wanglab/gogpt-training-data huggingface dataset:
Protein: Cadherin-1 (CAM 120/80) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3] (P12830)
Organism: Homo sapiens (Human)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:18343367, ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:27760340, ECO:0000269|PubMed:28169360}. Cell membrane {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:28301459}; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:15689490}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:15689490}. Cytoplasm {ECO:0000269|PubMed:22294297}. Cell junction, desmosome {ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492, ECO:0000269|PubMed:33596089}. Note=Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane. Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (PubMed:25208567, PubMed:29999492). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492}.
Interaction partners:
- Killer cell lectin-like receptor subfamily G member 1
- Catenin beta-1
- Catenin alpha-1
- Junction plakoglobin
- Catenin delta-1
- Epidermal growth factor receptor
- Ras GTPase-activating-like protein IQGAP1
- Integrin alpha-E
- Vinculin
- Cadherin-2
Sequence:
MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD
Protein: Nitrogen regulatory protein P-II 2 (Q9HTR6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Ammonium transporter
- Probable transporter
- Bifunctional uridylyltransferase/uridylyl-removing enzyme
- Sensory histidine kinase/phosphatase NtrB)
- Acetylglutamate kinase
- Glutamine synthetase
- Amino-acid acetyltransferase
- DNA-binding transcriptional regulator NtrC)
- Probable glutamine synthetase
- Probable glutamine synthetase
Sequence:
MKLVTAIIKPFKLDDVRESLSEIGVQGITVTEVKGFGRQKGHTELYRGAEYVVDFLPKVKIDVAIADDQLDRVIEAITKAANTGKIGDGKIFVVNLEQAIRIRTGETDTDAI
Protein: Alpha-amylase (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (Allergen Der p IV) (Mite group 4 allergen Der p 4) (allergen Der p 4.0101) (P49274)
Organism: Dermatophagoides pteronyssinus (European house dust mite)
Function: Aids in the digestion of starch and glycogen derived from food, such as skin scales, fungi and bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:10545763, ECO:0000269|PubMed:1710630, ECO:0000269|PubMed:1718897, ECO:0000269|PubMed:8781672}.
Interaction partners:
Sequence:
KYHNPHFIGNRSVITHLMEWKYDDIGDECERFLGPYGYGGVQVSPVNEHAILDRRPWYERYQPVSYDIRTRSGDEQQFRRMVKRCNKAGVRIYVDIVLNHMTGAQSGKGTNGHHYDGNTLQYPGVPFGPNDFHGHESCPTQDLEIHDYTNPKEARNCRLSGLRDLKQQSEYVRQKQVDFLNHLIDIGVAGFRSDASTHQWPDDLRSIYSRLHNLNKEFFPENSQPFIYHETIYYGGNGINSNEYTSLGRIIEFRFYKEITNVFRGNNPLHWLKNFGTEWGLVPSGDALVMIDSHDLRVGHTGKLGFNINCFEGRLLKAATAFMLAWNYGVPRVMSSYFWNQIIKDGKDVNDWVGPPSDKNGNILSVHPNPDMTCNHEWICEHRWREIYNMVKFRMIAGQEPVHNWWDNGDYQIAFSRGNRAFIAINLQKNQQNLQQKLHTGLPAGTYCDIISGNLIDNKCTGKSIHVDKNGQADVYVGHDEFDAFVAYHIGARIVS
Protein: Pectate lyase L (EC 4.2.2.2) (Pectate transeliminase) (Pel9A) (P0C1A7)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Presents an endo-cleaving activity on polygalacturonate or partially methylated pectin. Is effective in the maceration of plant tissue, and has an important role in soft-rot disease. Is 280-fold less active against polygalacturonate than the major pectate lyase PelB. When assayed on polygalacturonate, PelL releases oligogalacturonates of different sizes; upon prolonged incubation, PelL degrades the primary products to unsaturated tetramer and pentamer in addition to unsaturated dimer and trimer. When assayed on oligogalacturonates (degrees of polymerization of 2 to 8), it preferentially forms unsaturated tetramer, and displays the highest activity on the octamer.
Subcellular location: Secreted.
Interaction partners:
- Pectate lyase C
- Pectate lyase B
- Pectate lyase D
- Pectate lyase E
- Pectate lyase A
- Pectate lyase
- Pectinesterase A
- pectate lyase
- Pectin acetylesterase
- Pectate lyase
Sequence:
MKYLNCFISTGLAAFFLVNSTSVLAADCSSDLTSGISTKRIYYVAPNGNSSNNGSSFNAPMSFSAAMAAVNPGELILLKPGTYTIPYTQGKGNTITFNKSGKDGAPIYVAAANCGRAVFDFSFPDSQWVQASYGFYVTGDYWYFKGVEVTRAGYQGAYVIGSHNTFENTAFHHNRNTGLEINNGGSYNTVINSDAYRNYDPKKNGSMADGFGPKQKQGPGNRFVGCRAWENSDDGFDLFDSPQKVVIENSWAFRNGINYWNDSAFAGNGNGFKLGGNQAVGNHRITRSVAFGNVSKGFDQNNNAGGVTVINNTSYKNGINYGFGSNVQSGQKHYFRNNVSLSASVTVSNADAKSNSWDTGPAASASDFVSLDTSLATVSRDNDGTLPETSLFRLSANSKLINAGTKESNISYSGSAPDLGAFERN
Protein: Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (Leukocyte receptor cluster member 7) (P68104)
Organism: Homo sapiens (Human)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:8650580}. Nucleus {ECO:0000269|PubMed:17177976, ECO:0000269|PubMed:8650580}. Nucleus, nucleolus {ECO:0000269|PubMed:8650580}. Cell membrane {ECO:0000269|PubMed:26497934}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery (PubMed:19158340). Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens (PubMed:8650580). Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B (PubMed:26497934). {ECO:0000269|PubMed:19158340, ECO:0000269|PubMed:26497934, ECO:0000269|PubMed:8650580}.
Interaction partners:
- Elongation factor 1-gamma
- Elongation factor 1-beta
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Elongation factor 1-delta
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL3
Sequence:
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Protein: Transcription initiation factor IIF subunit alpha (Q5AMR1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU366044}.
Interaction partners:
- Transcription initiation factor IIF subunit beta
- DNA-directed RNA polymerase subunit
- RNA polymerase II subunit A C-terminal domain phosphatase
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase subunit
- Transcription factor TFIIE subunit
- Transcription initiation factor IIE subunit beta
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerase II subunit
Sequence:
MSQSDVPIKKEVTVKKEDGSTPTSPSKQQEWQTIPLKSCTEEDVKDIRFHIMKFATKQDVNITKDFTRPVRLHRKDPRNMQFHLTREELDQRKREKQQMEKLKQEEKEATAKPTEESEEKEEKDKPTADAAKVAPEKPTLNKNQADMSQVAPDGGARKNRKNLFKRKTRQINLMNEEKRKLRYEEHYPWVIEDYDGKNVFVGNYEAGSTEQQHVLFVFDKDGFKMIPAEKVYRFTPRNRYATLTLEEAEAKMERNSSVPRWLMKHMEDRSISEGTPDQRFRYNSPAANGSVIANVGNGSAGRRMRTVLGGSGSGNDRDSDHDDLDYDEEFADDEEAPIMDGDEEENKLSEKKIKKEMLKAAHFDGQSEAEAEDDLDDLFETEKTRKVDKEGKKLRKVLNKREGGVYDSDEEDGLMPYISKSDLESDEESDDEVQVKKEPSSDSQTDNNTNKTSRAREVGVKSIGDGFVVIKAPPSFLGTMPPGDWNPQARKRPTPEIASPRKKIKLDETIKVKKERTLSPPPVSPTTNAATNTSSPGNGMDLNDAGPDNLLVTVKDVLDIVKDQPLTTKELLMGLKSRVSAHKDNKLRIISIVKQNLRLVDGKLVLKD
Protein: RE54525p (Reduction in Cnn dots 2) (Q8SXY5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEKLITICLLLRILQSCAMPIIDPDSIDESLACPPCENDFPICYKVIVEVERGNGLPGSCCPRYECLDEEPVCDGSKRRFYKNKCTVCDPCEPLAIQCKEICPMEEPEPICLSDNNEYHRNGDIWMENNGCTTCMCEGGYVTRNAVQCNHYYRCNNPVEVKGQCCPVCPDELGVSNSIYDDGNHKYRNTTSAPILGESESSSSGWSSTVPTDTSDSVPDTSGSPNSSSTSSELATPTPNTSELSSSTERTSTDSSYEQLGEFATSESPDLRTDSEEQETSSSDSAMETTTNPTTFEATATSTVSSTSMELPTATDDGITKMDFNPDGRTPKATDEPTVILVNATNFLSVVTDNPITNQPAVVAPESTSQIKDLNSMEIQQIRYPYAEVPQERIQTDWPLECVVIMGFVILIVFISLYAIVKRYSKNKKYHAIPLNPVRKLNETEKAKTEQKL
Protein: Queuosine precursor transporter QueT (Queuosine precursor ECF transporter S component QueT) (A2RM05)
Organism: Lactococcus lactis subsp. cremoris (strain MG1363)
Function: Probably a queuosine precursor-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21135102}; Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
Interaction partners:
- Niacin transporter NiaX
- Manganese ABC transporter ATP binding protein
- Thoeris anti-defense 2-like domain-containing protein
Sequence:
MKKSKTYDIVTIAIVAALYVILTMTPGLSAISYGPIQFRVSEMLNFTAFFNKKYIIAVTIGCMISNFLSFTWVDVIVGGLSTLVFLSLGVLLFDRFKEDYFWNGQLNKAFFFFAIFFSISMFTIALELKFVAETPFLLTWGTLALGEFASLFIGAFIMDKLGKRVDLSR
Protein: SLAM family member 8 (B-lymphocyte activator macrophage expressed) (BCM-like membrane protein) (CD antigen CD353) (Q9P0V8)
Organism: Homo sapiens (Human)
Function: May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- SLAM family member 9
Sequence:
MVMRPLWSLLLWEALLPITVTGAQVLSKVGGSVLLVAARPPGFQVREAIWRSLWPSEELLATFFRGSLETLYHSRFLGRAQLHSNLSLELGPLESGDSGNFSVLMVDTRGQPWTQTLQLKVYDAVPRPVVQVFIAVERDAQPSKTCQVFLSCWAPNISEITYSWRRETTMDFGMEPHSLFTDGQVLSISLGPGDRDVAYSCIVSNPVSWDLATVTPWDSCHHEAAPGKASYKDVLLVVVPVSLLLMLVTLFSAWHWCPCSGKKKKDVHADRVGPETENPLVQDLP
Protein: mRNA export factor MEX67 (Q99257)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the export of mRNA from the nucleus to the cytoplasm.
Subcellular location: Nucleus. Cytoplasm. Note=Localizes at both the nuclear and cytoplasmic site of the pores. Shuttles between the nucleus and the cytoplasm.
Interaction partners:
- RNA annealing protein YRA1
- mRNA transport regulator MTR2
- mRNA export factor GLE2
- Nuclear cap-binding protein subunit 2
- Nuclear mRNA export protein SAC3
- Nucleoporin NSP1
- Nucleoporin NUP2
- Probable metalloprotease ARX1
- Nuclear polyadenylated RNA-binding protein NAB2
- Nucleoporin NUP159
Sequence:
MSGFHNVGNINMMAQQQMQQNRIKISVRNWQNATMNDLINFISRNARVAVYDAHVEGPLVIGYVNSKAEAESLMKWNGVRFAGSNLKFELLDNNGASAGTSDTISFLRGVLLKRYDPQTKLLNLGALHSDPELIQKGVFSSISTQSKMFPAMMKLASTEKSLIVESVNLADNQLKDISAISTLAQTFPNLKNLCLANNQIFRFRSLEVWKNKFKDLRELLMTNNPITTDKLYRTEMLRLFPKLVVLDNVIVRDEQKLQTVYSLPMKIQQFFFENDALGQSSTDFATNFLNLWDNNREQLLNLYSPQSQFSVSVDSTIPPSTVTDSDQTPAFGYYMSSSRNISKVSSEKSIQQRLSIGQESINSIFKTLPKTKHHLQEQPNEYSMETISYPQINGFVITLHGFFEETGKPELESNKKTGKNNYQKNRRYNHGYNSTSNNKLSKKSFDRTWVIVPMNNSVIIASDLLTVRAYSTGAWKTASIAIAQPPQQQASVLPQVASMNPNITTPPQPQPSVVPGGMSIPGAPQGAMVMAPTLQLPPDVQSRLNPVQLELLNKLHLETKLNAEYTFMLAEQSNWNYEVAIKGFQSSMNGIPREAFVQF
Protein: Uncharacterized protein YLR257W (Q06146)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized protein YGR017W
Sequence:
MVDARGSTPCLIGDSIRNVNDGNSLDFQYTNQFNEESEASRLLTPQTSSNHALSKMQKDDDIRDRSYTSVAELNREGALLTDEVDLENVDASKVRSNRDDLEAEEKRKKLLLLKKKQRNKSINSESFSSPSLRASKSNSLITSTDPVEDHISKYSSSGTPENITGEADDEDEDIIRNSYGQMIKNNSNRPHLAKGESYQSAEQEIDHTAPEKSEKRQERSGRSFDRQKSSAEFLRSLSRSISRGPTKNKTVSPSKGEDSRMYSTSNYSISLVDLENGPKIIPETLEEEQEDAEKEGVLMEDEGNEEYTKDLEEAANKAQPQ
Protein: Vesicle-associated membrane protein 7A (Q54NW7)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the targeting and/or fusion of transport vesicles to their target membrane during transport of proteins from the early endosome to the lysosome. Required for heterotypic fusion of late endosomes with lysosomes and homotypic lysosomal fusion. Required for calcium regulated lysosomal exocytosis.
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Lysosome membrane {ECO:0000269|PubMed:12175335}; Single-pass type IV membrane protein {ECO:0000269|PubMed:12175335}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255}. Note=During macropinocytosis highest levels are found in endosomes with lower levels observed in the lysosomes. {ECO:0000250|UniProtKB:P70280, ECO:0000250|UniProtKB:Q9JHW5, ECO:0000255, ECO:0000269|PubMed:12175335}.
Interaction partners:
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Syntaxin-7A
- Syntaxin-8A
- Probable syntaxin-8B
- Vesicle-associated membrane protein 7B
- Vacuolar protein sorting-associated protein 16 homolog
- t-SNARE family protein
- t-SNARE coiled-coil homology domain-containing protein
- t-SNARE family protein
- t-SNARE family protein
Sequence:
MSQTDILYACVSYKGVCLVEHKIANGNFIDLARRLITKIPPTSKKIYTSENHNFHYISENDLAFLCLCHEKLGVQIPSEFLSDIRQQFIRSYGQSFSQNSPTATYDPFIRVLEERMKYYSNPKSNKMNLVMDQVSEAKGALTDAIEKTIHRGEKIEIIVDKTERLQSESFVFKSNSVALKRKLWWQNKKLAIAIGLVVCILIAVITLALLKYFKVI
Protein: Negative elongation factor E (Q6MG75)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Negative elongation factor complex member B
- Negative elongation factor complex member C/D
- Wolf-Hirschhorn syndrome candidate 2
- DNA-directed RNA polymerase subunit
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- Nuclear cap-binding protein subunit 1
- DNA-directed RNA polymerase II subunit RPB3
- Cyclin-dependent kinase 9
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSGTASQGGVKRSLSEQPVVDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSMSADEDLQEPSRRPQRKSLYESFVSSSDRLRELGQDGEEAEAPGAGEGPPRGFDWSYEEHSGARSSASPPRSRSRDRSHDRSRDRDRDKERDRDRDRDRERDKDKDRDRDRDRDKERDRDRDRERDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGKSVWGSLAVQNSPKGCHRDKRTQIVYSDDL
Protein: Monoacylglycerol lipase (MGL) (EC 3.1.1.23) (A0QNZ7)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Contributes to cell growth, probably by hydrolyzing exogenous lipids. Catalyzes the hydrolysis of monoacylglycerols (MAG) with fatty acid chains ranging from C14 to C18, with a maximum activity on monoolein. Is unable to hydrolyze long-chain diacylglycerol (DAG).
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:20601476}.
Interaction partners:
- Hydrolase, alpha/beta fold family protein
- Secreted protein
- Cutinase superfamily protein
- Secreted protein
- Carboxylesterase Culp6 homolog
- TIGR04338 family metallohydrolase
Sequence:
MVSSTRSEHSFAGVGGVRIVYDVWTPDTDPRGVVVLAHGYAEHAGRYHHVAQRFGAAGLLVYALDHRGHGRSGGKRVHLRDLSEFVEDFRTLVGIAANDHPTLPRIVLGHSMGGGIVFAYGARYPGEYSAMVLSGPAVNAHDGVSPVLVAVAKVLGKLAPGIPVENLDADAVSRDPEVVAAYKADPMVHHGKLPAGIARALIGLGQSMPQRAAALTAPLLVVHGDKDRLIPVAGSRLLVDRVASEDVHLKVYPGLYHEVFNEPEQKLVLDDVTSWIVSHL
Protein: Methyltransferase, putative (Q38CH6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Telomerase-associated protein, putative
- Serine/threonine-protein kinase RIO1
- Histone H4
- Histone H4
- Serine/threonine-protein kinase, putative
- Uncharacterized protein
- Protein arginine N-methyltransferase 7
Sequence:
MKPCVSAAAPADWPVASDEQKPSRPETAMEHDEETRGCSSSSVRLQGYGVSGAGSLMDSMRQREMSGSAFFMFSLDGVNTDDPLAGNVSPLAALCPAGQYSKESQHWFWKVLSNTSSWGMTACGSVSYSSWADPKSVRCIEGQLRLGAFLGIHAVVVPLPDFDEEDPQCSEKLKAAALVISKHLQHSQTTNVWVRCDASRQADRVAFSRLRTFVLWGGENPPTAEEAPHRVVRPAPYRIVAFLNFSETFGAIPSEWLGESVAAFELPNAEKLRRALSASDCGRHMKLPSDLMPLKDSYWGTAQPMFVSLATFVVELLRRRAAPVFAMEEFVDSYQLLNTLYEMHVADGGRDKFFDYEDVLQLPLQPLGHMLASGVYEVFEQDRTKYQQYHTAMSKYFNEWLNHSESRSHEKMWLQGPNPRDGCGCSAMGSVYVVLLGAGRGPLISECLCAATGVGVRVHLFVVEKNPEALELVRLRVRADPQWHDWMNYSGHVVETIYADGRSVWSGEAPGSDDRLPPYWGLCDLVVSELLGSFGDNELSPECLDDFYCNLLSYQESSGIPCNPYLTSIPQQYTAWIAPLHSARMEESVATAAFGGLTTPPADCHDRHAALYHSMFVSNVCRAVGLCLPQPCWTFHHFATKVQSKEREATLNFTLSGDGRFSGFICYFSAVLFTPGDTGNVEDSIALLCASAGSLSTVQYGRTTGLFSWFPAFLPVEPRDVVEVKCGDELSIHLKRCVDVKKGRVWYEYEASILVKGHPDGKFMKRLTKTMNAGGWAGHISLLT
Protein: Hyaluronidase Tab y 2.0101 (EC 3.2.1.35) (Allergen Tab a 2) (allergen Tab y 2.0101) (E0XKJ9)
Organism: Tabanus yao (Horsefly)
Function: Hydrolyzes high molecular weight hyaluronic acid to produce small oligosaccharides.
Subcellular location: Secreted {ECO:0000305|PubMed:20608917}.
Interaction partners:
Sequence:
MKLHQGLVCLSVLILLPTCILGDRKFEVYWNIPTFMCPDQNKTIMDLNKKHGVIQNTEDLFRGDKISLLYHPGAFPAITRNKTTNTLIYENGGVPQAGNLSLHLKLLEKDINEQITDKNFSGLAVIDFELWRPIFRQNGGSLSDYQNLSLKLEKDLHPEFNEDQLRKEAERRIEKFGRSFIKQTLIKAKKLRPKAQWGYYAFPYCFNGRRRYVDTCIPSAKIDNDRILYMFENSDVIYPAVYLQTDLAQKNQTGLVKGRVDEAVRMAKMVKKPAKPPVLVYHRYVFTDTLEYISKENTTAVFKAMKDNGADGVIIWGSSFDLNSKEKCAKFLDYLREVLWPVIDEVKRS
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B (EC 3.4.21.-)) (Q9W5U8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- trypsin
- Zinc carboxypeptidase A 1
- RE65433p
- Venom allergen-1
- Trypsin theta
- Peptidase S1 domain-containing protein
- Lipase
- GH20109p
- Jonah 44E, isoform A
- Jonah 25Biii
Sequence:
MNRLLLSVVALVALAASCHGNPGLDFPFGRIVNGEDVDIENYPYQVSVQTTKGSHFCGGSLIDSETVLTAAHCMQSYAASELQVRVGSTSRSSGGEVVTVRAFKYHEGYNSKLMINDVAIIKLSSPVRQTSKIRAIELADSEAVSGTNAVVSGWGTTCFLFCSSPDTLQKVEVDLLHYKDCAADTYNYGSDSILETMVCATGEKKDACQGDSGGPLVADNKLVGVVSWGSGCAWTGYPGVYADVASLRSWIVDTTDSL
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q8VZ73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT5G12460.1
- At5g01015
- Small ribosomal subunit protein mL103
- Pentatricopeptide repeat-containing protein At2g18520
- Fanconi anemia group F protein
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- ATP-dependent protease La
- ARM repeat superfamily protein
- Phosphorylase superfamily protein
- At4g24340
Sequence:
MPPLPSSTAPSSSRHLRSPESIAKFAGRAIFPALQGKSCPICLENLTERRSAAVITVCKHGYCLACIRKWSSFKRNCPLCNTRFDSWFIVSDFASRKYHKEQLPILRDRETLTYHRNNPSDRRRIIQRSRDVLENSSSRSRPLPWRRSFGRPGSVPDSVIFQRKLQWRASIYTKQLRAVRLHSRRLELSLAVNDYTKAKITERIEPWIRRELQAVLGDPDPSVIVHFASALFIKRLERENNRQTGQTGMLVEDEVSSLRKFLSDKVDIFWHELRCFAESILTMETYDAVVEYNEVE
Protein: Mitochondrial thiamine pyrophosphate carrier (Mitochondrial thiamine pyrophosphate transporter) (MTPPT) (Mitochondrial uncoupling protein 1) (Solute carrier family 25 member 19) (Q9HC21)
Organism: Homo sapiens (Human)
Function: Mitochondrial transporter mediating uptake of thiamine diphosphate into mitochondria. It is not clear if the antiporter activity is affected by the membrane potential or by the proton electrochemical gradient.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:15539640, ECO:0000269|PubMed:27188525, ECO:0000269|PubMed:31506564}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- Ubiquitin-like protein FUBI
- Alpha-aminoadipic semialdehyde dehydrogenase
- Lipid transferase CIDEA
- 3',5'-cyclic-AMP phosphodiesterase 4D
- Thiamine transporter 2
- 3',5'-cyclic-AMP phosphodiesterase 4A
- 3',5'-cyclic-AMP phosphodiesterase 4B
- Thiamine pyrophosphokinase 1
Sequence:
MVGYDPKPDGRNNTKFQVAVAGSVSGLVTRALISPFDVIKIRFQLQHERLSRSDPSAKYHGILQASRQILQEEGPTAFWKGHVPAQILSIGYGAVQFLSFEMLTELVHRGSVYDAREFSVHFVCGGLAACMATLTVHPVDVLRTRFAAQGEPKVYNTLRHAVGTMYRSEGPQVFYKGLAPTLIAIFPYAGLQFSCYSSLKHLYKWAIPAEGKKNENLQNLLCGSGAGVISKTLTYPLDLFKKRLQVGGFEHARAAFGQVRRYKGLMDCAKQVLQKEGALGFFKGLSPSLLKAALSTGFMFFSYEFFCNVFHCMNRTASQR
Protein: Bifunctional purple acid phosphatase 26 [Includes: Acid phosphatase (EC 3.1.3.2); Peroxidase (EC 1.11.1.7)] (Q949Y3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Metallo-phosphoesterase involved in phosphate metabolism. Acid phosphatase activity with phosphoenolpyruvate, inorganic pyrophosphate, phenyl-phosphate and p-nitrophenyl-phosphate as the most effective substrates. No activity with phytic acid, phosphocholine or bis-p-nitrophenyl-phosphate. Has a peroxidase activity at alkaline pH.
Subcellular location: Vacuole {ECO:0000269|PubMed:16963519}.
Interaction partners:
- Inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Purple acid phosphatase 17
- Probable transcription factor At4g00610
- ENHANCED DISEASE RESISTANCE protein
- CHP-rich zinc finger protein-like
- Retrotransposon ORF-1 protein
- Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic
- SPX domain-containing membrane protein At1g63010
- Putative methyl-CpG-binding domain protein 12
- Expressed protein
Sequence:
MNHLVIISVFLSSVLLLYRGESGITSSFIRSEWPAVDIPLDHHVFKVPKGYNAPQQVHITQGDYDGKAVIISWVTPDEPGSSQVHYGAVQGKYEFVAQGTYHNYTFYKYKSGFIHHCLVSDLEHDTKYYYKIESGESSREFWFVTPPHVHPDASYKFGIIGDMGQTFNSLSTLEHYMESGAQAVLFLGDLSYADRYQYNDVGVRWDSWGRFVERSTAYQPWLWSAGNHEVDYMPYMGEVTPFRNYLQRYTTPYLASKSSSPLWYAVRRASAHIIVLSSYSPFVKYTPQWHWLSEELTRVDREKTPWLIVLMHVPIYNSNEAHFMEGESMRAAFEEWFVQHKVDVIFAGHVHAYERSYRISNVRYNVSSGDRYPVPDKSAPVYITVGDGGNQEGLAGRFTEPQPDYSAFREASYGHSTLDIKNRTHAIYHWNRNDDGKKVATDEFVLHNQYWGKNIRRRKLKKHYIRSVVGGWIAT