wanglab/gogpt-training-data huggingface dataset:
Protein: Chaperone CupA5 (Q9I1Y3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
Interaction partners:
- Usher CupA3
- Fimbrial subunit CupA1
- Fimbrial subunit CupA4
- Usher CupC3
- Usher CupB3
- Chaperone CupA2
- EAL domain-containing protein
- Fimbrial-type adhesion domain-containing protein
- Probable fimbrial subunit CupB1
Sequence:
MSSRRALALLAMLCLAPTSEAGVTAERTRLVFVEGQREASLLLVNQNPYPVLVQAWVDDGALDGEPDTALAPFLPLPPVFRLEPGRQRSLRLLATGQAQARDRESLYWLNIYEIPPQATAEAAGRPRLTVTLRTQMKVLYRPHGLHPHAEDAAAELGFALRDETLRVDNPTPYFVSLAGLALEIGETRLDLPGTLLAPRSQRRLGLPRRVDGGTRGEVAFDWIDDNGVSRQERKALQ
Protein: Protein SLF1 (Q12034)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates the copper-dependent mineralization of copper sulfide complexes on the cell surface in cells cultured in medium containing copper salts.
Interaction partners:
- RNA-binding protein SRO9
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic translation initiation factor 4E
- RNA polymerase II degradation factor 1
- mRNA-binding protein PUF3
- Probable ATP-dependent RNA helicase DHR1
- KRR1 small subunit processome component
- Small ribosomal subunit protein uS3
Sequence:
MSSQNLNDNPKNTSSAAEDKKKQTSSLKLAPIPTTSPWKSSSPDSNTVIPVEELRDISKTAKPSKNGSGSIKLTSNTKWTPITPSVIISGSKDTNSKSGKNSKNSKTNKKMKKRGKYNNDINKKDFNGQTNSTSEISNVSNLESKPLDANAKVNIHSSSGATANGNIKRITNNNNSTNGRQSRNYQNRNGKTRYNNNSRHSQAANNAISFPNNYQARPEYIPNASHWLNNNSRNSYKQLSYFRQQQYYNNINYQQQLQTPYYYSMEPIFKSIESIKNQIEFYFSEENLKTDEFLRSKFKKANDGFIPMSLIGKFYRMVNLSLGGDPNLILASMREVLQHKETNHLEIALGSIEGAQKNMADDFNPLENYFIRRENWAEYAMESNFDENDDETEKYNIEKLLGPNDLDNYSYMGYPNFFPSNENGKKSQSYDQGEISRQFEQNLQIND
Protein: Thioredoxin-like protein 1 (32 kDa thioredoxin-related protein) (O43396)
Organism: Homo sapiens (Human)
Function: Active thioredoxin with a redox potential of about -250 mV.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19349277}. Nucleus {ECO:0000269|PubMed:19349277}. Note=At least 85% of the cellular TXNL1 is proteasome-associated.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 4
- Tumor protein p53-inducible protein 11
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- DAZ associated protein 2.
- COP9 signalosome complex subunit 5
- Thioredoxin domain-containing protein 17
- 26S proteasome regulatory subunit 6A
- 26S proteasome regulatory subunit 4
- demerged
Sequence:
MVGVKPVGSDPDFQPELSGAGSRLAVVKFTMRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFLFFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFINKAGCECLNESDEHGFDNCLRKDTTFLESDCDEQLLITVAFNQPVKLYSMKFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGIVPLRYVKFQNVNSVTIFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKRVVGKKGESH
Protein: Relaxin receptor 2 (G-protein coupled receptor 106) (G-protein coupled receptor affecting testicular descent) (Leucine-rich repeat-containing G-protein coupled receptor 8) (Relaxin family peptide receptor 2) (Q8WXD0)
Organism: Homo sapiens (Human)
Function: Receptor for relaxin. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. May also be a receptor for Leydig insulin-like peptide (INSL3).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Insulin-like 3
- Prorelaxin H2
- Prorelaxin H1
- Relaxin-3 receptor 1
- Relaxin-3 receptor 2
- Relaxin-3
- Relaxin receptor 1
- Insulin-like peptide INSL5
- Guanine nucleotide-binding protein G
- Insulin
Sequence:
MIVFLVFKHLFSLRLITMFFLLHFIVLINVKDFALTQGSMITPSCQKGYFPCGNLTKCLPRAFHCDGKDDCGNGADEENCGDTSGWATIFGTVHGNANSVALTQECFLKQYPQCCDCKETELECVNGDLKSVPMISNNVTLLSLKKNKIHSLPDKVFIKYTKLKKIFLQHNCIRHISRKAFFGLCNLQILYLNHNCITTLRPGIFKDLHQLTWLILDDNPITRISQRLFTGLNSLFFLSMVNNYLEALPKQMCAQMPQLNWVDLEGNRIKYLTNSTFLSCDSLTVLFLPRNQIGFVPEKTFSSLKNLGELDLSSNTITELSPHLFKDLKLLQKLNLSSNPLMYLHKNQFESLKQLQSLDLERIEIPNINTRMFQPMKNLSHIYFKNFRYCSYAPHVRICMPLTDGISSFEDLLANNILRIFVWVIAFITCFGNLFVIGMRSFIKAENTTHAMSIKILCCADCLMGVYLFFVGIFDIKYRGQYQKYALLWMESVQCRLMGFLAMLSTEVSVLLLTYLTLEKFLVIVFPFSNIRPGKRQTSVILICIWMAGFLIAVIPFWNKDYFGNFYGKNGVCFPLYYDQTEDIGSKGYSLGIFLGVNLLAFLIIVFSYITMFCSIQKTALQTTEVRNCFGREVAVANRFFFIVFSDAICWIPVFVVKILSLFRVEIPDTMTSWIVIFFLPVNSALNPILYTLTTNFFKDKLKQLLHKHQRKSIFKIKKKSLSTSIVWIEDSSSLKLGVLNKITLGDSIMKPVS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q75Y03)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSNTSSCSSSGETSPDDTPRGGGTIRVYLPNKQRTVVNVRPGQTVYDSLDKALKVRGLSQDCCAVFRLLEGRKRLTEWDTDITPLVGEELLVEVLDDVPLTMHNFVRKTFFKLAYCDFCHKFLFNGFRCQTCGYKFHQHCSSKVPTVCVDMDTMTKRCVNNTEDCPAILIYPATNSISQSDLPLTSDSPGGELPSSPSNFCLFIRGEDGQSLQRHRSTSTPNVHMVSTLEPGAAGLLEEPFKISTVASYTGYESSPKPSTSPPHLGSPGRKPPKSPSEPKERKQSSSDDKKKVHRGGYRDSSYYWEVHPREVSMLKRIGAGSFGTVFKGKWHGDVAIKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGSSLYRHLHVTETKFDTMRRIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGWTVKIGDFGLATVKSRWSGSQQVEQPSGSILWMAPEVIRMQDTNPYTFQSDVYGYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPDLSKLYSNCPKSMKRLIIDCLKFKRDERPLFPQILVSIEQVQELLPKIERSASEPSLHRAVHAEDLNPLLLHTTRFL
Protein: Beta-arrestin-1 (Arrestin beta-1) (Q5XJ55)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cell projection, pseudopodium {ECO:0000256|ARBA:ARBA00037818}. Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Membrane, clathrin-coated pit {ECO:0000256|ARBA:ARBA00004600}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGDKGTRVFKKASPNGKLTVYLGKRDFVDHVDLVEPVDGVVLIDPEYLKERKVFVTLTCAFRYGREDLDVLGLTFRKDLFVANIQAFPPVPEEKKSLTRLQERLIKKLGEHAYPFTFEIPPNLPCSVTLQPGPEDTGKACGVDFEVKAFCAEKKKKK
Protein: Putative esterase F42H10.6 (EC 3.1.2.-) (P34419)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MVGHSESSTDAVIEPTSEELLAEQVRVFNKMKGSTNFNRVAEDVYPVEVTKSKLVCEMVVQHQHLNSKGTLHGGQTATLTDVITARAVGVTVKDKGMASVELAVSYLLPVKVGDVLEITAHVLKVGRTMAFTDCEFRRKSDGKMSAKGKHTLAFLPNQPGISVENGTQF
Protein: Phosphate-regulating neutral endopeptidase PHEX (Metalloendopeptidase homolog PEX) (EC 3.4.24.-) (Phosphate regulating neutral endopeptidase) (Vitamin D-resistant hypophosphatemic rickets protein) (X-linked hypophosphatemia protein) (HYP) (P70669)
Organism: Mus musculus (Mouse)
Function: Peptidase that cleaves SIBLING (small integrin-binding ligand, N-linked glycoprotein)-derived ASARM peptides, thus regulating their biological activity (By similarity). Cleaves ASARM peptides between Ser and Glu or Asp residues (By similarity). Regulates osteogenic cell differentiation and bone mineralization through the cleavage of the MEPE-derived ASARM peptide. Promotes dentin mineralization and renal phosphate reabsorption by cleaving DMP1- and MEPE-derived ASARM peptides. Inhibits the cleavage of MEPE by CTSB/cathepsin B thus preventing MEPE degradation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11811562}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Fibroblast growth factor 23
- Matrix extracellular phosphoglycoprotein
- Dentin matrix acidic phosphoprotein 1
- Parathyroid hormone
- Sodium-dependent phosphate transport protein 2C
- Sodium-dependent phosphate transport protein 2A
- Sclerostin
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Klotho
- Polypeptide N-acetylgalactosaminyltransferase 3
Sequence:
MEAETGSTMETGKGTNRGIRIALALFIGGTLVLGTLLFLVSQGLLSFQAKQEYCLKPECIEAAAAIMSKVNLSVDPCENFFRFACDGWISNNPIPEDMPSYGVYPWLRHNVDLKLKALLEKSVSRRRDTEAVQKAKILYSSCMNEKAIEKADAKPLLHILRHSPFRWPVLEANIGPEGVWSERKFSLLQTLATFRGQYSNSVFIRLYVSPDDKASNEHILKLDQATLSLAVREDFLDNTTEAKSYRDALYKFMVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIPHENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDTRLYPHLKDIGPSENVVVRVPQYFKDLFRILGAERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIESALPYVVGKMFVNVHFQEDKKEMMEELIEGVRWAFIDMLEKENEWMDAGTKRKAQEKARAVLAKVGYPEFIMNDTYVNEDLKAIKFSESDYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFWGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSVESEEKFKEKTKCMINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKWINDRRQGVEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPRNSTMNRGADSCRLW
Protein: APC-like, isoform A (APC-like, isoform B) (Q9VAS9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Armadillo segment polarity protein
- Axin
- Adenomatous polyposis coli 2
- Segment polarity protein dishevelled
- Protein kinase shaggy
- F-box-like/WD repeat-containing protein ebi
- GEO01805p1
- LP10147p
- GEO10396p1
- CG11942
Sequence:
MLEPTLTPDLEEGIAELSLEDVDVDSVPERKPHFLDYDAVPPPDYEEGFGASSGEQLKMDKKYERDGEVSDYELAASGYTKKEFTQDDNTLHFTQSAVGLGSGAVGKKPAAKHFLDENPIPPDYMLAQELREMREHRSLDRNFERQSAQQQQLDELPPRNGGGSPASAGRPSRSKEPSYTLSRFLDGDAPAPAPRLPKGAAWTTSFDERYTSSAVEATLGSKVECVYSLLSMLGSNDPLEMAKKFLELSGNAQSCATLRRSGCMPLLVQMMHAPDNDQEVRKCAGQALHNVVHSHPDEKAGRREAKVLRLLDQIVDYCSFLKTLLQSGGEAIADDSDRHPLAAISSLMKVSFDEEHRHAMCELGALHAIPNLVHLDHAVHGPKPEDQCCNSLRRYALMALTNLTFGDENNKALLCGQKQFMEALVAQLDSAPDDLLQVTASVLRNLSWRADSNMKAVLNEIGTVTALALAAMRNRSENTLKAILSALWNLSAHCSTNKAEFCAVDGALAFLVGMLSYEGPSKTLKIIENAGGILRNVSSHIAVCEPYRQILRQHNCLAILLQQLKSESLTVVSNSCGTLWNLSARSAEDQKFLWDNGAVPMLRSLIHSKHAMISEGSSSALKNLLNFRPAVQNHHQLDPIARSMGLKALPTLEARKAKALQQELGERHTAETCDNLDTGGKLDKERASSSSRRHPAPRLTRSAMLTKSESRDSVYSAKSDCAYDHLIRSASASDAHRKVKPKITDFDLEMEQDTEATEEQPIDYSVKYSENATKTSTYQETDLDQPTDFSLRYAENQIESDLDISGPAGGQKSTITPPAETVPEKSEGQEILLILDDSVKCYQTEDTPYVISNAASVTDLRVAAKADAEAEVKPEVREVTSKEGAPKKLPKLSQCGSGSYTPEKPINYCEEGTPGYFSRYDSLSSLDESGKANQAIVGTDADIKPKLEKQEEQESQPAEQVLTKPPTQANSALETPLMFSRRSSMDSLVHDPDVDVANCDDKSSVVSDFSRLASGVISPSEIPDSPTQSMPQSPRRNSVAGSGQNVDSPPVVIPASLQPLRSVFEDDLSSFNVEHTPAQFSTATSLSNLSIVDDEKAPASVAEEDNEDELLLANCINMGMQRKPTEAVKSTVVNSEVDVAEETIRSYCTEDTPALLSKVPSNTNLSVISMSSTDPKDATAGQAQMYAHQLSDDVSSNASDCGGASGHLLQQCIRDGMKKPLGEATSDPIAMLRRGGNELPGYLPSADEMNKFLVEDSPCNFSVVSGLSNLTVGSSLVGPAVQLKETEPSSADQNPEMKAKPGKQEQVRRPPHWQDDSLSSLSIDSEDDTNLLSQAIAAGCNRPKSNLGFSSNGKRSSSLSSSQPIAINAATSASSLNSAMTVRKSQQQESYSSVDSSDSNDNQSKSLFELCILKGMYKTKEPGARAQQMQEQPIVGSSSVQSNPSLKQFDSLPVQLPSSGQVKRQRHHHHHHHHRERERERKDEKLLQECINTGISKKINAVPKNVLATSAAALEPCHPMAATTSASALSTAAPDVEQKAHATSNPQQQSSTHPSSHILPNPIDAIATVTDTVRSPAAPNQGNGNASQNGLETATGSKDLDSEDRSSDESNQSFIMETMVRLDSALNETCISGASEKHKDPDLMLKSVERLTMEFVTSAEQLRSSSHNHSSSNSHKNNSSNNTWNESTCPNDVSFPSVSQTAPVLASLSLDEDATEARSLHELIEITPTNEQQPESLEGETDTLVNGHADSYSGSSGGLNFQLGGQVQNAGVRLEPQRLLFNGTSASIMTNSTMIAFEARALAENLLQPAATDDDTTEMTFSLNSLDLDNIRPPSGMESLNSCYQDHSQPSSLRQAMPSKSPRFARKMFPANLVARRALGHLAGSAESVNSSCNLLDNIKPPSLMDELLDSMISVDSIQSEVADGEQDCSMATTISVSNYETAACDDQTMTVLQSCFDEDEDATMNDYSSAESTPKHGSTPSPNRRSLTPKDKRRLTKDRFKTYTIATSCEMEAPEANETLQIEIVEAAVPVATPSPRANGRRRGSAERYKTQLIECPLALIQPQPDDCPSEQLSSIRAMMQQFTFITDINIGHSQETCESTDHPEDAGESPECDQNSETESCDGQEPDQLPPPPSIVDLRTSVVKPTTLEPATAVKLVRGRKKPAYVSPYSMQSQRNSNNAAPSKKKTLSPTIAKRSLVPGGSGVRLPAKKKPTPPPEPAPARLERQGTFVKDEPTNSNVQVPVVETKPAQTSPTHRASKLPTKKGTASGGSPSKAGSPKRIPLAPARRMTPQRANTSLRLAAGKSHAASRVVSGRVSSTTPPSRSNSNLNGSSAAAAAAAKINHAQSRIANIWKRVDEAKTKQSSSNLRTQKTKSSNMLNANGTKPTLLRSSTFDNTPSTAGGVKSKLPVVGARK
Protein: Glucoside xylosyltransferase 2 (EC 2.4.2.42) (Glycosyltransferase 8 domain-containing protein 4) (A0PJZ3)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucose:glycoprotein glucosyltransferase 1
- Glucoside xylosyltransferase 1
- Xyloside xylosyltransferase 1
- Coagulation factor VII
- Protein O-glucosyltransferase 1
Sequence:
MKLRSKAAALLLLALAALLLALLSLRAGRAEPPALPARPASAPQRHPAPVPARWPGPGALPGASPGVRRRRPPRPRPRAGRRGAARLEKLARRPGEPRSFQAVLPPELWIHLAVVACGNRLEETLVMLKSAVLFSHRKIQFHIFTEDSLKPEFDKQLRQWPDSYTKKFEHRIYPITFSVGNPQEWKKLFKPCAAQRLFLPVILKDVDSLLYVDTDVLFLRPVDDIWKLLRLFNSTQLAAMAPEHEIPKIGWYSRFARHPFYGSAGVNSGVMLMNLTRIRSTQFKNSMIPTGLAWEDMLYPLYQKYKNAITWGDQDLLNIIFYFNPECLYVFPCQWNYRPDHCMYGSNCREAEHEGVSVLHGNRGVYHDDKQPTFRALYEAIRDFPFQDNLFQSMYYPLQLKFLETVHTLCGRIPQVFLKQIEKTMKRAYEKHVIIHVGPNQMH
Protein: Blood group Rh(CE) polypeptide (Rh polypeptide 1) (RhPI) (Rh30A) (RhIXB) (Rhesus C/E antigens) (CD antigen CD240CE) (P18577)
Organism: Homo sapiens (Human)
Function: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Ammonium transporter Rh type A
- Glycophorin-B
- Glycophorin-A
- Transmembrane protein 50A
- Leukocyte surface antigen CD47
- Ankyrin-1
- Band 3 anion transport protein
- Delta
- Protein 4.2
- Protein phosphatase 1 regulatory subunit 3A
Sequence:
MSSKYPRSVRRCLPLCALTLEAALILLFYFFTHYDASLEDQKGLVASYQVGQDLTVMAALGLGFLTSNFRRHSWSSVAFNLFMLALGVQWAILLDGFLSQFPPGKVVITLFSIRLATMSAMSVLISAGAVLGKVNLAQLVVMVLVEVTALGTLRMVISNIFNTDYHMNLRHFYVFAAYFGLTVAWCLPKPLPKGTEDNDQRATIPSLSAMLGALFLWMFWPSVNSALLRSPIQRKNAMFNTYYALAVSVVTAISGSSLAHPQRKISMTYVHSAVLAGGVAVGTSCHLIPSPWLAMVLGLVAGLISIGGAKCLPVCCNRVLGIHHISVMHSIFSLLGLLGEITYIVLLVLHTVWNGNGMIGFQVLLSIGELSLAIVIALTSGLLTGLLLNLKIWKAPHVAKYFDDQVFWKFPHLAVGF
Protein: Branched-chain amino acid ABC transporter, ATP-binding protein (Q5LNB7)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Interaction partners:
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- AMP-binding enzyme
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, permease protein
- Branched-chain amino acid ABC transporter, periplasmic branched-chain amino acid binding protein, putative
- Branched-chain amino acid ABC transporter, permease protein
- Phenylacetate-CoA ligase, putative
Sequence:
MGASPRPPSRQPGHCRKTRETPMLDASEGYTTADGRKIGGVVMEMKNITLRFGGVVAIKDISFDIREGEIRAIIGPNGAGKSSMLNVISGFYVPQEGEVWFHGKKRPGMRPYEVARQGIARTFQNIALFEGMSVLDNVMTGRLNYMKTGLLSQAIWKGKAEREEVENREAVEKIIDFLEIQHIRKTPVSRLPYGLKKRVELARALAAEPKLLLLDEPMAGMNVEEKEDMSRFILDVNDEFGTTIALIEHDMGVVMDLSDRVVVMDYGKKIGDGTPEEVRNNQEVIDAYLGVAHD
Protein: Bromodomain-containing protein 2 (Q1LWX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METALSPPFDSSLGGCDGMQGLTMMEQTISGPGKRIRKPSLLYEGFEGPALPHIAQSGPPQPAVRDPSRQGRMTNQLQFLQKALVKTLWRHHFAWPFHEPVDAAKLNLPDYYNIIKQPMDMGTIKKRLENNYYRSASECMQDFNTMFTNCYIYNKPTDDIVLMAQSLEKAFLQKVAQMPEVEEEIPAPVPRGKQSKPKKGQKLFSGGITTAHQVPAISSLSQLAYSPPTPDTPDSVLSTPPQTLITKNFPPPPLHSTPALLGLPPTQPTAKKKGVKRKADTTTPTTTVMPLTLGVGGMGMGMGMGMSMGMGMGMGLGGDSPLTLSNMGMDSKQSLSLSLGMSLEDKVPARRGGSGRPIKPPRKDLPDSQNQHQPVRRGKLSQQLRYCSTILKELLSKKHTAYAWPFYKPVDVSSLGLHDYYDIIMYPMDLSTIKRKMDHREYRDALQFAADVRLMFSNCYKYNPPDHDVVAMARRLQDVFEFRFAKMPDEPLESLPPASLGGGLGGDSSSSSSSSSSSSESDVSSESESESSPSSDSEEERAHRLAQLQEQLRAVHEQLAALSSTPIIKPKKKKEKKDKKKKKKPEKHKRSRSVIEDEVVMRPAKIPKLPKTPKSRSNSKAATSTQSKKSSNKKSNKSKSSKKAQPTFFPPPLSHSGLTPHYDSEEEEETSPMSYDEKRQLSLDINRLPGEKLGRVVHIIQSREPSLRDTNPEEIEIDFETLKPSTLRELERYVMMCLRKKPRKPFVAIKGSAGKSREELALEKKRELERRLQDVSGQLNSVKKPQKTKAEKPSAVEPHAVASRLSASSSSSDSSSSSSSSSSSDTSESDSD
Protein: Protection of telomeres homolog 2 (O45595)
Organism: Caenorhabditis elegans
Function: Telomeric DNA-binding protein, which binds to two or more single-stranded G-rich repeat sequences (G-strand), with high specificity to the 5'-TTAGGC-3' sequence. In addition, repeat sequence binding requires a 3' single-stranded telomeric overhang. Acts redundantly with pot-1 to negatively regulate telomerase-mediated telomere extension. Also regulates telomere length by the telomerase-independent telomere maintenance pathway called ALT (alternative lengthening of telomeres). Does not appear to have a role in anchoring telomeres to the nuclear envelope.
Subcellular location: Nucleus {ECO:0000305|PubMed:18329362, ECO:0000305|PubMed:23390606}. Chromosome, telomere {ECO:0000305|PubMed:18329362, ECO:0000305|PubMed:23390606}.
Interaction partners:
- Protection of telomeres homolog 1
- Telomerase reverse transcriptase
- Double-strand telomeric DNA-binding proteins 2
- Double-strand telomeric DNA-binding proteins 1
- Ku domain-containing protein
- CDK5RAP1-like protein
- ATP-dependent DNA helicase II subunit 2
- Cell cycle checkpoint protein RAD1 homolog mrt-2
- Homolog of S. Pombe Rad
Sequence:
MSSFDRRIEAACKFDDERYYKQYHRYFDVLAQVHSVVETINGAQMLRVWRGRKFGPGASAERRERRLFHVTQDSFKRYIVPPNPRIGKAIEENGKELLIEIDVYDDHRDGLKNLNSGDFVAIQNVHAASTRQTEMQVLHGGGASYQRGITTVPVDFEHEAFQNFKKKVEAVLETVAYDENFTEFQQPEEVAENHVDEEPQEEALPRGVVLRTETCDFMDMELDNWPEGPPKTFAEAIARANNSRRPRDPPQ
Protein: Zgc:77366 (Q6NYB0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTAQMENQLCKLFVGGLNVQTTDDGLRNHFEQYGKLTDCVVVQNQQLKRSRCFGFVTYSSPDEADSAMSARPHILDGNNVELKRAVAREDAGKPEALAKVKKIFIGGLKDDIEEDHLRDCFSQFGAVEKAEVITDKETGKKRGFGFVYFEDNDSADKAVVLKFHMINGHKVEVKKALTKQEMQAAGSRGGGRGGRGGGRGMGRPQNGYGGRGGGYGNYGGGGYGGNDGYGGGYGGGYGGGYGGGYGDQMEGYGGGNGYNDFGSGYGQQSSGYGPMKGNYSGRSNAPYSRGGGGGGYGRGGYGGSY
Protein: Preproghrelin-2 (Q4LET8)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MLGHGRVGHMMLLLCAFSLWAETVMCGSSFLSPTQKPQNRGDRKPPRVGRRTAAELEAPLPSEENIMVSAPFQLAVSLSDAEYEDYGPVLQRMLLDVLGDPPTLDGAN
Protein: Product of latency-related protein (Q77CA8)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Interaction partners:
Sequence:
MRDLGHKSPAHARAVTFGLGMTAATAARKLSMQAGGRKYTAVRCGGLRVAEWVGGEPAAAIIAARRCRRCSGRAARPGSGPGDRLAAAPGPRCCGGGSPGGFLAPRRPLPFRCAASSAPSSRGRGPGRPAPWRSLAFSPGRGCHCGRPRPGRLRPGPERRPAGGRRQGRGRRETGSGLGWK
Protein: Eukaryotic translation initiation factor 4E-binding protein 3-like (4E-BP3) (eIF4E-binding protein 3) (Eukaryotic translation initiation factor 4E-1A-binding protein) (4E-BP) (eIF4E-1A-binding protein) (Q98TT6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Regulates eif4e1a activity by preventing its assembly into the eIF4F complex.
Interaction partners:
- Eukaryotic translation initiation factor 4E-1B
- Eukaryotic translation initiation factor 4E-1A
- Neuroguidin
- Eukaryotic translation initiation factor 4eb
- Eukaryotic translation initiation factor 4E type 2
Sequence:
MSTNTQQSKSCPIPTRVLHLKDWSQLPDCYSQTPGGTLFSTTPGGTRIIYDRKFLLDCRNSPIARTPPCCLPQIPGVTIPSLHPVSKLQELKEELEEEKELAADDSQFEMDI
Protein: Enkurin domain-containing protein 1 (Q9H0I2)
Organism: Homo sapiens (Human)
Function: Microtubule-binding protein which regulates microtubule organization and stability. Promotes the stability of astral microtubules and facilitates the proper orientation of the mitotic spindle. This allows the oriented division of basal keratinocytes and contributes to epidermal stratification (By similarity). Required for the assembly of both primary and motile cilia. Destabilizes the interaction between CCP110 and CEP97 by competing with CEP97 for binding to CCP110 which promotes the removal of CCP110 and CEP97 from the mother centriole and allows the initiation of ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:35072334, ECO:0000269|PubMed:35301795}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:35301795}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:35301795}. Cell projection, cilium {ECO:0000269|PubMed:35072334}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:35072334}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:35072334}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:35072334}. Note=Localized at the centrosome and accumulates at the parental centrioles during centriole duplication in cycling cells (PubMed:35301795). In ciliated cells, detected at the basal body of the cilium (PubMed:35301795). Localizes to the centrosome during interphase, to the primary cilium at G0, to the spindle poles during mitosis and to the centrosomes and central spindle during telophase and cytokinesis (PubMed:35072334). {ECO:0000269|PubMed:35072334, ECO:0000269|PubMed:35301795}.
Interaction partners:
- Glucose-fructose oxidoreductase domain-containing protein 2
Sequence:
MCEGPSRISGPIPPDPTLCPDNYRRPTSAQGRLEGNALKLDLLTSDRALDTTAPRGPCIGPGAGEILERGQRGVGDVLLQLEGISLGPGASLKRKDPKDHEKENLRRIREIQKRFREQERSREQGQPRPLKALWRSPKYDKVESRVKAQLQEPGPASGTESAHFLRAHSRCGPGLPPPHVSSPQPTPPGPEAKEPGLGVDFIRHNARAAKRAPRRHSCSLQVLAQVLEQQRQAQEHYNATQKGHVPHYLLERRDLWRREAEARKQSQPDPAMPPGHTRMPENQRLETLTKLLQSQSQLLRELVLLPAGADSLRAQSHRAELDRKLVQVEEAIKIFSRPKVFVKMDD
Protein: Calcineurin-binding protein cabin-1 (Calcineurin inhibitor) (CAIN) (Q9Y6J0)
Organism: Homo sapiens (Human)
Function: May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:9655484}.
Interaction partners:
- Protein HIRA
- Ubinuclein-1
- Histone chaperone ASF1A
- Myocyte-specific enhancer factor 2B
- Myocyte-specific enhancer factor 2D
- Ubinuclein-2
- Calmodulin-like protein 5
- Histone chaperone ASF1B
- Calmodulin-1
- Calmodulin-like protein 4
Sequence:
MIRIAALNASSTIEDDHEGSFKSHKTQTKEAQEAEAFALYHKALDLQKHDRFEESAKAYHELLEASLLREAVSSGDEKEGLKHPGLILKYSTYKNLAQLAAQREDLETAMEFYLEAVMLDSTDVNLWYKIGHVALRLIRIPLARHAFEEGLRCNPDHWPCLDNLITVLYTLSDYTTCLYFICKALEKDCRYSKGLVLKEKIFEEQPCLRKDSLRMFLKCDMSIHDVSVSAAETQAIVDEALGLRKKRQALIVREKEPDLKLVQPIPFFTWKCLGESLLAMYNHLTTCEPPRPSLGKRIDLSDYQDPSQPLESSMVVTPVNVIQPSTVSTNPAVAVAEPVVSYTSVATTSFPLHSPGLLETGAPVGDISGGDKSKKGVKRKKISEESGETAKRRSARVRNTKCKKEEKVDFQELLMKFLPSRLRKLDPEEEDDSFNNYEVQSEAKLESFPSIGPQRLSFDSATFMESEKQDVHEFLLENLTNGGILELMMRYLKAMGHKFLVRWPPGLAEVVLSVYHSWRRHSTSLPNPLLRDCSNKHIKDMMLMSLSCMELQLDQWLLTKGRSSAVSPRNCPAGMVNGRFGPDFPGTHCLGDLLQLSFASSQRDLFEDGWLEFVVRVYWLKARFLALQGDMEQALENYDICTEMLQSSTAIQVEAGAERRDIVIRLPNLHNDSVVSLEEIDKNLKSLERCQSLEEIQRLYEAGDYKAVVHLLRPTLCTSGFDRAKHLEFMTSIPERPAQLLLLQDSLLRLKDYRQCFECSDVALNEAVQQMVNSGEAAAKEEWVATVTQLLMGIEQALSADSSGSILKVSSSTTGLVRLTNNLIQVIDCSMAVQEEAKEPHVSSVLPWIILHRIIWQEEDTFHSLCHQQQLQNPAEEGMSETPMLPSSLMLLNTAHEYLGRRSWCCNSDGALLRFYVRVLQKELAASTSEDTHPYKEELETALEQCFYCLYSFPSKKSKARYLEEHSAQQVDLIWEDALFMFEYFKPKTLPEFDSYKTSTVSADLANLLKRIATIVPRTERPALSLDKVSAYIEGTSTEVPCLPEGADPSPPVVNELYYLLADYHFKNKEQSKAIKFYMHDICICPNRFDSWAGMALARASRIQDKLNSNELKSDGPIWKHATPVLNCFRRALEIDSSNLSLWIEYGTMSYALHSFASRQLKQWRGELPPELVQQMEGRRDSMLETAKHCFTSAARCEGDGDEEEWLIHYMLGKVAEKQQQPPTVYLLHYRQAGHYLHEEAARYPKKIHYHNPPELAMEALEVYFRLHASILKLLGKPDSGVGAEVLVNFMKEAAEGPFARGEEKNTPKASEKEKACLVDEDSHSSAGTLPGPGASLPSSSGPGLTSPPYTATPIDHDYVKCKKPHQQATPDDRSQDSTAVALSDSSSTQDFFNEPTSLLEGSRKSYTEKRLPILSSQAGATGKDLQGATEERGKNEESLESTEGFRAAEQGVQKPAAETPASACIPGKPSASTPTLWDGKKRGDLPGEPVAFPQGLPAGAEEQRQFLTEQCIASFRLCLSRFPQHYKSLYRLAFLYTYSKTHRNLQWARDVLLGSSIPWQQLQHMPAQGLFCERNKTNFFNGIWRIPVDEIDRPGSFAWHMNRSIVLLLKVLAQLRDHSTLLKVSSMLQRTPDQGKKYLRDADRQVLAQRAFILTVKVLEDTLSELAEGSERPGPKVCGLPGARMTTDVSHKASPEDGQEGLPQPKKPPLADGSGPGPEPGGKVGLLNHRPVAMDAGDSADQSGERKDKESPRAGPTEPMDTSEATVCHSDLERTPPLLPGRPARDRGPESRPTELSLEELSISARQQPTPLTPAQPAPAPAPATTTGTRAGGHPEEPLSRLSRKRKLLEDTESGKTLLLDAYRVWQQGQKGVAYDLGRVERIMSETYMLIKQVDEEAALEQAVKFCQVHLGAAAQRQASGDTPTTPKHPKDSRENFFPVTVVPTAPDPVPADSVQRPSDAHTKPRPALAAATTIITCPPSASASTLDQSKDPGPPRPHRPEATPSMASLGPEGEELARVAEGTSFPPQEPRHSPQVKMAPTSSPAEPHCWPAEAALGTGAEPTCSQEGKLRPEPRRDGEAQEAASETQPLSSPPTAASSKAPSSGSAQPPEGHPGKPEPSRAKSRPLPNMPKLVIPSAATKFPPEITVTPPTPTLLSPKGSISEETKQKLKSAILSAQSAANVRKESLCQPALEVLETSSQESSLESETDEDDDYMDI