wanglab/gogpt-training-data huggingface dataset:
Protein: Ceramide synthase LAG1 (Longevity assurance factor 1) (Longevity assurance gene 1 protein) (Longevity assurance protein 1) (Very-long-chain ceramide synthase LAG1) (EC 2.3.1.297) (P38703)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ceramide synthase complex that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward hexacosanoyl-CoA (C26:0-CoA). N-acylates sphinganine and phytosphingosine bases to form dihydroceramides and phytoceramides, respectively. Redundant with LAC1. Facilitates ER-to-Golgi transport of GPI-anchored proteins. Involved in the aging process. Deletion of LAG1 results in a pronounced increase (approximately 50%) in mean and in maximum life span.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Ceramide synthase subunit LIP1
- Alkaline ceramidase YDC1
- Alkaline ceramidase YPC1
- Ceramide synthase LAC1
- Sphingoid long chain base kinase 4
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- 3-ketodihydrosphingosine reductase TSC10
- Sphingolipid C4-hydroxylase SUR2
- Sphingoid long chain base kinase 5
- Dihydrosphingosine 1-phosphate phosphatase YSR3
Sequence:
MTSATDKSIDRLVVNAKTRRRNSSVGKIDLGDTVPGFAAMPESAASKNEAKKRMKALTGDSKKDSDLLWKVWFSYREMNYRHSWLTPFFILVCVYSAYFLSGNRTESNPLHMFVAISYQVDGTDSYAKGIKDLSFVFFYMIFFTFLREFLMDVVIRPFTVYLNVTSEHRQKRMLEQMYAIFYCGVSGPFGLYIMYHSDLWLFKTKPMYRTYPVITNPFLFKIFYLGQAAFWAQQACVLVLQLEKPRKDYKELVFHHIVTLLLIWSSYVFHFTKMGLAIYITMDVSDFFLSLSKTLNYLNSVFTPFVFGLFVFFWIYLRHVVNIRILWSVLTEFRHEGNYVLNFATQQYKCWISLPIVFVLIAALQLVNLYWLFLILRILYRLIWQGIQKDERSDSDSDESAENEESKEKCE
Protein: Single-stranded DNA-binding protein 3 (Lck-associated signal transducer) (Sequence-specific single-stranded-DNA-binding protein) (Q9D032)
Organism: Mus musculus (Mouse)
Function: May be involved in transcription regulation of the alpha 2(I) collagen gene where it binds to the single-stranded polypyrimidine sequences in the promoter region.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- LIM domain-binding protein 1
- LIM domain-binding protein 2
- Single-stranded DNA-binding protein 2
- LIM/homeobox protein Lhx2
Sequence:
MFAKGKGSAVPSDGQAREKLALYVYEYLLHVGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPERRDTCEHSSEAKAFHDYSAAAAPSPVLGNIPPNDGMPGGPIPPGFFQGPPGSQPSPHAQPPPHNPSSMMGPHSQPFMSPRYAGGPRPPIRMGNQPPGGVPGTQPLLPNSMDPTRQQGHPNMGGSMQRMNPPRGMGPMGPGPQNYGSGMRPPPNSLGPAMPGINMGPGAGRPWPNPNSANSIPYSSSSPGTYVGPPGGGGPPGTPIMPSPADSTNSSDNIYTMINPVPPGGSRSNFPMGPGSDGPMGGMGGMEPHHMNGSLGSGDIDGLPKNSPNNISGISNPPGTPRDDGELGGNFLHSFQNDNYSPSMTMSV
Protein: Non-structural protein ORF3 (ORF3) (K9N796)
Organism: Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1)
Subcellular location: Host endoplasmic reticulum {ECO:0000269|PubMed:24318862}.
Interaction partners:
Sequence:
MRVQRPPTLLLVFSLSLLVTAFSKPLYVPEHCQNYSGCMLRACIKTAQADTAGLYTNFRIDVPSAESTGTQSVSVDRESTSTHDGPTEHVTSVNLFDVGYSVN
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FTR6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
Sequence:
MKFSTLITSALLGTAIAAPHAAHTHKEKRDVVTKTMHAVQTVVVGPDGTPVQKAEAINEQVVENAPQPTTQQQQQQQQQASPAPAKSTTELAPASSPASSSSSSSSSNTKKPDTQVGGAGVKGITYTPYNADGTCKDASAVASDLAALSQYPTIRLYGTDCNQVENVFKAKASGQKLFLGVFDVSNIQGSVDAIKSAVNTYGSWDDVTTVSIGNELVNGGQASPAQVGQYVAAGRAALQAAGFNGPVVSVDTFIAVINNPELCQYSEYMAVNAHAYFDQYTKAQDAGSWLLQQIQRVWTACDGKKEVVITESGWPSKGQTLGVAVPSKQNQKDAVNSITAACGADTFLYNAFNDYWKADGPYGCEKYWGVLSDE
Protein: At5g26610 (D111/G-patch domain-containing protein) (Q147M4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor SYF2
- Casein kinase 1-like protein 10
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH3
- RNA helicase
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH2
- Tetratricopeptide repeat
- DExH-box ATP-dependent RNA helicase DExH14
- Transducin/WD40 repeat-like superfamily protein
- Pre-mRNA-processing factor 17
Sequence:
MDISRRESKTEASSREKRIYEKDQMNQESFIEGLAEEFRLPITHRVTENVDLEDVEQASLDVKISSSNVGFRLLQKMGWKGKGLGKQEQGITEPIKSGIRDRRLGLGKQEEDDYFTAEENIQRKKLDIEIEETEEIAKKREVLAEREQKIQSDVKEIRKVFYCELCSKQYRTVMEFEGHLSSYDHNHKKRFKEMKEMHGASGRDERKKREQQRQEREMTKMADARKQHQMQQSQQEVPENVPVSAPAKTTVAPLAVQDQRKTLKFGFSSKSGIISKSQPTSSIKKPKVAIASVFGNDSDED
Protein: Short-chain dehydrogenase/reductase pkfC (EC 1.1.1.-) (Aspernidine A biosynthesis cluster protein pkfC) (C8VI80)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone. The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA. Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E. The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Interaction partners:
- FAD-dependent monooxygenase pkfD
- Dehydrogenase pkfF
Sequence:
MVFGSRPPALTEANIGDQSGKVFIVTGATSGYGLLLSTYLYQNNGTVYLAARNAKKTAEVIADLKQRFPASRGRLDSISLNLSDLSTIKKSAEEFLAKETRLHVLWNNAGVMFPPAGSTTSQGYELQLGTNNVGPHLFTKLLYPTLAATAKEAPKNTVRVVWVSSDAASWAPKPAIDFNNLDYRRNESDRSKYGRSKAGTVMQAVELARRARKDGSGIVSIALDPGIANTGLQRDMGRLMSTMVKLIANKPEIGAYTQLFAGLSPEITAEVAEKEWVVPPGKIGCPRRDLFTDTETSRKWWEWNEEQVKAYL
Protein: Nucleolar and coiled-body phosphoprotein 1 (B8JIY2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Nucleolar protein 56
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit DKC1
- rRNA 2'-O-methyltransferase fibrillarin
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase I subunit RPA2
- Ribosomal L1 domain-containing protein 1
- RNA polymerase I and III subunit C.
- Ribosome biogenesis protein BRX1 homolog
- Kelch repeat and BTB domain-containing protein 8
Sequence:
MAEDSTVPSDLYQHVYSFLVENKFAKAAKEFLRQAKVKPQDQNEDSLMDIFNFWVKSPETKKRKAVTSGPAAVNGPSAKKAKKDADSSSSEDSSSEEEQAAPAKKAVQVKAPPPKKPAAVATKESSSEDSSDSEDEAPAKTTAKKPAAVKAAVQPAAAARKKDTSSSSEESDSEEEPSKTPAKVVKPVTGTPKTVSTPVSAAQKKQDSSSEDSSSDSEDEPPAKSAVKAAVPVKTPPPAKPAAPAVSSSDDSSSDEEDAPPSKKPKTGQFSAVPPPGTLTAQAPVKTPAASVKTVTPKAAAKNDSSSSDSSDSSSEDEAKKPAVKAAPAKAAPAKKAPTKVAPAQKKDSSSSDSSSSEDEATKPAIKVTPAKAASAKSTPAKAAQAKAAPAKVTPAAEESSSSSSEESEEESKKPAAKVAPGKAAAKRAPPKKTPAKVTPAAKESSPSSSDSEEDEPPTPAKATPAKAAPAKATPAKATPAKAAPAKKDDSSSSDSESSEDEAPAKPAATSKPVSTPKPGAKPAESSSASDSSSDEDEGPQKKPVTTPVSKPAPAKPPAAKTTNKPAESSSSSSDSSSDEEPKKKPATTPVSKPTPAKPTPTVKTTNKQAESSSDSSSDEEDKPQKKAATTPASKPVATSAKTTPAAKPAESSSDSDSSSDEEAQKKTTTPVPSKPATPAKPAAKAAESSSDSSDSEDETPAAKTAKPAAATATKSPAAASKPPVSASKPAAESSSSDSDSSSEDEKQAKTTVTPKAAPKPAVTPVNAKKAESSSSESSDSSDSETEAKKTPAKPVVANGKPVTKTPTSAAKTPAKKTAESSSSSDSSSDEEEPSKTPATKTPPATKTPPATKTPPATKTPPATKKQAAEAKAESSSSEESSEEEETPAATNGTQSAKKATPKNKKIATSTPQTFPRTKQKDSNAPFRRIREEDVEVDPRLKDNSFDAKMGANGDWGQKANNVLKFTKGKSFRHEKTKKKRGSYRGGAISTTVNSIKFDSD
Protein: Serum paraoxonase/lactonase 3 (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Q62087)
Organism: Mus musculus (Mouse)
Function: Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Serum paraoxonase/arylesterase 1
Sequence:
MGKLVALTLLGACLALIGERLLNFRERVSTTREIKATEPQNCHLIEGLENGSEDIDILPSGLAFISTGLKYPGMPAFAPDKPGRIFLMDLNEQNPEAQALEISGGLDQESLNPHGISTFIDKDNTAYLYVVNHPNMDSTVEIFKFEEQQRSLIHLKTLKHELLKSVNDIVVLGPEQFYATRDHYFTSYFLVLLEMILDPHWTSVVFYSPKEVKVVAQGFSSANGITVSLDQKFVYVADVTAKNIHIMKKHDNWDLTPVKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLIYNPEDPPGSEVLRIQDSLSDKPRVSTLYANNGSVLQGSTVASVYHKRMLIGTIFHKALYCDL
Protein: ATP synthase F(0) complex subunit g, mitochondrial (ATPase subunit g) (ATP synthase membrane subunit g) (O75964)
Organism: Homo sapiens (Human)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
Sequence:
MAQFVRNLVEKTPALVNAAVTYSKPRLATFWYYAKVELVPPTPAEIPRAIQSLKKIVNSAQTGSFKQLTVKEAVLNGLVATEVLMWFYVGEIIGKRGIIGYDV
Protein: Profilin-1 (Pollen allergen Zea m 12) (ZmPRO1) (allergen Zea m 12) (P35081)
Organism: Zea mays (Maize)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10760246}.
Interaction partners:
- Actin-1
- Actin-1
- Uncharacterized protein.
- Electron transporter
- Expansin-B10
- Ribosome-inactivating protein 9
- Expansin-B9
Sequence:
MSWQTYVDEHLMCEIEGHHLTSAAIVGHDGATWAQSTAFPEFKPEEMAAIMKDFDEPGHLAPTGLILGGTKYMVIQGEPGAVIRGKKGSGGITVKKTGQSLIIGIYDEPMTPGQCNLVVERLGDYLLEQGM
Protein: Ribitol-5-phosphate transferase (A3KP10)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MARLNRTFVLTLLIAVSSVFLLFQLYNYRLSAAKNGLNVLNNKGYLSGKEAHWHLLKRFLGLVHKFKLPVFLVDTVSLALLSQDAVLYRDSQLKDPHCSFLCTHRDFTSFALLGNLWKYDAALLDAASERGLELLEIHGKDPRLISTDDLTAKEIPLHFLFRFNGRVVHVVVLYERSGKYLWHGPLRLTASLDRTFAPFGKLDYGHHAGAYDRPELILTTLDGLDVRIPKNFSGFLHEYSSSRFLECRSREAKAFFQLYPEDTSPEAVDFRMRAKSLLHLASRVLFTLRVPFWLSSGTCLGWYRQCNIIPYSKDVDVGIWIKDYRPDIIPAFQKAGLPLKHKFGKVEDSLELSFQGNDVKLDIFFFYDDGDVVWNGGTQAKSGRKFKYVFPRFSLCWTEFMELKVQVPCETEDYVRANYGPDWNIPVKTWDWKTSPFNVQENGVWPLREWDDVIQVY
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (Q6IVU5)
Organism: Junin mammarenavirus (JUNV) (Junn mammarenavirus)
Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
Interaction partners:
Sequence:
MGNCNGASKSNQPDSSRVTQPAAEFRRVAHSSLYGRYNCKCCWFADTNLITCNDHYLCLRCHQVMLRNSDLCNICWKPLPTTITVPVEPTAPPP
Protein: Integrin subunit beta 1 binding protein 1 (C9JBU8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALY
Protein: Carboxypeptidase B (EC 3.4.17.2) (Pancreas-specific protein) (PASP) (P15086)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000250|UniProtKB:P00732}. Zymogen granule lumen {ECO:0000250|UniProtKB:P55261}.
Interaction partners:
- Carboxypeptidase A1
- Carboxypeptidase B2
- Chymotrypsinogen B
- Chymotrypsinogen B2
- Chymotrypsin-like elastase family member 3A
- Chymotrypsin-like elastase family member 3B
- Chymotrypsin-like protease CTRL-1
- Plasminogen
- Bile salt-activated lipase
- Carboxypeptidase E
Sequence:
MLALLVLVTVALASAHHGGEHFEGEKVFRVNVEDENHINIIRELASTTQIDFWKPDSVTQIKPHSTVDFRVKAEDTVTVENVLKQNELQYKVLISNLRNVVEAQFDSRVRATGHSYEKYNKWETIEAWTQQVATENPALISRSVIGTTFEGRAIYLLKVGKAGQNKPAIFMDCGFHAREWISPAFCQWFVREAVRTYGREIQVTELLDKLDFYVLPVLNIDGYIYTWTKSRFWRKTRSTHTGSSCIGTDPNRNFDAGWCEIGASRNPCDETYCGPAAESEKETKALADFIRNKLSSIKAYLTIHSYSQMMIYPYSYAYKLGENNAELNALAKATVKELASLHGTKYTYGPGATTIYPAAGGSDDWAYDQGIRYSFTFELRDTGRYGFLLPESQIRATCEETFLAIKYVASYVLEHLY
Protein: Phosphomannomutase (EC 5.4.2.8) (A0A0K9RL25)
Organism: Spinacia oleracea (Spinach)
Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide for the synthesis of D-mannose-containing cell wall polysaccharides (galactomannans and glucomannans), glycolipids, glycoproteins and the antioxidant L-ascorbate (Probable).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0A0U1WZ18}.
Interaction partners:
- Mannose-6-phosphate isomerase
- NTP_transferase domain-containing protein.
- NTP_transferase domain-containing protein.
- NTP_transferase domain-containing protein.
- Phosphotransferase.
- Phosphotransferase.
- Phosphotransferase.
- Phosphotransferase.
- Phosphotransferase.
- Phosphotransferase.
Sequence:
MAAKPAIIALFDVDGTLTAPRKEVTPEMLKFMKELRKVVPVGVVGGSDLTKISEQLGKTVINDYDYVFAENGLVAYKDGAEVAIMSLKKLLGEEKLKEFINFTLKYIAELDIPIKRGTFIEFRNGMINVSPIGRNCSQEERDEFEKYDKIQKVRSTMVSVLREKFGHFNLTFSIGGQISFDVFPRGWDKTYSLRYLEDFNEIHFFGDKTFEGGNDYEIFASERTVGHTVTSPEDTMKQCTEIFLTKKE
Protein: Spermatogenesis-associated protein 32 (Testis-expressed protein 34) (Q96LK8)
Organism: Homo sapiens (Human)
Interaction partners:
- Spermatogenesis-associated protein 31A7
Sequence:
MGVTGAHGFPCCGKGSVEVAEMRDDLSQHQIQEEQELEADMLEQKPQLQVDLDLDPDPDPDPELEIGQVPALLESELYPALKLEAELDTEANSNEESDFEEPMQLVCKIESVHSNMGLPTPQTFRPWSLNSNCRSFTEENHVSACHHSISAQTSKHLFWANKLIQASEHSLQRAINMQLNNGSAGQPIRSPLREAIPTNALCSEEQLQIPDAHSAPPTTSSQAPSPLLSSDLPPPIDLTELITFASSLAMASSSRMDLPSLEHMMKAPPQEALEPSTEPLLTTVEEREPENHAETLPEKPREARAPLKSWSQEDKNFAQSYFDFSKPGIKRATIKGQIQLLQPPATSPLLQGSKEDSVPPGKEKENPLLVKIHFKLSAPTIPEK
Protein: Interferon (Q800H1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MWTYIFVIYVILQSQSSASTCEWLGRYRIITTESLNLLKNMGGKYADLETPFPSRLYTLMDKSKVEDQVKFLVLTLDHIIHLMDAREHMNSVNWDQNTVEDFLNILHRKSSDLKECVARYAKPAHKESYEIRIKRHFRTLKKILKKKQYSAEAWEQIRRVVKSHLQRMDIIASNARVNP
Protein: Calmodulin-binding protein CmbB (CaM-BP46) (Q54JC0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MTSNHLPHHNLTDEDQQEYNKIFKEFIFNIPHNMNPFSPQLDEKKNSHIVEYHWRSPSNTIPSTCNTLYVCFNSPIPVNVIPNNVIILCFLCENKTGFTKGPDFNHPIHPGTIPMSVRYIYFINATYNKPLIAHALPPSAEYLFLSDCYNQAFRAGDLPPNLNILETGDEYNQPFDPLVIPKSLRSLFLGKGYNQPLEFGGLTSLTCLVYDEGSISELPIISLPPNLEFLLLSDAFNHPIEAGMLPPKLKTLTFGDGFNQPLAVGTLPPSLENINFGKVFDQPFLPNVLPHHLKSISFHQFSYFSQTFENIPSHVQTVEFGYTYNKPITSLPSHLKYIKFSEKYNHPIDGVLPQSLTHCYLGKSFKRPLVPGIFPPGLKVLILNGYPKKIPPGTVPANCNFQKNPKQGACSVM
Protein: Neuronal growth regulator 1 (Kindred of IgLON) (Kilon) (Q9Z0J8)
Organism: Rattus norvegicus (Rat)
Function: May be involved in cell-adhesion. May function as a trans-neural growth-promoting factor in regenerative axon sprouting in the mammalian brain (By similarity).
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Transmembrane protein 18
- Glucosamine-6-phosphate isomerase
- IgLON family member 5
- Mitochondrial carrier 2
- Kctd15 protein
Sequence:
MVLLAQGACCSNQWLAAVLLSLCSCLPAGQSVDFPWAAVDNMLVRKGDTAVLRCYLEDGASKGAWLNRSSIIFAGGDKWSVDPRVSISTLNKRDYSLQIQNVDVTDDGPYTCSVQTQHTPRTMQVHLTVQVPPKIYDISNDMTINEGTNVTLTCLATGKPEPAISWRHISPSAKPFENGQYLDIYGITRDQAGEYECSAENDVSFPDVKKVRVVVNFAPTIQEIKSGTVTPGRSGLIRCEGAGVPPPAFEWYKGEKRLFNGQQGIIIQNFSTRSILTVTNVTQEHFGNYTCVAANKLGTTNASLPLNPPSTAQYGITGSACDLFSCWSLALTLSSVISIFYLKNAILQ
Protein: Sensory rhodopsin II (A0A1U7EZ03)
Organism: Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sensory rhodopsin II transducer
- Gamma-glutamyl phosphate reductase
- Chemotaxis protein CheA
- Lycopene beta-cyclase
Sequence:
MVGLTTLFWLGAIGMLVGTLAFAWAGRDAGSGERRYYVTLVGISGIAAVAYAVMALGVGWVPVAERTVFVPRYIDWILTTPLIVYFLGLLAGLDSREFGIVITLNTVVMLAGFAGAMVPGIERYALFGMGAVAFIGLVYYLVGPMTESASQRSSGIKSLYVRLRNLTVVLWAIYPFIWLLGPPGVALLTPTVDVALIVYLDLVTKVGFGFIALDAAATLRAEHGESLAGVDTDTPAVAD
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A8BPA7)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Interaction partners:
- non-specific serine/threonine protein kinase
- DNA helicase
- DNA replication licensing factor MCM4
- DNA helicase
- DNA helicase
- DNA replication licensing factor MCM7
- DNA helicase
- Kinase
- CDC45-like protein
- Origin recognition complex subunit 1
Sequence:
MTRRHQADTGTADYTQYRQEFPEIPFDRYKITQHVGKGAFSKVFLAYTPEFQRRAIKRIRLTAKPHQLLKEIEFLRRLEGKSHIVQIKEIRFSDATLQTTVITSYSDTDDFKSVILDFTPREIQAYMRSILTALSHLEKLKIIHRDIKPGNFLFERKTGKGLLIDFGLAQTLREVREFPLLRGQSKSRKGVIHINLDRLMRQSNQYLTDLTAQGEETYYTARMSLKEGQTVPAAHVTGSNAAASTNVVRPNDDTAERLPIAGYINKDHSTFRPLPPSAHSGTHGYRAPEILVPVRNQDCKIDSWSVGVILIQILTGKTSLFRGNPTVDIYEILAIRSIIGTDRFIQGMSRLKADFSLTAGAPMPQAIALEELAEWYNPDLLAVLPASCFDLCRKLLEFDPESRLSATEALSHPFLAMDENLLPNYRFQDGAHSKSLLSFTGYANATNSQDSMNREEETLQALRKRGSEIAERLGLCRVTSETLADEYSTMSPQSMIPLPRDLRKQAMKSVQKFALDKTVQGPSGIIVERSKTSDYSFPSNSSVQDLSSCGGVTLSRPRLAAAPGSHARHCAIDAAMRQKIAYYKEKGIRVTLDDLHREVLDQQWEIANKDKETFERAVRATAVRRRLDPWVQPLKALDKELRICQKDVRKAAEEYRRTVLSLGIIDLETKTADEGHRHKVSAGLDGDKDKLDAKNEQGRTQLSGATGITVTGQGAGAFTNYHSYLSALIPSPNALKTAVNIKLASDAKIQVAKTMDVKTVESFYYPKYYAINKIRTHRLLNFIVKSELAQTAALDTGNSVGVAGVTTCTNHLTKTLATVIATKAWEVVHSNSSKNMITKEKSRSVYDLTMKAAKIASVSHRLALSGPDAWEAKGESFFLSPNSRLGMIEIKADECKFRVHDFNTKILQHQHHASQCQFIIQERTGFLSKIAQLEESIRSKMNANTEQIKILQGTLKSSANKNDTIQEEINYLTAQKEQQEAAISKFVAVVADNKTLIAQHKESYANLTSELSVMIANKNEWVKEYKQIYERDIKDADYSFGEEHEHLLENFSDCWSETISVSDEGVEARPAFKPFGVYNPSELQEPYFTSMDEMKTALRQQDAAMDRRKSRREQRRRLECLIAKRRDPILEQLRQMNDDIQTARAELLDSMITGEGISPAPTDKTDKTKHNSLMPKQALSVSPSMLAQAVAIKSLAAKYATVMGFFTKHTLSGAYCVTSTFEPGRTRQPAEVGLLSFRNGNITGEMHQTDGGAKRASSTGPNSRGNTTVAGMSTNASINPNANRGSAGGLSNDNKQLHALKPYARNALAYISQQLEVERKAHALLTLISSPYGRYLMPFHKILSDGAPFPSGARSNSFYIMCSKSDLFIPAELQEAILTLQNLSERYFRTSIGRKDLYLIAAACQTELDLRAQNATNTNNPNNANNELQHLGLSRRPPNLDYMLLLQGKLNNLIPYFEDTRSTSAISGLNKSATHRSLADPGRTSQRYPQTCKYIQTILEQVMRRFVAMPGVLSGLYEECIEGISNIKGRILEAVVIELINILQTGSTENVDRVRGGCSFYENNVMLLRCLRLLQTAINTLGAGTVFEILRGLVYPVTLLRGSGFINGVEKTQKPVAESDSPDKKPRRFNYLTEEDVKSVAKMVSKPENITGSFDASLLQKIDDSNARRRLLLQTQYGGRHHLNAIRQRRRRAEIYF
Protein: Protein DBF4 homolog A (Activator of S phase kinase) (Chiffon homolog A) (DBF4-type zinc finger-containing protein 1) (Q9UBU7)
Organism: Homo sapiens (Human)
Function: Regulatory subunit for CDC7 which activates its kinase activity thereby playing a central role in DNA replication and cell proliferation. Required for progression of S phase. The complex CDC7-DBF4A selectively phosphorylates MCM2 subunit at 'Ser-40' and 'Ser-53' and then is involved in regulating the initiation of DNA replication during cell cycle.
Subcellular location: Nucleus {ECO:0000269|PubMed:10373557}.
Interaction partners:
- DNA replication licensing factor MCM4
- Cell division cycle 7-related protein kinase
- Origin recognition complex subunit 4
- Origin recognition complex subunit 6
- Origin recognition complex subunit 2
- DNA replication licensing factor MCM7
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM2
- DNA replication licensing factor MCM6
- DNA replication licensing factor MCM5
Sequence:
MNSGAMRIHSKGHFQGGIQVKNEKNRPSLKSLKTDNRPEKSKCKPLWGKVFYLDLPSVTISEKLQKDIKDLGGRVEEFLSKDISYLISNKKEAKFAQTLGRISPVPSPESAYTAETTSPHPSHDGSSFKSPDTVCLSRGKLLVEKAIKDHDFIPSNSILSNALSWGVKILHIDDIRYYIEQKKKELYLLKKSSTSVRDGGKRVGSGAQKTRTGRLKKPFVKVEDMSQLYRPFYLQLTNMPFINYSIQKPCSPFDVDKPSSMQKQTQVKLRIQTDGDKYGGTSIQLQLKEKKKKGYCECCLQKYEDLETHLLSEQHRNFAQSNQYQVVDDIVSKLVFDFVEYEKDTPKKKRIKYSVGSLSPVSASVLKKTEQKEKVELQHISQKDCQEDDTTVKEQNFLYKETQETEKKLLFISEPIPHPSNELRGLNEKMSNKCSMLSTAEDDIRQNFTQLPLHKNKQECILDISEHTLSENDLEELRVDHYKCNIQASVHVSDFSTDNSGSQPKQKSDTVLFPAKDLKEKDLHSIFTHDSGLITINSSQEHLTVQAKAPFHTPPEEPNECDFKNMDSLPSGKIHRKVKIILGRNRKENLEPNAEFDKRTEFITQEENRICSSPVQSLLDLFQTSEEKSEFLGFTSYTEKSGICNVLDIWEEENSDNLLTAFFSSPSTSTFTGF
Protein: F-box and leucine-rich repeat protein 17 (H7C835)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVCKRKGAGVPACTPCKQPLCPPPSSPTSEGAPTEAGGDAVRAGGTAPLSAQQQHECGDADCRESPENPCDCHREPPPETPDINQLPPSILLKIFSNLSLDERCLSASLVCKYWRDLCLDFQFWKQLDLSSRQQVTDELLEKIASRSQNIIEINISDCRSMSDNGVCVLAFKCPGLLRYTAYRCKQLSDTSIIAVASHCPLLQKVHVGNQDKLTDEGLKQLGSKCRELKDIHFGQCYKISDEGMIVIAKGCLKLQRIYMQENKLVTDQSVKAFAEHCPELQYVGFMGCSVTSKGVIHLTKLRNLSSLDLRHITELDNETVMEIVKRCKNLSSLNLCLNWIINDRCVEVIAKEGQNLKELYLVSCKITDYALIAIGRYSMTIETVDVGWCKEITDQGATLIAQSSKSLRYLGLMRCDKVNEVTVEQLVQQYPHITFSTVLQDCKRTLERAYQMGWTPNMSAASS