTHVPYQVLALYNSTRELLEEMHGEREEGCTQETSESEYYAKEIHKFDMIQGLAEHNELAVCPKGITSKVFRFNVSSVEKNGTNLFRAEFRVLRVPNPSSKRTEQRIELFQILRPDEHIAKQRYIGGKNLPTRGTAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENVHEVMEIKFKGVDNEDDHGRGDLGRLKKQKDHHNPHLILMMIPPHRLDSPGQGGQRKKRALDTNYCFRNLEENCCVRPLYIDFRQDLGWKWVHEPKGYYANFCSGPCPYLRSSDTTHSTVLGLYNTLNPEASASPCCVPQDLEPLTILYYVGRTPKVEQLSNMVVKSCKCS
Protein: Nucleoside diphosphate kinase, mitochondrial (NDK) (NDP kinase) (EC 2.7.4.6) (P34093)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Subcellular location: Mitochondrion intermembrane space.
Interaction partners:
- CTP synthase
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
- Thymidylate kinase
- Inosine triphosphate pyrophosphatase
- Guanosine-3',5'-bis
- Ribonucleoside-diphosphate reductase large subunit
- UMP-CMP kinase
- Probable nucleoside diphosphate kinase DDB_G0292928
- Guanylate kinase
- dCTP deaminase
Sequence:
MFSRFARAFPKILASGASQRTFATVQKAFANPTSKKLIVGSSLLIGSAFATTSFVACENKSVPLVGLPGTNQERSFIAIKVSSTQRRLIGEIIARFEKKGFKLVGIKILVPTPEHAAKHYEDLNKKPFFNGLVKFFSSGAVVAMVFEGKDVVRTGRVLIGATDPSQSAPGTIRFDLCIETGRNIIHGSDSNESAAHEIALWFKEDEIANWVSTNPVYEKM
Protein: Pollux, isoform D (Q8IPP5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFTVPFHRDTILTTSVSDASVLNKSRAMAELMHQMRDPAHTLGGSVGSIPQTLIGGGGGSHGNSNGALNGIHATPATNLKMSEAMRNAQHDTSPNPVSSKMKASKSYTHGLSSSSGTVNIPTSTSAQSNLSLLADISPNHTHFFEVMYVGKIRVSQKRVPNTFIDDALPKFKAYDAQRLRLLQNRKMSLSSEGGVGIEAKPSSSLKSHDLKEEDEEEQEQHKGHDDSQDSQAKPLVQLQLTGAEEGAAPRPLEDNKENKSPEKRPLLRGQSQIELGHKEHSDGSQPLAANSQLEAPNVIVNKQPTPPRDQGVGTGTASASAGPSQLHPNYAMDNIPKQRDRSASQGCIPPYVEQNRTMVFLVGRCDLRLISPDRKQVLLYKDFKDVASCVHGQKSLDHFGIICRELNNDGYIGYVFKCQSEHVCDDIVAAIAQAFDTCAEQKKKQDTQIFSCEHCPMLWYHKLCTDVEGLSEKKTQALILRRIETLSDDEQEIVWAKFCGSEKTNSPVAEQNQFLMMLLRAHCESRQQRHVHDTAENRSEFLNQYLGGSTIFMKAKRSLTNSFDNLLKRKPSKDDIAVPSHNLRDIREGSAEPLGTQSPPEGFRSRSNTVGASPSSKPTAEQLKSPMMDIFIKVGNSPKEAETHQGSWRQAILNSVVTPSKGLDSEVPTEFLSPMRKPAKRGKRDAAELRELWRTAIRQTIMLNRMETENAMLQARQNENELKRIKLDYEEIVPCDKQLIERWEQIIERNSTQIGNKKDPKVLGHAIRTGVPRSKRGDVWTFLAEQHSMNTAPVDTKRFPNFNTPYHMLLKHLTEHQHAIFIDLGRTFPNHQFYKDPLGLGQLSLFNLLKAYSILDPELGYCQGLGFICGVLLLHCDEANSFQLLKHLMFRRNMRTKYLPDMKKFQLQLYQLSRLVKDHLPDLYVWLDQNDVSPTLYAAPWILTVFSSQFPLGFVARVFDLLFLESSDVIFKFAIALLSVHKQQLLAKDNFEEIMDYLKTVVPKMEHTCMEQIMKLVFSMDIGKQLAEYKVEYNVLQEEITTTNHHLEMLNREKTQNQHLEQQLQFAQSSIAQLETTRSSQQAQITTLQSQVQSLELTIQTLGRYVGQLVEHNPDLELPNEVRRMLQQLDDLDRQRRKPIFTERKIGKSVSVNSHLGFPLKVLEELTERDELGSPQKQKKEKTPFFEQLRQQQQQHRLNGGGQSSNVGESGSPTPPSRPNRLLDNASARTVMQVKLDELKLPEHVDKFVANIKSPLEVDSGVGTPLSPPSTASNSSGGSIFSRMGYRTTPPALSPLAQRQSYGVAITTAPCPQHMEEVAPATTMAVMPQEDVEEPQPMHPLSMVGGDVNVRFKGTTQLKSIRPVHHMRAIPLGGVQHPSSTEPAVRVAPVPVELAPPAATATTGRS
Protein: Proliferating cell nuclear antigen 1 (PfPCNA1) (P31008)
Organism: Plasmodium falciparum (isolate K1 / Thailand)
Function: Auxiliary protein of DNA polymerase delta and is involved in the control of DNA replication by increasing the polymerase processibility during elongation of the leading strand. Involved in DNA damage response (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P61074}. Chromosome {ECO:0000250|UniProtKB:P61074}. Cytoplasm {ECO:0000250|UniProtKB:P61074}. Note=During early-to mid replicating trophozoite stages, colocalizes with ORC1 and ORC5 to distinct nuclear foci which probably are DNA replication origin sites. Dissociates from ORC1 and ORC5 during the late schizont stage. {ECO:0000250|UniProtKB:P61074}.
Interaction partners:
Sequence:
MLEAKLNNASILKKLFECIKDLVNDANVDADESGLKLQALDGNHVSLVSLHLLDSGFSHYRCDRERVLGVNIASLNKVFKLCGANESVVISSKDDEDNLNFVFENNKEDKVTNFSLKLMSIELDSLNIPDCEEGFDAEVELSSKELTNIFRNLSEFSDTVFIEIDSNCIKFTTKGIVGDAEVALKPRDSTSEDDIGVTIKSKKKIKQSFAIKYLNLFSKSNILADVVVLGLSDSRPIEFKYEIKDTSPDSDTLKIGFVKFFLAPKMDDDMDNKD
Protein: Enoyl-CoA hydratase, mitochondrial (mECH) (mECH1) (EC 4.2.1.17) (EC 5.3.3.8) (Enoyl-CoA hydratase 1) (ECHS1) (Short-chain enoyl-CoA hydratase) (SCEH) (P30084)
Organism: Homo sapiens (Human)
Function: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-CoA) to the corresponding (3S)-3hydroxyacyl-CoA species through addition of a water molecule to the double bond. Catalyzes the hydration of medium- and short-chained fatty enoyl-CoA thioesters from 4 carbons long (C4) up to C16. Has high substrate specificity for crotonyl-CoA ((2E)-butenoyl-CoA) and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA (3-methyl-(2E)-butenoyl-CoA) and methacrylyl-CoA ((2E)-2-methylpropenoyl-CoA). Can bind tiglyl-CoA (2-methylcrotonoyl-CoA), but hydrates only a small amount of this substrate. Plays a key role in the beta-oxidation spiral of short- and medium-chain fatty acid oxidation. At a lower rate than the hydratase reaction, catalyzes the isomerase reaction of trans-3-enoyl-CoA species (such as (3E)-hexenoyl-CoA) to trans-2-enoyl-CoA species (such as (2E)-hexenoyl-CoA), which are subsequently hydrated to 3(S)-3-hydroxyacyl-CoA species (such as (3S)-hydroxyhexanoyl-CoA) (By similarity).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Peroxisomal acyl-coenzyme A oxidase 1
- Trifunctional enzyme subunit beta, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
Sequence:
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
Protein: Cilia- and flagella-associated protein 45 (Coiled-coil domain-containing protein 19) (Nasopharyngeal epithelium-specific protein 1) (Q9UL16)
Organism: Homo sapiens (Human)
Function: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity). It is an AMP-binding protein that may facilitate dynein ATPase-dependent ciliary and flagellar beating via adenine nucleotide homeostasis. May function as a donor of AMP to AK8 and hence promote ADP production.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33139725, ECO:0000269|PubMed:36191189}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33139725}. Cell projection, cilium {ECO:0000269|PubMed:31429579}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:31429579}. Note=Located in the proximal region of respiratory cilia. {ECO:0000269|PubMed:33139725}.
Interaction partners:
- Enkurin
- Cilia- and flagella-associated protein 52
- EF-hand domain-containing protein 1
- EF-hand domain-containing family member C2
- Tektin-2
- Tektin-1
- Protein Flattop
- Cilia- and flagella-associated protein 161
- EF-hand domain-containing family member B
- Parkin coregulated gene protein
Sequence:
MPLSTAGILSSSSAASNRSRNKARYRTKAVSSEVDESLFGDIKSPAQGQSDSPIVLLRDKHTLQKTLTALGLDRKPETIQLITRDMVRELIVPTEDPSGESLIISPEEFERIKWASHVLTREELEARDQAFKKEKEATMDAVMTRKKIMKQKEMVWNNNKKLSDLEEVAKERAQNLLQRANKLRMEQEEELKDMSKIILNAKCHAIRDAQILEKQQIQKELDTEEKRLDQMMEVERQKSIQRQEELERKRREERIRGRRQIVEQMEKNQEERSLLAEQREQEKEQMLEYMEQLQEEDLKDMERRQQQKLKMQAEIKRINDENQKQKAELLAQEKLADQMVMEFTKKKMAREAEFEAEQERIRREKEKEIARLRAMQEKAQDYQAEQDALRAKRNQEVADREWRRKEKENARKKMETEAELRKSRLEQVAFKEHALAVQVQRDRDEFERILRAQREQIEKERLEEEKKATGRLQHANELRRQVRENQQKEVQNRIATFEEGRRLKEEAQKRRERIDEIKRKKLEELRATGLPEKYCIEAERKANILPATSVN
Protein: Guanine nucleotide-binding protein subunit gamma (O94309)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cell membrane {ECO:0000305|PubMed:11238401}; Peripheral membrane protein {ECO:0000305|PubMed:11238401}; Cytoplasmic side {ECO:0000305|PubMed:11238401}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein alpha-2 subunit
- Guanine nucleotide-binding protein negative regulator 1
- Glucose receptor protein git3
- Adenylate cyclase
- 3',5'-cyclic-nucleotide phosphodiesterase
- cAMP-dependent protein kinase regulatory subunit
- Glucose-insensitive transcription protein 7
- Adenylate cyclase activation protein git1
- cAMP-dependent protein kinase catalytic subunit
Sequence:
METEALLNEKISVQQARQEFANYANNIPEPMMVSVAPPKANPSVSSKTKQQQHFKPGKATKDKATTKCCTIS
Protein: Pyruvate kinase (PK) (EC 2.7.1.40) (P46614)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Enolase 1
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- Phosphoglycerate mutase
- Pyruvate decarboxylase
- Phosphoglycerate kinase
- Pyruvate carboxylase
- Phosphoenolpyruvate carboxykinase
- malate dehydrogenase
Sequence:
MSHSSLSWLSNFNVETVPSKYLRRSSIIGTIGPKTNNVDVLVKLRKAGLNVVRMNFSHGSYEYHQSVIDNARKSEEVYKGRPLAIALDTKGPEIRTGTTIGDKDYPIPPNHEMIFTTDDAYKTKCDDKVMYIDYKNITKVIAPGKIIYVDDGVLSFEVISVDDEQTLKVRSLNAGKISSHKGVNLPGTDVDLPALSEKDIADIKFGVKNKVHMIFASFIRTANDVLEIRKVLGEEGKDIQIISKIENQQGVNNFDEILEVTDGVMVARGDLGIEIPAPQVFVVQKQLIAKCNLAAKPVICATQMLESMTYNPRPTRAEVSDVGNAILDGADCVMLSGETAKGNYPVEAVSMMHNTCLTAEKAIAYPQLFNELRSLAKKPTATTETCAVAAVSAAYEQDAKAIVVLSTSGLSARLVSKYKPDVPILMVTRNERAAKFSHLYRGVYPFIYDKPSIENWQEDVENRLRWAVSEAVELGIISKGDSIVTVQGWTRGSGHSNTVRIVQA
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (M9PCA2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLRSLATTRNELGALRSVLLRSNNATYVRRSTGNVVVRALSSQLINSRKLQSIRSKLNTSQSPVTWSYNFARAYANLPEHIRVPLPALSPTMERGSIVSWEKKEGDKLNEGDLLCEIETDKATMGFETPEEGFLAKILIQGGTKDVPVGQLLCIIVPDQGSVAAFANFKDDGAAAAPAAPAAAPAPAPAAAAAPPPPPPPAAAPAAAAPPPAPAAAPAAAGQKAAAKPAAAAPAKAPRAAGARYEDIPVTNMRAVIAKRLLESKTQLPHYYVTVQCQVDKLLKFRAKVNKKYEKQGARVSVNDFIIKAVAIASLKVPEANSAWMDTVIRKYDDVDVSVAVSTDKGLITPIVFNADRKGVLEISKDVKALAAKARDNKLQPHEFQGGTISVSNLGMFGVNQFAAVINPPQSCILAIGTTTKQLVADPDSLKGFKEVNMLTVTLSADHRVVDGAVAARWLQHFRDYMEDPSNMVL
Protein: Peroxisomal ATPase PEX1 (Peroxin-1) (Q9Y090)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MFKRTFKVVYRPIRSNFVLLPDQYYGVVSTYDTGCLSLQYNGRTHYASWAPQKGGGGIKDTEIGINARAAKEIGLHENDLVKCALIADVLNLRSVHVTPVSSKDWEIIELSTEKISGSVLEQTRIVNSTQILIVWINKSMQVALTVDRLKPHMNYGRIDHNTELVVAPNLYKGLTNGTSNGVIEENTKLSRSKTTAQVKDELTEKLTPLTHSSTVSNVKNTIQRNKRQDHMERLKKDLRRESSRSFEFRVIRGLWREQAQESDVFVNGKHLPEFFDLDLFYCMHTASDKDYYVRVRTVEDDIEDDLPETIHPSIELNANLMKLLGIKELERVVLRPKTTVVNFVEKIELFANKKTHYKIMENAFKRFVIERTQHKPMLFNQEEVVRLEDDLLVTVGILPEHFRYCVVDAQFLKESKIYAADLVRPVGEIIKEETPPTSPLSVQDLIQLPEYDKIVDQVVQELRMNLCLSADNSVMRQCNVLLAGASGTGKTVLVERILDQLSRKPDYCHFEFFHGSRSKGRKTESIQKDLRNIFTSCLQHAPAIVVLENLDVLAHAAGEQSSQDGEYYNRMADTVYQLIVQYTTNNAIAVIATVNELQTLNKRLSSPRGRHVFQTVARLPNLERADREIILRELCSHINVAKDLDLVKFSNLTEGYRKCDLVQFVERAIFYAYRISKTQPLLTNDQLIESLEHTNSYCLQGIQSNQRTGNDADANEMRVEELPGLESVVGVLEEVLMWPSRYPTIFNASPLRNQAGVLLYGPPGTGKTYLVSQLATSWNLRIISVKGPELLAKYIGQSEENVRNLFNRARSARPCVLFFDEFDSLAPKRGHDSTGVTDRVVNQLLTELDGVEGLQGVTVIAATSRPELLDPALLRSGRIDRLVECPLPDAPARVRIFEALSSTLSLDECVDFDWFAGKTANYTGADIQSILTSANMAAVKEALAQFGHEKLAKKISLKQKHLIESFQTTRPSLSASDVAKYHRTYARFTNKEKTSREFVAKRATLA
Protein: RIC3 acetylcholine receptor chaperone, isoform M (RIC3 acetylcholine receptor chaperone, isoform U) (E1JGP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGCCDVVLDREQFLNATKKDTVEPFGPHLYRKQINVYTGEISLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLVVTAIQGLIDAADEQLNGQDKQRATSDTETDSNKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ
Protein: Secretion-regulating guanine nucleotide exchange factor (Deafness locus-associated putative guanine nucleotide exchange factor) (DelGEF) (Guanine nucleotide exchange factor-related protein) (Q9UGK8)
Organism: Homo sapiens (Human)
Function: Probable guanine nucleotide exchange factor (GEF), which may be involved in the secretion process.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10571079}. Nucleus {ECO:0000269|PubMed:10571079}.
Interaction partners:
- Diphthamide biosynthesis protein 3
- Exocyst complex component 2
- Harmonin
Sequence:
MEREPSASEAAPAAAALFAWGANSYGQLGLGHKEDVLLPQQLNDFCKPRSVRRITGGGGHSAVVTDGGDLFVCGLNKDGQLGLGHTEDIPYFTPCKSLFGCPIQQVACGWDFTIMLTENGQVLSCGSNSFGQLGVPHGPRRCVVPQAIELHKEKVVCIAAGLRHAVAATASGIVFQWGTGLASCGRRLCPGQTLPLFFTAKEPSRVTGLENSKAMCVLAGSDHSASLTDAGEVYVWGSNKHGQLANEAAFLPVPQKIEAHCFQNEKVTAIWSGWTHLVAQTETGKMFTWGRADYGQLGRKLETYEGWKLEKQDSFLPCSRPPNSMPSSPHCLTGATEVSCGSEHNLAIIGGVCYSWGWNEHGMCGDGTEANVWAPKPVQALLSSSGLLVGCGAGHSLALCQLPAHPALVQDPKVTYLSPDAIEDTESQKAMDKERNWKERQSETSTQSQSDWSRNGGL
Protein: FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) (Augmenter of liver regeneration) (hERV1) (Hepatopoietin) (P55789)
Organism: Homo sapiens (Human)
Function: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.
Subcellular location: [Isoform 1]: Mitochondrion intermembrane space. Mitochondrion {ECO:0000269|PubMed:23676665}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Secreted.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Protein salvador homolog 1
- Sulfhydryl oxidase 2
- Sulfhydryl oxidase 1
- Mitochondrial import inner membrane translocase subunit Tim13
- Cytochrome c oxidase copper chaperone
- Mitochondrial import inner membrane translocase subunit Tim10
- Bcl-2/adenovirus E1B 19 kDa-interacting protein 2-like protein
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Cytochrome c
Sequence:
MAAPGERGRFHGGNLFFLPGGARSEMMDDLATDARGRGAGRRDAAASASTPAQAPTSDSPVAEDASRRRPCRACVDFKTWMRTQQKRDTKFREDCPPDREELGRHSWAVLHTLAAYYPDLPTPEQQQDMAQFIHLFSKFYPCEECAEDLRKRLCRNHPDTRTRACFTQWLCHLHNEVNRKLGKPDFDCSKVDERWRDGWKDGSCD
Protein: Paralemmin A kinase anchor protein (A2APJ1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDRMAEGERANGHSTDQPQDLLGNSLQAPASPSSSTSSHCSSRDGEFTLTTLKKE
Protein: Serine protease Hayan (EC 3.4.21.-) (A8JUP7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine protease which, by converting prophenoloxidase 1 (PPO1) into its active form, plays an essential role in the melanization immune response to physical or septic wounding. May function in diverse PPO1-activating cascades that are negatively controlled by different serpin proteins; Spn27A and Spn28D in the hemolymph, and Spn28D and Spn77BA in the trachea. Also required in the systematic wound response by mediating the redox-dependent activation of the JNK cytoprotective cascade in neuronal tissues after integument wounding.
Subcellular location: Secreted {ECO:0000305|PubMed:22227521}.
Interaction partners:
- tyrosinase
- Serine protease inhibitor 27A
Sequence:
MAMISARRYFLLGLLVLTTSAYVTVGDEGDPCQVRSDIPGICLSSSACENIRGYLKSGTLSTSQVPSCGFGAREEIICCPTVACCATDRGREVQFHATSSERSSLPEPKREPTPEPEPLPPTTTEGKRERESRLDENQNFFDFNKLLSTTVKPQKTHESLKLPTQESMKTPTHESMKMPTHESMKLPTHEPMKLPIQSVGAWGIAPSKTQPIASTQRSFMEPEWGREPRIVNRPLTTPRSRPQRPNNSNFNTNPSPNNNNLIHLVNDRLREQGMQIEPAREVPMVLQTTPTPTPAPTPTQLIDPFEPYRFRGQDRDKDTQPQEPWNDVSNNLDADPAPSIFNPAETRPTTPNPNPSRVNLPEKERPSVAACEKIRSGGKPLTVHILDGERVDRGVYPHMAAIAYNSFGSAAFRCGGSLIASRFVLTAAHCVNSDDSTPSFVRLGALNIENPEPGYQDINVIDVQIHPDYSGSSKYYDIAILQLAEDAKESDVIRPACLYTDRSDPPANYKYFVAGWGVMNVTNRAVSKILLRAALDLVPADECNASFAEQPSANRTLRRGVIASQLCAADKNQRKDACQGDSGGPLILEIDDVDGTYSIVGVISSGFGCATKTPGLYTRVSSFLDYIEGIVWPSNRF
Protein: Ice-structuring protein B (ISP B) (Antifreeze protein B) (HPLC8) (Q99013)
Organism: Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus)
Function: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
MALSLFTVGQLIFLFWTMRITEARPDPAAKAAPAAAAVPAAAAPDTASDAAAAAALTAANAAAAAKLTADNAAAAAAATARG
Protein: C3G protein (Q9QYV3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
FKTIVDKMAIDKKVLEMLPGSASKVLEAILPLVQTDPRIQHSSALSSCYSRVYQSLANLIRWSDQVMLEGVNSEDKEMVTTVKGVIKAVLDGVKELVRITIEKQGRPSPTSPVKPSSPASKPDGQPELPLTEREMEILNKTSVSPSTELLPDSTSEEVAPPKPPLPGIRVVDNSPPALPPKKRQSAPSPTRVAVVAPMSRAVSGSSLPVGINRQDFDVECYTQRRLSGGSRSCGGESPRLSPCSSTGKLSRSDEQLSSLDRDSGQCSRNTSCETLDHYDPDYEFLQQDLSNADQTPPQAACNLSPLPESMGESGPPFVGYSFQLPLGSCLQQDGQQTDTPPALPEKKRRSAVSQTTDSSGCRVSYERHPSQYDNISEDDLQNPAQPVSYPPFAAILPFQQGASSTPVEFVGDFSVPESAGDPEKPPPLPEKKNKHMLAYMQLLEDYSEPQPSMFYQTPQSEHIYQQKNKMLMEVYGFSDSFCGSDSTQELAPPPALPPKQRQLASYAASSFSVSHCVQQTKVAFTPEDGSAAQGLSVSVSNSFLNRHGSLPVPSEPPSGKDGHPRDLSVSSASGKDSRENGERSPKSLDALESAQSEEEVDELSLIDHNEIMARLTLKQEGDDGPDVRGGSGDILLVHATETDRKDLVLYCEAFLTTYRTFISPEELIKKLQCRYEKFSPFADTFKKRVSKNTFFVLVRVVDELCLVELTEEILKLLMELVFRLVCSGELSLARVLRKNILDKVDQKKLLRCAHSDQPLAARGVAARPGTLHDFHSHEIAEQLTLLDAELFYKIEIPEVLLWAKEQNEELKSPNLTQFTEHFNNMSYWVRSIIMLQEKAQDRERLLLKFIKIMKHLRKLNNFNSYLAILSALDSAPIRRLEWQRQTSEGLAEYCTLIDSSSSFRAYRAALSEVEPPCIPYLGLILQDLTFVHLGNPDYIDGKVNFSKRWQQFNILDSMRCFQQVHYEIRRNDDIINFFNDFSDHLAEEALWELSLKIKPRNITRRKTDREEKT
Protein: Prostate-specific antigen (PSA) (EC 3.4.21.77) (Gamma-seminoprotein) (Seminin) (Kallikrein-3) (P-30 antigen) (Semenogelase) (P07288)
Organism: Homo sapiens (Human)
Function: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum.
Subcellular location: Secreted.
Interaction partners:
- Alpha-1-antichymotrypsin
- Androgen receptor
- Alpha-2-macroglobulin
- Kallikrein-2
- Prostatic acid phosphatase
- Glutamate carboxypeptidase 2
- Plasma serine protease inhibitor
- Beta-microseminoprotein
- Alpha-1-antitrypsin
- Solute carrier family 45 member 3
Sequence:
MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP
Protein: COBRA-like protein 10 (Q9LJU0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the deposition of apical pectin cap and cellulose microfibrils in pollen tubes. Not essential for pollen development, hydration or germination, but required for pollen tubes growth in the female transmitting tract of pistil and toward micropyles, via the perception of ovule guidance cues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23384085, ECO:0000269|PubMed:24963069, ECO:0000269|PubMed:27872247}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:23384085, ECO:0000269|PubMed:24963069}. Cytoplasm {ECO:0000269|PubMed:24963069, ECO:0000269|PubMed:27872247}. Vesicle {ECO:0000269|PubMed:23384085}. Note=Localization to the plasma membrane is dependent of the GPI-anchor at Ser-646 (PubMed:23384085, PubMed:24963069). Localized at the apical plasma membrane of pollen tubes (PubMed:23384085, PubMed:24963069). Colocalizes with A36 and A39 at the plasma membrane and in the cytoplasm in the growing pollen tubes (PubMed:27872247). In the cytoplasm, observed in motile punctate vesicles (PubMed:23384085). {ECO:0000269|PubMed:23384085, ECO:0000269|PubMed:24963069, ECO:0000269|PubMed:27872247}.
Interaction partners:
- Pectin lyase-like superfamily protein
- At5g42680
- Protein trichome birefringence-like 15
- Cation/H
- Transcription factor MYB97
- Mannosyltransferase APTG1
- TATA box-binding protein-associated factor RNA polymerase I subunit B
- AT5G65740 protein
- Casparian strip membrane protein 2
- GPI-anchored protein LORELEI
Sequence:
MRAIDVKTGMKIPWDVRYSLSLFIFLSSILFLSNGQDYGMPGEDGGGGAEPPPEMAHCNGIFMSYNFGSREREYPHVKNVTAQSWAFKSTAMIVNAGREELKGWQMFIGFRHKELIVSATGATPMDGDYPLDASNGTTFVGSPNMDLKTSIETAGDFTQISANIEITGTLFGVSKAVTPMPRTIKLTNDGWECPAAKRKGGSMHVCCKRNPKIKNKIGLKTKFAPRRYGDLNIVYDVLQSFDSNYLAQVTIDNDNPLGRLDRWNLTFEWMRGEFINTMRGAYTHKKDPSECLYSKAGQYYKDLDFSQVMNCQRKPAISDLPPEKKEDNMTGKLPFCCKNGTLLPPIMDPSKSRSMFQLQVFKLPPDLNRTALYPPQHWKIDGVLNPQYKCGPPVRVDPSQFPDPSGLLAVTYAISSWQVVCNITKPKAQASRCCVSFSAFYNNSAVPCNTCACGCNDIDTDTCNANSNPLLLPPDALLVPFDNRTLKAKAWAKQNHMPVPKKLPCPDNCGVSINWHVSTDYKNGWTARLTVFNWRDFAFEDWFVAIDMGKAGPGYENVYSFNGTRVPPSNRTVIFQGLPGMNYLVGQVNGTNPLRDPPVPGKQQSVISFTKKNIKGLNIPEGDGFPTKLFFNGEECALPKHFPKKSSGHRRGISVSMSFVFATIAAFALMMD
Protein: BTB/POZ domain-containing protein At3g26490 (Q9LIM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Interaction partners:
Sequence:
MKFMELGFRPDTFYTVESVRSVSSDLLNDLVIQVKSTKYLLHKFPMLSKCLRLKNLVSSQETETSQEQQVIQLVDFPGETEAFELCAKFCYGITITLCAHNVVAVRCAAEYLGMTEEVELGETENLVQRLELFLTTCVFKSWRDSYVTLQTTKVLPLWSEDLGITNRCIEAIANGVTVSPGEDFSTQLETGLLRNRSRIRRDEILCNGGGGSKAESLRWWGEDLAELGLDLYRRTMVAIKSSHRKISPRLIGNALRIYASKWLPSIQESSADSNLVLESVISLLPEEKSSVPCSFLLQLLKMANVMNVSHSSKMELAIKAGNQLDKATVSELLIPLSDKSGMLYDVDVVKMMVKQFLSHISPEIRPTRTRTEHRRSRSEENINLEEIQEVRGSLSTSSSPPPLLSKVAKLVDSYLQEIARDVNLTVSKFVELAETIPDTSRICHDDLYNAIDVYLQVHKKIEKCERKRLCRILDCKKLSVEASKKAAQNELLPLRVIVQILFVEQARATLATTRNNITTNETAVLKRSFTTRREEGGQEEEERDETKPSGGFLQSTPSRFMALCAIPRQPKKLLCKLLSISRSLSQRI
Protein: HIG1 domain-containing protein (Q21524)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
- Cytochrome c oxidase subunit 6A, mitochondrial
- Putative pyridoxamine 5'-phosphate oxidase
- COX5B-domain-containing protein
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 2
- Cytochrome oxidase c subunit VIb
- Regulator of hypoxia-inducible factor 1
- Proteasome subunit beta type-1
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase
Sequence:
MGMFRTAFMNVAGVHEEPKKGSYEWKKEHMTPQQLARTMDNAEKYNGIPAIPVDIGYHSGKNTGGAQKTGVVSNAASNPGVILGMGLTTAALLGMFKSSFLGDKVGAQKMMQYRIMAQFFTVTALVAGVTIFGATYEDEEHQK