wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl-coenzyme A diphosphatase YFT2 (EC 3.6.1.-) (FIT family protein YFT2) (Q06676)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Preferentially hydrolyzes unsaturated long-chain acyl-CoA substrates in the endoplasmic reticulum (ER) lumen (By similarity). This catalytic activity is required for maintaining ER structure and for lipid droplets (LDs) biogenesis, which are lipid storage organelles involved in maintaining lipid and energy homeostasis (By similarity). May directly bind to diacylglycerol (DAGs) and triacylglycerol, which is also important for LD biogenesis (By similarity). May support directional budding of nacent LDs from the ER into the cytosol by reducing DAG levels at sites of LD formation (By similarity). May play a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Involved in phospholipid biosynthesis (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03232, ECO:0000269|PubMed:26504167, ECO:0000269|PubMed:29526591}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03232}. Vacuole {ECO:0000269|PubMed:29417057}. Note=Enriched at sites of lipid droplet (LD) biogenesis. {ECO:0000269|PubMed:29526591}.
Interaction partners:
- Acyl-coenzyme A diphosphatase SCS3
- Seipin
- Protein PET10
- Peroxisomal membrane protein PEX30
- Diacylglycerol O-acyltransferase 1
- Protein LDB16
- Phospholipid:diacylglycerol acyltransferase
Sequence:
MIRQLNYWSRKAYLIYPFQVFVGALLSIVVSSETLNHQKETCALLKSSNIFNVIFAYKANQLWPFLFFSLAFLQIYFHYLARMDILPLPISSTETSSSYLTYTNHWPLLKNRIISIMITQYACKFVLKYLLLFLNFQFIDHVFIWTGGECSSGSKTTSAEKCRLENGKWDGGFDISGHFCFLVSISMILWMELHLFSRFVQAEDMFWVVNKWVRACLAIVCAVLVIWICILWVTAIYYHTILEKVLGCLMGFICPVFIYHILPKIGILHNYLYL
Protein: LP05312p (Q5U119)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCRDHLLGSGILEPLLHVLSNSDRITMIRNAVWTLSNLCRGKSPPADFAKISHGLPILARLLKYTDADVLSDTCWAIGYLSDGPNDKIQAVIDAGVCRRLVELLLHPQQNVSTAALRAVGNIVTGDDQQTQVILGYNALTCISHLLHSTAETIKKESCWTISNIAAGNREQIQALINANIFPQLMVIMQTAEFKTRKEAAWAITNATSSGTHEQIHYLVQVGCVPPMCDFLTVVDSDIVQVALNALENILKAGEKFQTRPNPYAITIEECGGLDKIEYLQAHENRDIYHKSFYIIEQYFGNEEEDSRVAPVAGTQQFEFDPDNMPSTGFNF
Protein: Cell division protein CrgA (P9WP57)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in cell division. Plays an important role in septal peptidoglycan synthesis and cell shape morphogenesis. May facilitate the recruitment of the peptidoglycan synthesis machinery to poles and septal zones and coordinate peptidoglycan synthesis at these sites.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00631, ECO:0000269|PubMed:21531798}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00631, ECO:0000269|PubMed:21531798}. Note=Localizes to midcell sites in an FtsZ-dependent manner and colocalizes with FtsZ. Localizes at septa, at poles and on membranes.
Interaction partners:
- Cell wall synthesis protein CwsA
- Cell wall synthesis protein Wag31
- Uncharacterized protein Rv0010c
- Peptidoglycan D,D-transpeptidase PbpA
- Penicillin-binding protein PbpB
- Cell division protein FtsZ
- Cell division protein FtsQ
- Probable cell division protein WhiA
- Uncharacterized protein Rv0057
- Probable conserved transmembrane protein
Sequence:
MPKSKVRKKNDFTVSAVSRTPMKVKVGPSSVWFVSLFIGLMLIGLIWLMVFQLAAIGSQAPTALNWMAQLGPWNYAIAFAFMITGLLLTMRWH
Protein: RNA 3'-terminal phosphate cyclase (RNA cyclase) (RNA-3'-phosphate cyclase) (EC 6.5.1.4) (P46849)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Subcellular location: Cytoplasm.
Interaction partners:
- RNA-splicing ligase RtcB
- Transcriptional regulatory protein RtcR
- Small ribosomal subunit protein uS4
- Ribonuclease D
- Small ribosomal subunit protein uS11
- tRNA
- Ribosomal RNA small subunit methyltransferase A
- Small ribosomal subunit protein bS1
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS12
Sequence:
MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQHLTAVKAATEICGATVEGAELGSQRLLFRPGTVRGGDYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQQTTLLRHGFYPAGGGVVATEVSPVASFNTLQLGERGNIVQMRGEVLLAGVPRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASTAAVGEYLADQLVLPMALAGAGEFTVAHPSCHLLTNIAVVERFLPVRFSLIETDGVTRVSIE
Protein: Large ribosomal subunit protein eL39 (60S ribosomal protein L39) (L46) (YL40) (P04650)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL36B
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL6B
- Large ribosomal subunit protein uL6A
- Large ribosomal subunit protein eL8B
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL15
Sequence:
MAAQKSFRIKQKMAKAKKQNRPLPQWIRLRTNNTIRYNAKRRNWRRTKMNI
Protein: Ribonuclease VapC24 (RNase VapC24) (EC 3.1.-.-) (Toxin VapC24) (P9WF87)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. Its cognate antitoxin is VapB24 (By similarity).
Interaction partners:
- Putative antitoxin VapB24
- Cyclo
- Methyltransferase type 12 domain-containing protein
- Ribonuclease VapC40
- Chorismate pyruvate-lyase
- Conserved protein
Sequence:
MLSIDTNILLYAQNRDCPEHDAAAAFLVECAGRADVAVCELVLMELYQLLRNPTVVTRPLEGPEAAEVCQTFRRNRRWALLENAPVMNEVWVLAATPRIARRRLFDARLALTLRHHGVDEFATRNINGFTDFGFSRVWDPITSDG
Protein: Trace amine-associated receptor 9 (TaR-9) (Trace amine receptor 9) (Trace amine receptor 3) (TaR-3) (Q96RI9)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5QD04}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5QD04}.
Interaction partners:
Sequence:
MVNNFSQAEAVELCYKNVNESCIKTPYSPGPRSILYAVLGFGAVLAAFGNLLVMIAILHFKQLHTPTNFLIASLACADFLVGVTVMPFSTVRSVESCWYFGDSYCKFHTCFDTSFCFASLFHLCCISVDRYIAVTDPLTYPTKFTVSVSGICIVLSWFFSVTYSFSIFYTGANEEGIEELVVALTCVGGCQAPLNQNWVLLCFLLFFIPNVAMVFIYSKIFLVAKHQARKIESTASQAQSSSESYKERVAKRERKAAKTLGIAMAAFLVSWLPYLVDAVIDAYMNFITPPYVYEILVWCVYYNSAMNPLIYAFFYQWFGKAIKLIVSGKVLRTDSSTTNLFSEEVETD
Protein: Probable DNA-directed RNA polymerases I, II, and III subunit RPABC2 (RNA polymerases I, II, and III subunit ABC2) (RPB6 homolog) (Q17684)
Organism: Caenorhabditis elegans
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit rpb-9
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- DNA-directed RNA polymerase subunit
- RNA polymerase Rpb4/RPC9 core domain-containing protein
- DNA-directed RNA polymerase II subunit RPB1
- Probable DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase I subunit RPA2 homolog
Sequence:
MADEDDYQDMDNDDFVDDNEMEDVIEEDPQRPDNEDEDDDNVDENFELFDQGKAVPTSEHVTTPFMTKYERARVLGTRALQIAMGAPVMVELEGETDPLEIARKELKQRRIPIIVRRYLPDGSYEDWPTDQLQLADW
Protein: Nucleoprotein (Nucleocapsid protein) (Protein N) (C5E522)
Organism: Influenza A virus (A/New York/1682/2009(H1N1))
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04070, ECO:0000256|RuleBase:RU361251}.
Interaction partners:
Sequence:
MASQGTKRSYEQMETGGERQDATEIRASVGRMIGGIGRFYIQMCTELKLSDYDGRLIQNSITIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVDGKWMRELILYDKEEIRRVWRQANNGEDATAGLTHIMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTIAMELIRMIKRGINDRNFWRGENGRRTRVAYERMCNILKGKFQTAAQRAMMDQVRESRNPGNAEIEDLIFLARSALILRGSVAHKSCLPACVYGLAVASGHDFEREGYSLVGIDPFKLLQNSQVVSLMRPNENPAHKSQLVWMACHSAAFEDLRVSSFIRGKKVIPRGKLSTRGVQIASNENVEIMDSNTLELRSRYWAIRTRSGGNTNQQKASAGQISVQPTFSVQRNLPFERATVMAAFSGNNEGRTSDMRTEVIRMMESAKPEDLSFQGRGVFELSDEKATNPIVPSFDMSNEGSYFFGDNAEEYDS
Protein: Transcriptional regulator LdrP (Cyclic AMP receptor protein/Fumarate and nitrate reduction regulator superfamily protein LdrP) (CRP/FNR superfamily protein LdrP) (Light induced transcription regulator-dependent regulatory protein) (LitR-dependent regulatory protein) (LdrP) (Q53W63)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Activates transcription. Positively regulates PcrtB promoter upstream of the crtB operon in a cAMP-independent manner. Regulated genes include genes encoding DNA photolyase, phytoene synthase and cytochrome P450 monooxygenase, which are involved in carotenoid biosynthesis. Positively regulates the light-inducible gene cluster in the megaplasmid in a cAMP-independent manner.
Interaction partners:
Sequence:
MKRFARKETIYLRGEEARTLYRLEEGLVRVVELLPDGRLITLRHVLPGDYFGEEALEGKAYRYTAEAMTEAVVQGLEPRAMDHEALHRVARNLARQMRRVQAYEAHLQTGELRARIARYLLFLADTPLSARDRQGIYVTVSHEEIADATASIRESVSKVLADLRREGLIATAYRRVYLLDLAALEREAGSALEAA
Protein: At3g23170 (Q9LTD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitogen-activated protein kinase 11
Sequence:
MSTTMKRQGCSSDSGDLRRQPSRLLKRPPALKIVPATPAANNWNTAIPLLSPLALSPESSPVDQPPVEKNQSTAVAVEKTPVFKKWQHPAAPFYYESSTFVPPFVPV
Protein: Retrograde regulation protein 2 (P32608)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for a novel path of interorganelle communication between mitochondria, peroxisomes and the nucleus, thereby maintaining a functional metabolic interaction between the tricarboxylic acid and glyoxylate cycles. In particular, required for the retrograde expression of the peroxisomal isoform of citrate synthase, CIT2.
Interaction partners:
- Retrograde regulation protein 1
- Negative regulator of RAS-cAMP pathway
- Protein BMH1
- Retrograde regulation protein 3
- Protein BMH2
- Peroxisomal catalase A
- Citrate synthase, peroxisomal
- Target of rapamycin complex subunit LST8
Sequence:
MSTLSDSDTETEVVSRNLCGIVDIGSNGIRFSISSKAAHHARIMPCVFKDRVGLSLYEVQYNTHTNAKCPIPRDIIKEVCSAMKRFKLICDDFGVPETSVRVIATEATRDAINADEFVNAVYGSTGWKVEILGQEDETRVGIYGVVSSFNTVRGLYLDVAGGSTQLSWVISSHGEVKQSSKPVSLPYGAGTLLRRMRTDDNRALFYEIKEAYKDAIEKIGIPQEMIDDAKKEGGFDLWTRGGGLRGMGHLLLYQSEGYPIQTIINGYACTYEEFSSMSDYLFLKQKIPGSSKEHKIFKVSDRRALQLPAVGLFMSAVFEAIPQIKAVHFSEGGVREGSLYSLLPKEIRAQDPLLIASRPYAPLLTEKYLYLLRTSIPQEDIPEIVNERIAPALCNLAFVHASYPKELQPTAALHVATRGIIAGCHGLSHRARALIGIALCSRWGGNIPESEEKYSQELEQVVLREGDKAEALRIVWWTKYIGTIMYVICGVHPGGNIRDNVFDFHVSKRSEVETSLKELIIDDANTTKVKEESTRKNRGYEVVVRISKDDLKTSASVRSRIITLQKKVRKLSRGSVERVKIGVQFYEE
Protein: Calcium/calmodulin-dependent protein kinase cmkA (CMPK) (EC 2.7.11.17) (Multifunctional calcium/calmodulin-dependent protein kinase) (ACMPK) (CaMK) (Q00771)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Calcium/calmodulin-dependent protein kinase. Required in nuclear division cycle for progression from G2 to mitosis. Required for hyphal growth.
Interaction partners:
- Calmodulin
- Calmodulin
Sequence:
MSFANMFNKLSGQPESYEKKSLYRFGRTLGAGTYGIVREADCSSGKVAVKIILKRNVRGNERMVYDELDLLQKLNHPHIVHFVDWFESKDKFYIVTQLATGGELFDRICEYGKFTEKDASQTIRQVLDAVNYLHQRNIVHRDLKPENLLYLTRDLDSQLVLADFGIAKMLDNPAEVLTSMAGSFGYAAPEVMLKQGHGKAVDIWSLGVITYTLLCGYSPFRSENLTDLIEECRSGRVVFHERYWKDVSKDAKDFILSLLQVDPAQRPTSEEALKHPWLKGESASDRDLLPEIRAYIARSRLKRGIEIIKLANRIEALKMQEEDEEDIPSAVDVQASEASDKSGLSPFPALSTENSNTHPASTGNGESGGTKKRSLSKIARGAIFREVVLAKVREMKENEEREKVEREARERAHS
Protein: Candida glabrata strain CBS138 chromosome K complete sequence (Q6FN33)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL5
- L37
- 40S ribosomal protein S12
- Candida glabrata strain CBS138 chromosome K complete sequence
- Small ribosomal subunit protein uS9
- 40S ribosomal protein S26
- 60S ribosomal protein L29
- Candida glabrata strain CBS138 chromosome F complete sequence
- 60S ribosomal protein L27
Sequence:
MSDIQKDKVQEQEAPQIIKIRMTLTSTKVKQLENVSANIIRNAEQNNLVKKGPVRLPTKVLRISTRKTPNGEGSKTWETYEMRIHKRYIDFEAPVSIVKRITQITIEPGVDVEVVVASN
Protein: ribonuclease III (EC 3.1.26.3) (Q2Q3V6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVASIADVHFEHWNKYGDSVTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHPSNVQQREQQPAPRPEDFEGKIVTQWYANYDKPMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSRPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKMIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHFYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA
Protein: FarA (Q5AXD0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MSAAAGDKFIDSSASRPSPTPSTAGSTGTAGISVRAGANGQMSFRRQRASRACETCHARKVRCDAASLGVPCTNCVAFSIECRIPTPKRKKSQAKPREVGDSNGDGDDKSQSQEKREESLPMPGKDAFGYQNSNTSNTNAMAVNGMPVTTLTEAQAAQQASQNSTYAQFMKPKFARAPIKEAGRVAYLGESSNLSLLVQDRHGTTDVVHYPLPPNIRGSRARVSDLDNLELDILHQRGAFLLPPKSLCDELVDAYFKWVAPVVPIVNRSRFMRQYRDPKNPPSLLLLQAILLAGSRVCTNPQLMDANGSTTPAAMTFYKRAKALYDANYEDDRVTIVQALVLLGWYWEGPEGWCPKPIMVTGLLTCPDVTKNVFYWTRVAIIVAQGSGMHRSVESSQLSKPDKRLWKRIWWTLFTRDRSVAVALGRPICINTDDADVEMLTEEDFVEDEIDIAAEYPPDPVHVQFFLQYVKLCEIMGLVLSQQYSVASKSRRMNAMDLTHSDMALADWLQNCPREVCWQRQRHHFWAALLHANYYTTLCLLHRAHMPPASSVPSSYRVEEMAYPSRTIAFQAAGIITSIVENLQTHNEIRYTPAFIVYSLFSALIMHVYQMRSSVPSIVATCQERINICMQALKDVSKVWLVAKMVHTLFESILGNKLLEERLQKAAGKRHQRVKPDSNHSNQHLPSRRPDPPPKRKFDDMDLALPNGGPTPPVSYERSRPQTPAATPSRELPQSTMSIPQTSPTAAKDGLPGAGNSRANTRPTTPFNAQFSLPATPPDLFLVTRTSPNLSPSLWENFQPDQLFPDGTAIFPELTSPQNTTVDPQLQMQSQLHTHDMVQQQMPPRTSLAGTQGSPEILSSMPPAIGMQGQPQQMYGMDPQQSWQMPGLDPTVAGAMDNASQDDNWSSSSRSGPTAPTTLNVEDWFQFFGINGSFGEMAV
Protein: KISS1 receptor (K7EQ45)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MHTVATSGPNASWGAPANASGCPGCGANASDGPVPSPRAVDAWLVPLFFAALMLLGLVGNSLVIYVICRHKPMRTVTNFYIGLGAGHVCHSDRHECG
Protein: Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA) (Q6ENH4)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00458}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00458}.
Interaction partners:
- Photosystem I iron-sulfur center
- Photosystem I reaction center subunit II
- Photosystem I P700 chlorophyll a apoprotein A2
- Uncharacterized protein
- Photosystem I reaction center subunit III
- NAD
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit VIII
- Photosystem I reaction center subunit psaK, chloroplastic
- Chlorophyll a-b binding protein
Sequence:
MMIRSPEPEVKIVVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTGDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALIFASLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINQFLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYAEFLSFRGGLDPITGGLWLSDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSTTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWVQNLHAGAPSVTAPGATTSTSLTWGGGELVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG
Protein: Superoxide dismutase (EC 1.15.1.1) (Q381T3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein uL15/eL18 domain-containing protein
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL3m
Sequence:
MAFSIPPLPWGYDGLAAKGISKEQVTFHYDKHHMGYVTKLNAAAKSNPALAAKSVEEIIRTEKGPIFNLAAQIFNHNFYWESMSPNGGGEPSGKLAEAIRASFGSFAKFKEEFTNAAVGHFGSGWAWLVQDTTTKKLKVFQTHDAGCPLTEADLKPILACDVWEHAYYIDYKNDRPAYVQTFWNVVNWDHAENQFTRKRNPGAPHSDL
Protein: Hemagglutinin-esterase (HE protein) (EC 3.1.1.53) (E3 glycoprotein) (P15776)
Organism: Bovine coronavirus (strain Mebus) (BCoV) (BCV)
Function: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface. {ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:2319653}.
Interaction partners:
Sequence:
MFLLLRFVLVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTNYVGVYDINHGDAGFTSILSGLLYDSPCFSQQGVFRYDNVSSVWPLYSYGRCPTAADINTPDVPICVYDPLPLILLGILLGVAVIIIVVLLLYFMVDNGTRLHDA
Protein: BBSome complex member BBS4 homolog (Bardet-Biedl syndrome 4 protein homolog) (A1Z8E9)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be required for microtubule anchoring at the centrosome. Required for ciliogenesis (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}.
Interaction partners:
- Bardet-Biedl syndrome 1
- BBSome complex member BBS5
- Bardet-Biedl syndrome 9
- Bardet-Biedl syndrome 8
- BBSome interacting protein 1
- Centrosomal protein Cep290
- Intraflagellar transport 20
- No mechanoreceptor potential B, isoform D
- Intraflagellar transport protein 57 homolog
- Outer segment 5
Sequence:
MYEPGTEQINCNGRLIELPTLEVVRPAPKMPSDANIDWLLHIYFTRREFTRCRRLIERELNRHLNPEYLYFVQGLIDREEGNHIEALRHLQKSAELNPRNIETYKEIGRTLYIMGRFSQALGVFREAEQRSSRQDHEIYHYLGELLYRAATTQSQKDVASQQQDEARTYFELAVQSGRKLESYVRLAELYRKDKQYQKAIEILENCLHLTPENSEVLIEISVLYLKINETQKAHDRLAEVVSIERKCSPKGLLAFGAILQSRNDIDGALSKYSQIANAEPEIAELWNNIGLCFFKKQKFIVAISSLRKSVWLSPLNYNALYNLSLIYIASEQYASAFHTLAAAINLRKDNAECYMLLGLCLRKLDDMENAFVALERASSMATGQQGAGRNPLVVLNFALFCYETGRLALSTEQYNRFMSQAQDLLLPTEYKFQATKLKSLLRISNQGNGILLDSADMGESDLGHNRATELLPDELPLEVNAVVSQN
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (H3BQB1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
XADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPGQRVVVVDDLLATGGAGLEHLLSAAQANWGPHPPIPRNHERCL