wanglab/gogpt-training-data huggingface dataset:
Protein: t-SNARE coiled-coil homology domain-containing protein (Q9TY08)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004409}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004409}.
Interaction partners:
- Putative syntaxin 6
- Vacuolar protein sorting-associated protein 45
- t-SNARE coiled-coil homology domain-containing protein
- YKT6
- Alpha-soluble NSF attachment protein
- Putative syntaxin-5
- V-SNARE coiled-coil homology domain-containing protein
- Golgi SNAP receptor complex member 1
- Vacuolar protein sorting-associated protein 53 homolog
- Soluble NSF attachment protein 29
Sequence:
MASSSVTAAANAAKKNEIYGTTRNLTEVFMLLRSNAHQSRLIYKDDTDIIVRSRGDEERMALVELEDGRQESDEEPVWIHTADQVEFEVERVQRRLDELGEAQRKHISRPNFGDEAFEKEEKQMEQTTEQITQMLTHCQRLIRMISGSHNKEKPMQRKLRENAAATLSLTLSQITDEFRGRQLKYLSDIQNRSRNVDNYLITTDPLIDAPNWAELDVSPSTEISMAQLQQFMNNDREVREREKEVMAVNTSIRELNTLFQDLSEMIVDQGSVIDRIDYNVEQTSIRVSKAVEDVFKAERYQKGNKKMHCICMLTVAIIFVLILIIVTKL
Protein: Lysosome-associated membrane glycoprotein 2 (LAMP-2) (Lysosome-associated membrane protein 2) (CD107 antigen-like family member B) (Lysosomal membrane glycoprotein type B) (LGP-B) (CD antigen CD107b) (P17047)
Organism: Mus musculus (Mouse)
Function: Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live. Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy. Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes. Required for normal degradation of the contents of autophagosomes. Plays a role in lysosomal protein degradation in response to starvation. Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity).
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:11082038, ECO:0000269|PubMed:2142158}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Endosome membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:12221139}. Cell membrane {ECO:0000250|UniProtKB:P13473}; Single-pass type I membrane protein {ECO:0000255|PROSITE-ProRule:PRU00740}. Note=This protein shuttles between lysosomes, endosomes, and the plasma membrane. {ECO:0000250|UniProtKB:P13473}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Lysosome-associated membrane glycoprotein 1
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- CD63 antigen
- Ubiquitin carboxyl-terminal hydrolase isozyme L1
- Heat shock 70 kDa protein 1B
- Alpha-synuclein
- Cathepsin D
- Early endosome antigen 1
Sequence:
MCLSPVKGAKLILIFLFLGAVQSNALIVNLTDSKGTCLYAEWEMNFTITYETTNQTNKTITIAVPDKATHDGSSCGDDRNSAKIMIQFGFAVSWAVNFTKEASHYSIHDIVLSYNTSDSTVFPGAVAKGVHTVKNPENFKVPLDVIFKCNSVLTYNLTPVVQKYWGIHLQAFVQNGTVSKNEQVCEEDQTPTTVAPIIHTTAPSTTTTLTPTSTPTPTPTPTPTVGNYSIRNGNTTCLLATMGLQLNITEEKVPFIFNINPATTNFTGSCQPQSAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVYMYLANGSAFNISNKNLSFWDAPLGSSYMCNKEQVLSVSRAFQINTFNLKVQPFNVTKGQYSTAQDCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF
Protein: INO80 complex subunit E (Zgc:77312) (Q6P110)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Nuclear factor-related to kappaB-binding protein.
- Actin-related protein 5
- INO80 complex ATPase subunit.
- TCF3
- INO80 complex subunit C
- INO80 complex subunit Da
- Actin-related protein 8
- INO80 complex subunit B.
- RuvB-like 2
- RuvB-like 1
Sequence:
MNGQAEVEVDYKRKYKNLKRKLKFLVYEQECFQEELRRAQRKLLKVSRDKSFLLDRLLQYERVDEESSDSDATVSSDSDGEGARERDREAGKKRRSPGVPPVPSSSSPHLSLLSRSGALQSSASAQYLNALPFPPEYLAPSAERVKKERKTKLAKHRKDGSGKVVGPLSSSYPAGSGPAGGASGPFSWVPQQMLSEDAGEDEGDSEGESDRGEEERGEGDEAELVIDIPNE
Protein: ATP-dependent Clp protease ATP-binding subunit (At5g62140) (Q9FIS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AIG2-like protein A
- ATP-dependent Clp protease ATP-binding subunit CLPT1, chloroplastic
- AT3g09210/F3L24_8
- ATP-dependent Clp protease ATP-binding subunit CLPT2
Sequence:
MASTKINSLTTTIYNYKSPRRYINHKSQNQIKLISNSLNPKPNTTQLPNTLYSVSFKTIGTGKLGISRYPDFEYSPLGGSGAGTAKKIDDKNRASNSELSVCFNVATLYIPSLTSQTTKFLGFPLPPFLKIDISPEIFQGTINQESGKVELEFMAKFFFTAGGGIYRAPALVVRTVLTTEESIGENKRGKGERLDEEGKCRLVGVAKVETIDDLFMNTFLSLPAECLADLQAIISVSDNQS
Protein: Transcription initiation factor IIE subunit beta (TFIIE-beta) (General transcription factor IIE subunit 2) (P29084)
Organism: Homo sapiens (Human)
Function: Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Subcellular location: Nucleus {ECO:0000269|PubMed:7651391}.
Interaction partners:
- Transcription initiation factor IIB
- General transcription factor IIF subunit 1
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 4
- General transcription factor IIF subunit 2
- General transcription factor IIE subunit 1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription factor IIH subunit 3
- TATA-box-binding protein
- Transcription initiation factor IIA subunit 2
Sequence:
MDPSLLRERELFKKRALSTPVVEKRSASSESSSSSSKKKKTKVEHGGSSGSKQNSDHSNGSFNLKALSGSSGYKFGVLAKIVNYMKTRHQRGDTHPLTLDEILDETQHLDIGLKQKQWLMTEALVNNPKIEVIDGKYAFKPKYNVRDKKALLRLLDQHDQRGLGGILLEDIEEALPNSQKAVKALGDQILFVNRPDKKKILFFNDKSCQFSVDEEFQKLWRSVTVDSMDEEKIEEYLKRQGISSMQESGPKKVAPIQRRKKPASQKKRRFKTHNEHLAGVLKDYSDITSSK
Protein: Serine hydroxymethyltransferase (SHMT) (Serine methylase) (EC 2.1.2.1) (P0A825)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305}.
Interaction partners:
- Aminomethyltransferase
- Bifunctional purine biosynthesis protein PurH
- Glycine dehydrogenase
- Bifunctional protein FolD
- Thymidylate synthase
- 5,10-methylenetetrahydrofolate reductase
- Glycine cleavage system H protein
- Phosphoserine phosphatase
- L-serine dehydratase 1
- Phosphoribosylglycinamide formyltransferase
Sequence:
MLKREMNIADYDAELWQAMEQEKVRQEEHIELIASENYTSPRVMQAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRAKELFGADYANVQPHSGSQANFAVYTALLEPGDTVLGMNLAHGGHLTHGSPVNFSGKLYNIVPYGIDATGHIDYADLEKQAKEHKPKMIIGGFSAYSGVVDWAKMREIADSIGAYLFVDMAHVAGLVAAGVYPNPVPHAHVVTTTTHKTLAGPRGGLILAKGGSEELYKKLNSAVFPGGQGGPLMHVIAGKAVALKEAMEPEFKTYQQQVAKNAKAMVEVFLERGYKVVSGGTDNHLFLVDLVDKNLTGKEADAALGRANITVNKNSVPNDPKSPFVTSGIRVGTPAITRRGFKEAEAKELAGWMCDVLDSINDEAVIERIKGKVLDICARYPVYA
Protein: RuvB-like helicase (EC 3.6.4.12) (Q4QQS4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Dynein axonemal particle {ECO:0000256|ARBA:ARBA00024190}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU363048}.
Interaction partners:
Sequence:
MATVAATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSFGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTSPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS
Protein: WASP homolog-associated protein with actin, membranes and microtubules (WAS protein homology region 2 domain-containing protein 1) (WH2 domain-containing protein 1) (Q571B6)
Organism: Mus musculus (Mouse)
Function: Acts as a nucleation-promoting factor (NPF) that stimulates Arp2/3-mediated actin polymerization both at the Golgi apparatus and along tubular membranes. Involved as a regulator of Golgi positioning and morphology. Its activity in membrane tubulation requires F-actin and interaction with microtubules. Proposed to use coordinated actin-nucleating and microtubule-binding activities of distinct WHAMM molecules to drive membrane tubule elongation; when MT-bound can recruit and remodel membrane vesicles but is prevented to activate the Arp2/3 complex. Required for RhoD-dependent actin reorganization such as in cell adhesion and cell migration (By similarity). Participates in vesicle transport between the reticulum endoplasmic and the Golgi complex.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8TF30}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:Q8TF30}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q8TF30}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:Q8TF30}. Note=Localized to a perinuclear compartment near the microtubule-organizing center (MTOC). Also detected on tubulo-vesicular structures in the cell periphery that frequently localized along microtubules. {ECO:0000250|UniProtKB:Q8TF30}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- Actin-related protein 2
- Cell division control protein 42 homolog
- Actin-related protein 3B
- Actin-related protein 3
- Actin, cytoplasmic 1
- Actin, cytoplasmic 2
- Rho-related GTP-binding protein RhoD
Sequence:
MDSEQPDSLDGWVPLREDLFPEPERHQLRFLVAWNAAKGQFAVTCHDRTAQRRRRERREAGDGGCSWAGVLSPAGFRGAHRQLAALWPALEPCFPPLPPELDAASGAGWGLGRGLWALLWPLLWPAPADPGDSALQELCRQLEHYLGLAAEGCGGATVRDVLFPAPGDSADCEGLSEFRERTLRARLGQTATRLHQVLQDHGKANTMVALMKVYQEEDELYQELVTMATTFFQYLLQPFRDMREVATSCKLGILKSLDEDELGPRRVAALQKEASEWTRQAEEAVGSIQDITVNYFKETVTALTGMQKQMEQDQKRFGQAAWATAMPRLENLKLMLARETLQLMRAKELCLKHRQAEIQRKVEDLPRQGKQLDVVDELEIQCYEIQLELYDVKLEMLRNEETILVTRLDSVKRLITEKQAEVIYYDPCESPEELQSLAPDLELHLGDNRELRALSQQCQRLEAQRGRICSRRALLRNRKDHCRENHQLRLQQAKQSLRHLHQHHSIQMKRDKVKEEEQKKKEWIDHERQKTLERLRAYKEKCPAHRSALKTTCSESMVSNLPGGRSQKRLSTAHHHKTAHPASSKTGSAVPLPEASVRPPEHQDPCGSVPVQAFVPVSDQTLSGSSEDLSLPPQPPAPPLPPPPPPPPPPPLPPALSSFQGTTHQNLGLRTLATEDRPLPLACDPSAGRPCDYQGPGSMDEVLASLRQGKASLRKVETPTLPHPGTSVNEQVLAAIRQGVQLKKVHTGQGVDPGKKSTSDLERSIREALERIKKVSADSEEDNDEPSPTEWDR
Protein: BPI fold-containing family A member 1 (Palate lung and nasal epithelium clone protein) (Q8K4I4)
Organism: Rattus norvegicus (Rat)
Function: Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC). Plays a role in the innate immune responses of the upper airways. Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae. Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus. Plays a role in the airway inflammatory response after exposure to irritants. May attract macrophages and neutrophils.
Subcellular location: Secreted {ECO:0000269|PubMed:11821380}. Note=Apical side of airway epithelial cells. Detected in airway surface liquid, nasal mucus and sputum.
Interaction partners:
- BPI fold-containing family B member 1
- Secretoglobin, family 3A, member 1
- BPI fold-containing family B member 4
- Mucin-2
- BPI fold containing family B, member 2
- Pneumo secretory protein 1
- Bactericidal permeability-increasing protein
- Uteroglobin
Sequence:
MFLVGSLVVLCGLLAQSTAQLAGLPLPLGQGLPLPLGQGLPLPLGQGLPLAVSPALPSNPTDLLAGNFANALSGGLLSGGLLGILENIPLLDVIKSGGGSSNGLVGGLLGKLTSSVPLLNNILDIKITDPRLLELGLVQSPDGHRLYATIPLSLKLQVNMPVVGSFLQLAVKLNITAEIVAMKDNQGRIHLVLGDCTHSPGSLQITLLNGVTPVQSSLDSLTGILTKVLPELIQGKVCPLINGILSGLDVTLVHNIAELLIHGIQFVIKV
Protein: Lipoxygenase 1, chloroplastic (TcLOX1) (EC 1.13.11.-) (13-hydroperoxylinolenic acid synthase) (R9WTS6)
Organism: Tanacetum cinerariifolium (Dalmatian daisy) (Chrysanthemum cinerariifolium)
Function: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide. Plant lipoxygenases may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity). Mediates the peroxidation of linolenic acid leading to the production of 13-hydroperoxylinolenic acid.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MALAKQIMGASLMDQKTSVFGSNLCLNHVLVNKHRLRLRKTRKNGSMVVAAISEDLVKLXRVEKEKPVTFKVRAVLTVRNKNKEDFFKDTIFRKIDAITDQIGWNVVIQLFSNDIDPRTRAAKKSNEAVLKDWSKKSNVKTERVNYTADIMVDSDFGIPGAITISNKHQKEFFLETITIEGFACGPVHFPCNSWVQSTKDLPNPRIFFTNQPYLPDETPVGLKSLRYQELKDLRGDGTGVRKLSDRIYDYDVYNDLGNPDRGNDFVRPTLGGEKIPYPRRCRTGRVPSDTDITAESRVEKPFPLYVPRDEQFEESKANAFSTGRLRAVLHNLLPSMVTSISKKNDFKGFSQIDSLYSEGVFLKLGLQDDLLKKLPLPNLVTRLHESSQGGGLLKYDTPKILSKDKFAWLRDDEFARQTIAGVNPVSIEKLKVFPPVSQLDPEKHGPQESALREEHIVGFLDGRTVKQAIEEDKLFIIDYHDIYLPFLDRINALDGRKAYATRTIFYLNPSGTLKPVAIELSLPQALPGSESKRVLTPPSDATSNWMWQLAKAHXCSNDAGAHQLVHHFLRTHAAIEPFILAAHRQLSAMHPIYKLLDPHMRYTLEINQLARQNLINADGVIEACFTPGRYGMEISASAYKNWRFDLEGLPADLIRRGMAVPDPSKPHGLKLVMEDYPYASDGLMIWEAIQNWVKTYVNHYYPDSAQVCNDRELQAWYAESINVGHADLRHKDWWPTLAGADDLTSVLTTIIWLASAQHAALNFGQYPYGGYIPNRPPLMRRLLPDVNDPEYLSFHDDPQKYFLSALPSLLQSTKYMAVVDTLSTHSPDEEYIGERQQTDTWSGDAEIVEAFYAFSAEIQRIEKEIEKRNSDTSLKNRCGAGVLPYELLAPSSGPGATCRGVPNSISI
Protein: Beta-porphyranase B (EC 3.2.1.178) (D7GXF9)
Organism: Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
Function: Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone. In contrast to PorA, tolerates the presence of 3-6-anhydro-L-galactose in subsite -2.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Beta-agarase D
- Beta-agarase A
- Conserved hypothetical periplasmic protein
- Glycoside hydrolase
- 3,6-anhydro-alpha-L-galactosidase
- Conserved hypothetical lipoprotein
- Sortilin N-terminal domain-containing protein
- Glycoside hydrolase
- SusD/RagB family lipoprotein
- Cytochrome P450
Sequence:
MKLSNQFLITITLLITSITFAQEAPHFKPGEDPRQPHQEWKLIENMSDEFEGKKIDEKKWQISGQGWIGRAPGLFLAENISLNNGSLQITTTMLPEPIVKNNKTYTHGGGYVGSRNGMTYGYYECEMKANKTFMSSTFWLINEGKDRLGCDKRTTELDIQESVGQITNDADWMKYFDQTMNSNTHSRNIPEGCEYEKGSSKGKAELGGKAYEDFHVYGVWWKSKDEIIFFLDGKMQSKVTPPADFDIEMYLRMVVETYDWNPVPKDGGMTGSKEDRTTTYNWVRSWQLVDSKN
Protein: LD30829p (Q95TQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKLNVQLHINRQSVRLGDYEYYEKSIDNPYSSIRSGLQAIEKPGCAEAICQSSKPAFVECLPSSTSEEVPVVAVQEASSTNQLDAISVVNENLSEERDATPQPLAVSKNMEETMPSNPFHEQLEGSLEEIPVGSKIVVETEKANNPVRSEASAPATSDNQSLLAAKQGTQTIGTGICNKISKSTINMPNNWQLENPTEVTAASIEKVNKLPKSPRNRFLLPPKGGTETTRRDIYNQILKDMAAFPENTIVTAVLASVDVTDNCAYVAKWDESSDRIKKVLQRQLPLQELDQLPDYGDIFAVLDSINNIITRITINSSSAGGGYDAYLIDFGEHIHFDGNETIFKLPDDIKRLPAQAIRCDLINCDIANMHCFVNTYIKIRVHENNNSTLVAEPVIDRLSRPTKTNTTKYPAGITEDDMAMLNEIDESTSDPLKAVLGFRPKDEQRICRHYDPKLNGCFKGNNCRFAHEPFAPNGATKDVELARALPETIFDTTVHFEIGSIVGILITFINGPTEVYGQFLDGSPPLVWDKKDVPENKRTFKSKPRLLDIVLALYSDGCFYRAQIIDEFPSEYMIFYVDYGNTEFVPLSCLAPCENVDSFKPHRVFSFHIEGIVRSKNLTHQKTIECIEYLKSKLLNTEMNVHLVQRLPDGFLIRFLDDWKYIPEQLLQRNYAQVSQ
Protein: Uncharacterized protein C227.15 (Q9UTC4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole membrane {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase PP1-2
- Protein phosphatase 1 regulatory subunit SDS22
- SNF1-like protein kinase ssp2
- Protein kinase domain-containing protein ppk9
- Uncharacterized hydrolase C215.10
- LSM complex subunit lsm6
Sequence:
MSNKPDANDQCMVKETISRMSMSKEKPFLRRNYSSPSFNDSVNSVNDEFQTYQLPNGEFSDNMNDLYFPFRKGNESLMTENSNYPISEQDTQHNHISDFPSRRMQLDGMNHSNNDTYSTAIPFSKDSSVFDAVGQQSSVPIHINPAYTNSHQNSYSLNETYLSYDFFDNHRGASSSAVSKDGLASPRPTKDVDADDTTWYFTSSPSFQPLKDSDRSQTKNTHEETSPIVSSPEDDADAAFKPSSLPSTSISASSNAFYKPAAPDNERPLDPHITPYLRLQLLTTGADDNDIRKNALTQVDYLSYDWKETDIWASWREITKTKANYDNGIRLENASWRTWMKHKFKLKTISPETLNWLKECDVTWLYGPLLHTSMPSRHHSHRKKEKEKEKSKAPRVTPLTHKTNDDEANHSETSSGSSLAKKPILKRRTPQELLLSGRDLTPWPQIRRFDSLLARNRGDIFSNRNHATIRSALFSQRYPSHSKRHIHFNDRVQQCIAVDIDSLPSDSESASYNTDDANSVVSPSKDGISTTTVSSDATRSSQSSHFRIIEDLPDSKLKYSLEDQATYDQSSRYPGRHFGKTGRSHFPRAPEYYGENDFEEDEVYRDDRHYENEHDEYDPNLIYYDNEPTEENRLVFEDTNNTFIDTDSDDSNADESQFLEYANDSPNSSESLESLNNQSYSSSPYSVFSHPPPYMGRQSLNDSPQTSDFKASNLNDSSSNVHSIFQTRETTSPSVQNKTPTKYHRELKSSKDGHEQASPLVSSSPSGSFTSQISPAATTTATNLDAVSLSPSTVRTGSQISDIGNDAISTTRKTVRAFLENANPYSTNNDGNPSNNTSDVEVNETSMNDNSEEPISSNWLVDLFQKSLKSFRE
Protein: SUMO-conjugating enzyme ubc9 (EC 2.3.2.-) (Ubiquitin carrier protein 9) (Ubiquitin carrier protein hus5) (Ubiquitin-conjugating enzyme E2-18 kDa) (P40984)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the covalent attachment of ubiquitin-like protein SUMO/Smt3 to other proteins. Required for efficient recovery from DNA damage or S-phase arrest and normal mitosis. This may be as part of a checkpoint independent recovery process.
Subcellular location: Nucleus {ECO:0000269|PubMed:7768995}.
Interaction partners:
- Ubiquitin-like protein pmt3/smt3
- Ubiquitin-activating enzyme E1-like
- E3 SUMO-protein ligase pli1
- DNA damage tolerance protein rad31
- DNA repair protein rad60
- Ran GTPase-activating protein 1
- E3 SUMO-protein ligase nse2
- Structural maintenance of chromosomes protein 5
- Importin beta-like protein kap111
- Ubiquitin-like-specific protease 2
Sequence:
MSSLCKTRLQEERKQWRRDHPFGFYAKPCKSSDGGLDLMNWKVGIPGKPKTSWEGGLYKLTMAFPEEYPTRPPKCRFTPPLFHPNVYPSGTVCLSILNEEEGWKPAITIKQILLGIQDLLDDPNIASPAQTEAYTMFKKDKVEYEKRVRAQARENAP
Protein: Defensin-like peptide 3 (DLP-3) (P82141)
Organism: Ornithorhynchus anatinus (Duckbill platypus)
Function: Does not show antimicrobial, myotoxic, hemolytic and cell-promoting activities.
Subcellular location: Secreted {ECO:0000269|PubMed:10417345}.
Interaction partners:
Sequence:
FEMQYCWSHSGVCRDKSERNNKPMAWTYCENRQKKCEF
Protein: At3g13171 (Transmembrane protein) (Q9LK55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEFREKLLKFKLQIVFAFVLSLLTVALVAYSPGFLTVLSYFWPLFLSTALFLAAVFFFARTSDLPVSSTIIPGEGAGLKVAAEGILDYVVGGQHEDILFDSFTKLD
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (E7F0B3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MPGMVLFRRRWSVGSDDLVLPAFFLFVLHCIWLVVLSVVLFGLPYSSEQSCSVTLVDHGRGYLGILVSCLICESAIMWLSMRGSILYTQPREAVQYVLYIRLAILLVELVYAVVGIAWLVQYYQPCPDITAKNLALGIVACNWLVIFSVCFTMMCTFDPTGRTFVKLKATRRRQRNLTTYTLRHRLEEGQASSWSRRLKFFMCCTRAKDTQSDAYSEVASLFAEFFRDLDIVPSDIIAGLVLLRQRQRAKRSAILDQANNDVLAFLSGMPVTRNTKYLDLKNSTEMAMYKEVCYYMLFAMAAYGWPVYLLRKPACGLCRLVSTCSCNTSVSGSRLSQSVTVEEDNCCGCNVLAIRRQFLDRDLKEVQIVYTSCHDAVYETPFFVAVDHAKKKVVISIRGTLSPKDALTDLTGDSERLPVEEQHGTWLGHKGMVYSAEYIKKKLEQEMILSQAFGRDLSKGTMHYGLVIVGHSLGAGTAAILSFLLRPQYPSLQCYSYSPPGGLLSEDAMEYSKEFVTSVVLGKDLVPRIGLSQLEGFRRHLLEVLQKSDKPKWRIIAGGTKCIPKSELPMDDEAPVSQGVTPSSSRLWLHPSDLSIALSASTPLFPPGRVIHVVHNHPPEMCCGQEEPTYSALWGDNKAFDEVIISPAMLNEHMPHVVMDGLNKVLENYNKGKTALLSAAKIMVSPTEVDLNPETIFLDTSNSPQPTPATHHRRNSSVRSCARSEISLDGFSECPPPPVPIVLTGARERLAVELRERKAPLAIMESLSDAESVYSLDSRRSSAALRGSPCLGSLPFPLDAPIPEENPSLSSRTELLAAEGLTQDLGEAGPYIPTPPEPEEPSNDIPYNNEYFTPELKSTTDPETDSSVVPDSQDSYRVASRTGSRPEKLREFEEKEVKVDLSQTLPAVTPLSNGTPSQAVLEFAQYLDSLFRLDGSSSPPLELSDAESESGRGSYSQAEEHQEEQRVKNADKLLARAALEPNLVPKPPRTFAGSADPSSGISLSPSFPLSSSGELNDFSPADGVLPVNHTSTLRTSAASPNPKETALSSMV
Protein: Glycogen [starch] synthase, muscle (EC 2.4.1.11) (Glycogen synthase 1) (A2RRU1)
Organism: Rattus norvegicus (Rat)
Function: Transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan.
Interaction partners:
- 1,4-alpha-glucan branching enzyme
- Glycogenin-1
- UTP--glucose-1-phosphate uridylyltransferase
- Protein phosphatase 1 regulatory subunit 3C
- Glycogen synthase kinase-3 beta
- Protein phosphatase 1, regulatory subunit 3D
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase 1 regulatory subunit 3A
- Protein phosphatase 1 regulatory subunit 3B
- Protein phosphatase 1 regulatory subunit 3E
Sequence:
MPLSRSLSMSSLPGLEDWEDEFDPENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYYLVGPYTEQGVRTQVELLEPPTPELKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQNEEKPYVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADIFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALAKAFPDHFTYEPHEVDATQGYRYPRPASVPPSPSLSRHSSPHQSEDEEEPRDGPLREDSERYDEEEEAAKDRRNIRAPEWPRRASCSSSTGGSKRSNSVDTGPSSSLSTPTEPLSPTSSLGEERN
Protein: Small ribosomal subunit protein uS14 (40S ribosomal protein S29A) (A0A1D8PTR4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein eL37
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL11
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL43
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL20
Sequence:
MAHENVWFSHPRNFGKGSRQCRHCSSHSGLIRKYGLDLCRQCFREKAADIGFNKYR
Protein: Uncharacterized protein (Q583W0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRPGSQFTPKAIQVFKSFATAAPAVMEVGTQSGIPKDLIGGAIGQLCNEEGDATSNGGVPFKAAEIRLYSPPPLKNSKAQVMLLFRGTKFVTVEESIGAGPEGTILFFSSSLLVALPYGVLQEGESNAFRITLCRVERRPDSAILDKSHLPDKELAILEKHANDVEKLKASVSQWPHEGSDNTVYDGTMEYGDYGMVYCFNTNYVGVSTLLSADVQWGETVLTHSSEGKRV