wanglab/gogpt-training-data huggingface dataset:
Protein: Cytoskeleton-associated protein 2 (CTCL tumor antigen se20-10) (Tumor- and microtubule-associated protein) (Q8WWK9)
Organism: Homo sapiens (Human)
Function: Possesses microtubule stabilizing properties. Involved in regulating aneuploidy, cell cycling, and cell death in a p53/TP53-dependent manner (By similarity).
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Note=Contrary to the ectopically expressed protein, endogenous CKAP2 does not colocalize with microtubules in G1, S and early G2. At late G2 and prophase after separation of duplicated centrosomes, colocalizes with gamma-tubulin and centrosome-proximal microtubules. From prometaphase through anaphase B, colocalizes with mitotic spindle poles and spindle microtubules. During cytokinesis, absent from midbody microtubules.
Interaction partners:
- Centromere protein F
- DNA topoisomerase 2-alpha
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Abnormal spindle-like microcephaly-associated protein
- Dual specificity protein kinase TTK
- Kinesin-like protein KIF20A
- Centrosomal protein of 55 kDa
- Cyclin-dependent kinase 1
- Disks large-associated protein 5
Sequence:
MSTPAVPQDLQLPPSQRAQSAFKEQRRQKLKEHLLRRKTLFAYKQENEMLSSSRDQRVVTSEDQVQEGTKVLKLKTKMADKENMKRPAESKNNTVVGKHCIPLKPSNELTNSTVVIDTHKPKDSNQTPHLLLTEDDPQSQHMTLSQAFHLKNNSKKKQMTTEKQKQDANMPKKPVLGSYRGQIVQSKINSFRKPLQVKDESSAATKKLSATIPKATKPQPVNTSSVTVKSNRSSNMTATTKFVSTTSQNTQLVRPPIRSHHSNTRDTVKQGISRTSANVTIRKGPHEKELLQSKTALSSVKTSSSQGIIRNKTLSRSIASEVIARPASLSNDKLMEKSEPVDQRRHTAGKAIVDSRSAQPKETSEERKARLSEWKAGKGRVLKRPPNSVVTQHEPAGQNEKPVGSFWTTMAEEDEQRLFTEKVNNTFSECLNLINEGCPKEDILVTLNDLIKNIPDAKKLVKYWICLALIEPITSPIENIIAIYEKAILAGAQPIEEMRHTIVDILTMKSQEKANLGENMEKSCASKEEVKEVSIEDTGVDVDPEKLEMESKLHRNLLFQDCEKEQDNKTKDPTHDVKTPNTETRTSCLIKYNVSTTPYLQSVKKKVQFDGTNSAFKELKFLTPVRRSRRLQEKTSKLPDMLKDHYPCVSSLEQLTELGRETDAFVCRPNAALCRVYYEADTT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9NEI4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGLIGAANGKHHHPHLISPTHTSLPAGICSSDSGISTLSAISPPLSTSTTTASGAGGGVGGSPQLRTSPALSMLGSATATASGVTASSGCGLTAGILGPAASIDLGSSPLSHRNYSNSLKGFSFRRSFDDKIINTPYLSRAPAYTHGIPYPHFHGTQPAATTPHHLHLHHHGNGTAAGSGSGVGSGPGSGSGAGGLYQQPLSLASMTAALPLAPLYGSPLSLPLTSSQSTTKLSYRDDFLQQIGYLPTTRIYSTPTSIVDEDKAQQDFLSLSLSPPLNRRRDMPALRGPFVSLSEPRGTLSTTDEIYPDSSDSSLYVSDEEQEDASQYCRGGYHPVVIGDIFDNRFRVVRKLGWGHFSTVWLCRDLKDEKYVALKVVKSAPHYIETAADEIRLLEAIRDADPMDVKRERIVRLMNHFTVRGVNGMHTCLVFEALGCSLYKLIVKNNYQGLAIAQVRNIIRQVLEGLDYLHSKCSIIHTDIKPENILLVIDNAAAMNQQIDDEINSLRVKGVDFPDSYISSIEKQTKSRAKWPLIEPNGSTNTNTNTSNSTATNSNSSTPLAAVIMSTLDKEDTTTTTSSTLNSNTTSSLASKYSSLLGDSECNGGLGGSANINNRYRTEKKITAKQPTPNSTNSSCPSHNTATIAKSKINSNILSTCTSLTSTNEYCFTNTNTTTASTPSAPPSATPSSAPALASATPPSTCTPSFTQIAPSATAPATSTTCTTSAEFYDGDHKTTSTSTTTTSNAISSATTTTATTTTAIAKLNVHANAIPSQNQSQSSQNNTYTIQSLIDNSNVRVKIADLGNACYDYHHFTEDIQTRQYRSIEVLLGAPYNYTADIWSTACLAFELATGDYLFDPHAGESYSRDEDHLAHIVELLGSIPQSVIFRGKHGLKYFTSYGSLRNITKLKPWSLMNVLVEKYDWDPVEAKKFSDFLLPMLEYNPVIRASAAECLQHPWLEQEEFV
Protein: NF-kappa-B essential modulator (Inhibitor of nuclear factor kappa B kinase subunit gamma) (DmIKKgamma) (NEMO homolog) (Q9GYV5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential signaling component in transmitting the lipopolysaccharide (LPS) signal leading to cact degradation, which is required for NF-kappa-B (Rel) activation. Required for antibacterial immune response.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Mitogen-activated protein kinase kinase kinase 7
- Nuclear factor NF-kappa-B p110 subunit
- LD40663p
- Fas-associated death domain protein
- Putative mitogen-activated protein kinase kinase kinase 7-like
- FI16976p1
- Protein immune deficiency
- ubiquitinyl hydrolase 1
- GEO06356p1
Sequence:
MSDEESFVILGSSPCSSLMPDSSLRSDVCGNAQEAEETVASTSTQPPTVNCIPVSITASQQQHKSLDSGSSQQQSLATSFIMGEIQSDVLKNSVYSQFPSLCSLQGSAEEVVKLQNMMTEYLALKSTLDKVNQTMLNYHNLTQQWRQEAADREHQYKEHVKECQAQIAILRVENQELKRDLETKIEQIEGVHTIRLKEQDELRKSVSEKQSLIDNMRVEIDKLKQLNHSFEFVPEYATESKSQELIKKMQLDINELKARDIQKQEVIKGLQIQNDIYRRDFEMERADREKNAGEKDQYLMDLRSLQRRNQELIEALAESHKASKACSTASPLSSSRSNLREEQRPILDPTGASSRTSDTTLRCPICSKSFNALSVLQSHVNDCLDKN
Protein: Nuclear speckle splicing regulatory protein 1 (Coiled-coil domain-containing protein 55) (Nuclear speckle-related protein 70) (NSrp70) (Q9H0G5)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that mediates pre-mRNA alternative splicing regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:21296756}. Nucleus speckle {ECO:0000269|PubMed:21296756}. Note=Colocalizes with splicing factors SRSF1 and SRSF2 in speckles.
Interaction partners:
- Cell division cycle 5-like protein
- Beta-catenin-like protein 1
- EF-hand calcium-binding domain-containing protein 5
Sequence:
MAIPGRQYGLILPKKTQQLHPVLQKPSVFGNDSDDDDETSVSESLQREAAKKQAMKQTKLEIQKALAEDATVYEYDSIYDEMQKKKEENNPKLLLGKDRKPKYIHNLLKAVEIRKKEQEKRMEKKIQREREMEKGEFDDKEAFVTSAYKKKLQERAEEEEREKRAAALEACLDVTKQKDLSGFYRHLLNQAVGEEEVPKCSFREARSGIKEEKSRGFSNEVSSKNRIPQEKCILQTDVKVEENPDADSDFDAKSSADDEIEETRVNCRREKVIETPENDFKHHRSQNHSRSPSEERGHSTRHHTKGSRTSRGHEKREDQHQQKQSRDQENHYTDRDYRKERDSHRHREASHRDSHWKRHEQEDKPRARDQRERSDRVWKREKDREKYSQREQERDRQQNDQNRPSEKGEKEEKSKAKEEHMKVRKERYENNDKYRDREKREVGVQSSERNQDRKESSPNSRAKDKFLDQERSNKMRNMAKDKERNQEKPSNSESSLGAKHRLTEEGQEKGKEQERPPEAVSKFAKRNNEETVMSARDRYLARQMARVNAKTYIEKEDD
Protein: Translation initiation factor eIF2B subunit gamma (GCD complex subunit GCD1) (Guanine nucleotide exchange factor subunit GCD1) (eIF2B GDP-GTP exchange factor subunit gamma) (P09032)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as essential component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the synthesis of GCN4 in yeast under amino acid starvation conditions by suppressing the inhibitory effects of multiple AUG codons present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. GCD1 stabilizes the interaction between eIF-2 and GCD6 and stimulates the catalytic activity in vitro.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56288}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit alpha
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit alpha
- Translation initiation factor eIF2B subunit beta
- Eukaryotic translation initiation factor 2 subunit beta
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2 subunit gamma
- Protein DSS4
- Protein LTV1
- GTP-binding protein GTR1
Sequence:
MSIQAFVFCGKGSNLAPFTQPDFPFQTQNKDSTAATSGDKLNELVNSALDSTVINEFMQHSTRLPKALLPIGNRPMIEYVLDWCDQADFKEISVVAPVDEIELIESGLTSFLSLRKQQFELIYKALSNSNHSHHLQDPKKINFIPSKANSTGESLQKELLPRINGDFVILPCDFVTDIPPQVLVDQFRNRDDNNLAMTIYYKNSLDSSIDKKQQQKQKQQQFFTVYSENEDSERQPILLDVYSQRDVTKTKYLQIRSHLLWNYPNLTVSTKLLNSFIYFCSFELCQLLKLGPQSMSRQASFKDPFTGNQQQQNPPTTDDDEDRNHDDDDDYKPSATSIQPTYFKKKNDLILDPINCNKSLSKVFRDLSRRSWQHSKPREPIGIFILPNETLFIRANNLNAYMDANRFVLKIKSQTMFTKNIQIQSAAIGADAIVDPKCQISAHSNVKMSVLGTQANIGSRCRVAGSLLFPGVHLGDEVILENCIIGPMAKIGSKCKLSNCYIEGHYVVEPKNNFKGETLANVYLDEDEEDELIYDDSVIAGESEIAEETDSDDRSDEDSDDSEYTDEYEYEDDGLFER
Protein: NAD(P)-binding Rossmann-fold superfamily protein (Q8VZB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Vacuolar protein sorting-associated protein 36
- At2g41950/T6D20.26
- Probable CCR4-associated factor 1 homolog 2
- Uncharacterized protein
- At3g51410
- Carrier protein
- DUF241 domain protein, putative
- DUF241 domain protein, putative
- Uncharacterized protein
- Expressed protein)
Sequence:
MGFISCISFPTINSRILSTHHFSKHSTSASSSYSLKFALRRQEDKPKVSFFLPLTSSLMATPIQASSSSTIGETSDGLKVQSHVSIGANDLLIVGPGVLGRLVAEQWRQEHPESQIFGQTVTTNHHGELENLGIKPSLKGTEYGGKFSYVIFCAPPSQSADYAGEVRNAASNWNGEGSFLFTSSSAPYDCFDNGECNEDSPVVPLGKSPRTDVLLKAEKVVLECGGTVLRLAGLYTETRGAHTYWLSKETIDARPDHILNLIHYEDAASLAVAIMKKKAGARIFLGCDNHPLSRQEVMDLMAQSGKFDKKFKGFTSTSGPLGKKLNNSKTRAEIGWEPKYPSFAQFFGVST
Protein: Nuclear factor 1 (A0A8I5ZZR6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKAEVKQKWASRLLAKLRKDIRPECREDFVLAVTGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAACAHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSSSPRTGVGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASAGMRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPNSPTSSSRNWTEDMEGGISSPVKKTEMDKSPFNSPSPQDSPRLSSFTQHHRPVIAVHSGIARSPHPSSALHFPATPILPQTASTYFPHTAIRYPPHLNPQDPLKDLVSLACDPATQQPGPSWYLG
Protein: RNA transcription, translation and transport factor protein (F7EMB2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MFRRKLTALDYHNPTGFNCKDETEFRNFIVWLEDQKIRHYKIEDRGNLRNIHSSDWPKFFEKYLRDVNCPFKIQDRQEAIDWLLGLAVRLEYGDNAEKYKDSVPDNRKNADNAAKNSEPLINLDVNNPDFKAGVMALANLLQIQRHDDYLVMLKAIRILVQERLTQDAVAKANQMKEGLPVALDKHILGFDTGDAVLNEAAQILRLLHIEELRELQTKINEAIVAVQAIIADPKTDHRLGKVGR
Protein: Inositol polyphosphate multikinase (EC 2.7.1.140) (EC 2.7.1.151) (EC 2.7.1.153) (Inositol 1,3,4,6-tetrakisphosphate 5-kinase) (Q7TT16)
Organism: Mus musculus (Mouse)
Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) first to inositol 1,3,4,5-tetrakisphosphate and then to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5). Phosphorylates inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4). Phosphorylates glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate to glycero-3-phospho-1D-myo-inositol 3,4,5-trisphosphate (By similarity). Plays an important role in MLKL-mediated necroptosis via its role in the biosynthesis of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Binding of these highly phosphorylated inositol phosphates to MLKL mediates the release of an N-terminal auto-inhibitory region, leading to activation of the kinase. Essential for activated phospho-MLKL to oligomerize and localize to the cell membrane during necroptosis (By similarity). Required for normal embryonic development, probably via its role in the biosynthesis of inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) and inositol hexakisphosphate (InsP6).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8NFU5}.
Interaction partners:
- Inositol-pentakisphosphate 2-kinase
- Inositol-tetrakisphosphate 1-kinase
- Multiple inositol polyphosphate phosphatase 1
- Kinase
- Inositol-trisphosphate 3-kinase C
- Inositol-trisphosphate 3-kinase A
- Inositol polyphosphate 5-phosphatase K
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
Sequence:
MAAEPPALRLRPPGSTGDSPPVPRLLGGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYTMVYAADCADAVLLELRKHLPKYYGVWSPPTAPNDVYLKLEDVTHKFNKPCIMDVKIGRKSYDPFASSEKIQQQVSKYPLMEEIGFLVLGMRVYHLHSDSYETQNQHYGRGLTKETLKEGVSKFFHNGFCLRKDAIAASIQKVEKILQWFENQKQLNFYASSLLFVYEGSSQPATTKANDRTLAGRFLSKGPLTDADGLECNNNFHLFGAPPNGMSVGKSLSKAYSRHRKLYAKKHQSQTSLKVETLEQDNGWRSMSQEHLNGNVLAQLEKVFYHLPAGRPEIPEAEVRMIDFAHVFPSNTVDEGYVYGLKHLIAVLRSILDS
Protein: DNA gyrase subunit B (EC 5.6.2.2) (Type IIA topoisomerase subunit GyrB) (P0AES6)
Organism: Escherichia coli (strain K12)
Function: DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner to maintain chromosomes in an underwound state. This makes better substrates for topoisomerase 4 (ParC and ParE) which is the main enzyme that unlinks newly replicated chromosomes in E.coli. Gyrase catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. E.coli gyrase has higher supercoiling activity than other characterized bacterial gyrases; at comparable concentrations E.coli gyrase introduces more supercoils faster than M.tuberculosis gyrase, while M.tuberculosis gyrase has higher decatenation than supercoiling activity compared to E.coli. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB subunit is toxic in E.coli, while the E.coli copy can be expressed in S.typhimurium even though the 2 subunits have 777/804 residues identical. The enzymatic differences between E.coli gyrase and topoisomerase IV are largely due to the GyrA C-terminal domain (approximately residues 524-841) and specifically the GyrA-box.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
Interaction partners:
- DNA topoisomerase 4 subunit A
- DNA gyrase subunit A
- Chromosomal replication initiator protein DnaA
- Beta sliding clamp
- DNA replication and repair protein RecF
- DNA-directed RNA polymerase subunit beta
- Fumarate hydratase class II
- DNA gyrase inhibitor YacG
- Protein RecA
- RNA polymerase sigma factor RpoD
Sequence:
MSNSYDSSSIKVLKGLDAVRKRPGMYIGDTDDGTGLHHMVFEVVDNAIDEALAGHCKEIIVTIHADNSVSVQDDGRGIPTGIHPEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSQKLELVIQREGKIHRQIYEHGVPQAPLAVTGETEKTGTMVRFWPSLETFTNVTEFEYEILAKRLRELSFLNSGVSIRLRDKRDGKEDHFHYEGGIKAFVEYLNKNKTPIHPNIFYFSTEKDGIGVEVALQWNDGFQENIYCFTNNIPQRDGGTHLAGFRAAMTRTLNAYMDKEGYSKKAKVSATGDDAREGLIAVVSVKVPDPKFSSQTKDKLVSSEVKSAVEQQMNELLAEYLLENPTDAKIVVGKIIDAARAREAARRAREMTRRKGALDLAGLPGKLADCQERDPALSELYLVEGDSAGGSAKQGRNRKNQAILPLKGKILNVEKARFDKMLSSQEVATLITALGCGIGRDEYNPDKLRYHSIIIMTDADVDGSHIRTLLLTFFYRQMPEIVERGHVYIAQPPLYKVKKGKQEQYIKDDEAMDQYQISIALDGATLHTNASAPALAGEALEKLVSEYNATQKMINRMERRYPKAMLKELIYQPTLTEADLSDEQTVTRWVNALVSELNDKEQHGSQWKFDVHTNAEQNLFEPIVRVRTHGVDTDYPLDHEFITGGEYRRICTLGEKLRGLLEEDAFIERGERRQPVASFEQALDWLVKESRRGLSIQRYKGLGEMNPEQLWETTMDPESRRMLRVTVKDAIAADQLFTTLMGDAVEPRRAFIEENALKAANIDI
Protein: Cytochrome P450 71D18 (EC 1.14.14.51) ((-)-(4S)-Limonene-6-hydroxylase) (Q9XHE8)
Organism: Mentha spicata (Spearmint)
Function: Hydroxylates (-)-(4S)-limonene to (-)-trans-carveol, a precursor of (-)-carvone, responsible for the typical spearmint flavor note. Fluorinated substrate analogs are hydroxylated with the same regio- and stereochemistry.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELDLLSAIIILVATYIVSLLINQWRKSKSQQNLPPSPPKLPVIGHLHFLWGGLPQHVFRSIAQKYGPVAHVQLGEVYSVVLSSAEAAKQAMKVLDPNFADRFDGIGSRTMWYDKDDIIFSPYNDHWRQMRRICVTELLSPKNVRSFGYIRQEEIERLIRLLGSSGGAPVDVTEEVSKMSCVVVCRAAFGSVLKDQGSLAELVKESLALASGFELADLYPSSWLLNLLSLNKYRLQRMRRRLDHILDGFLEEHREKKSGEFGGEDIVDVLFRMQKGSDIKIPITSNCIKGFIFDTFSAGAETSSTTISWALSELMRNPAKMAKVQAEVREALKGKTVVDLSEVQELKYLRSVLKETLRLHPPFPLIPRQSREECEVNGYTIPAKTRIFINVWAIGRDPQYWEDPDTFRPERFDEVSRDFMGNDFEFIPFGAGRRICPGLHFGLANVEIPLAQLLYHFDWKLPQGMTDADLDMTETPGLSGPKKKNVCLVPTLYKSP
Protein: Repulsive guidance molecule BMP co-receptor a (A0A8I6ACJ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MRKRLDKVTPQFTEKELCSISGKVSLHLSPREICRKGSNMMAHLFFSIAISPCKILKCNSEFWSATSSGSHAPASDDVPEFCAALRTYALCTRRTARTCRGDLAYHSAVHGIEDLMSQHNCSKDGPTSQPRVRTLPPAGDSQERSDSPEICHYEKSFHKHSAAPNYTHCGLFGDPHLRTFTDHFQTCKVQGAWPLIDNNYLNVQVTNTPVLPGSAATATSKLTIIFKNFQECVDQKVYQAEMDELPSAFADGSKNGGDKHGANSLKITEKVSGQHVEIQAKYIGTTIVVRQVGRYLTFAVRMPEEVVNAVEDRDSQGLYLCLRGCPLNQQIDFQAFRANAESPRRPAAASPSPVVPETFPYETAVAKCKEKLPVEDLYYQACVFDLLTTGDVNFTLAAYYALEDGKMLHSNKDKLHLFERTRELPGAVAAAAFPLAPEMLPGTVTLLVLLPLFW
Protein: Zinc metalloproteinase barnettlysin-1 (EC 3.4.24.-) (Barnettlysin-I) (Snake venom metalloproteinase) (SVMP) (P86976)
Organism: Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti)
Function: Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen and fibrin but has no activity on beta- and gamma-chains. Cleaves X-Leu bonds. Inhibits platelet aggregation induced by the von Willebrand factor (VWF) (IC(50) is 1.4 uM) and type I collagen (IC(50) is 3.2 uM). Acts by cleaving the vWF and its receptor GPIb, and by cleaving the collagen-binding Alpha-2A domain of the collagen receptor alpha-2/beta-1 integrin (ITGA2/ITGB1). Also degrades the extracellular matrix protein fibronectin (FN1), but has no effect on laminin and type I collagen.
Subcellular location: Secreted {ECO:0000269|PubMed:26723171}.
Interaction partners:
Sequence:
TPEQQRYVELFIVVDHGMFMKXXXXXXXXXXXIHQMVNIMKEAYRYLYIDILLTGVEIWSNKDLINVQPAAPQTLDSFGEWRXXXXXXXKSHDNAQLLTSTDFDGPTIGLAYVGSMCDPKRSTAVIQDHSEIDLLVAVTMDHELGHNLGIRHDTGSCSCGGYPCVMSPVISHDISKYFSDCSYIQCWDFIMKENPQCILNKR
Protein: La-related protein Larp4B (La ribonucleoprotein domain family member Larp4B) (Q9I7T7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable RNA binding protein. Negatively regulates myc at the protein level, via an unknown mechanism, and may therefore have a role in growth. Has no effect on myc mRNA levels.
Interaction partners:
- LD12377p
- Polyadenylate-binding protein
Sequence:
MEYFLGGYVYMNGDALKIQPPVYTNVPVETAMLATNLFGATTQIAASPAAAAAAHIPLITAAAAAAAAAGAPAVAPPVAVAPVATASAAQAAVVPAQQQQQAHPHQAQILAHTHVAHQQQQQQQQQTIQQHLHQQQQQQSPHPAQHLTYGHQPALSQATAGGSGTISGGAVGPSGVVVEGQDTNEYAIMNGALGQTQDGTVVCYTTDALNNTNLVALDPQPHQIVVPVQVPVQVPVPVQLPANGSADPQQGSHNAAGGEEPNIPLDKLKQMLATQLEYYFSRENLANDTYLLSQMDSDQYVPIYTVARFNLVRKLTNDINLITEVLRESPNVQVDDKGLRVRPNRKRCIIILREISNNTPLDDVKALFSNESCPRPISCEFAANNSWYITFESDEDAQKAYKYLREEVKEFQGKPIMARIKPKSFINRIQAVPKNGYRLTSPPTANVFDPAGAGGATVSYAAAQQPRYLYTNGAAIAAPASVQYSNPVLIPIPQNQFYPGLVAGPWPPGTVAATTAHGQNFYELGGNIFTTNPLPPQPVTAGFAQAPPPTSQAMVTPKPQGGGRYNNNHRGNPNNVGGANSGPRAESRSKPPRSTPSASHIQGGNIMPIQITAPIPGGMVSVVPTNIVQDPLQPAPLQQQPQQVIQQIQQQPSSSAQQQQAATVQMNNTTRHYPIKSNWKGGMQKNLDKSYSGGVATHHHYTTQVQALPAHSHHLQAQQQLQGQTQQQHYQLASSSAASAPQVTYVTTAPAPQQPGQHQHHLVVQQTQPQQQQQQQQVVLQQQQVQVQELQEAGDGVEHSSHAMQQVNRSSNMSASSSSSLATSMSKEPLQWQNRPRRRRRDEEGGINYSPGGRVGLYGSSPSNPHPQQHLMSSSTGSNVQSAGGTDGGGASHRGGERQSHYNTIHDVPPPQHRGNYKGNNYNPHYHAQHSSMASGSHHHHHHNALSSQQQQHHLTTGTGQQGSGHHYHHHHHHNSIGSNVGNSGGLGVSSGGSGGGGSGGGSGSNSLSGGSNERGIHHSSLGYQGHQHQHQQQQQQQQQQQQQQPAAPVQPPQFDLEDAAFPPLPATSATAPHTPQATGGASLHNSTTSSSSSTGLGQKQTLHQQQQQAPQQHQVLSSSVESAGGDEQRSSNQQGIETSNIHLANSSTANNWVENRLSDVVRTGGGGGGGGKGKARKDNRHPQGQNQPHMAPNYQQHQPRNPPVSPTPALGAEYGIQIQEGNNTKNVTKQSSSNNNSIHVIKCQTPNINASSKEEAAGAQQQQQQQLDKSNKTEDEMHPKQPSQQRLVEGYVQQQQLPLLAAHNEYSAALAAGAGACSVVEGGLTTSLAECSLGQHKKPPSVAALHAKKDANLLEKGASKHKSVATSTSTENLSAAATASKLSYAQVAQHHKAAASSDSKETGSGGSTGTLSPTGSHKMDLVFGDPAVVVAAVEKSGLATVSTEKRVAGGASPAALIGKPAGGLPATNTTQGSSAVVVSAKEKDNRPNASVRPLSKEKQQQHYGSATEHNTNANIGLGASGNRKSRANNS
Protein: Mitochondrial prohibitin complex protein 2 (Prohibitin-2) (P50093)
Organism: Caenorhabditis elegans
Function: PHB proteins are essential during embryonic development and are required for somatic and germline differentiation in the larval gonad. A deficiency in PHB proteins results in altered mitochondrial biogenesis in body wall muscle cells. Required for clearance of paternal mitochondria after embryonic fertilization.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12794069}; Single-pass type II membrane protein {ECO:0000269|PubMed:12794069}; Intermembrane side {ECO:0000269|PubMed:12794069}.
Interaction partners:
- Mitochondrial prohibitin complex protein 1
- Conserved regulator of innate immunity protein 3
- Serine/threonine-protein kinase pink-1, mitochondrial
- Serine/threonine-protein phosphatase Pgam5, mitochondrial
- FUN14 domain-containing protein fndc-1
- AFG3-like protein spg-7
- Probable voltage-dependent anion-selective channel
- SEC7 domain-containing protein
- Elongation factor Tu, mitochondrial
- Transmembrane GTPase fzo-1
Sequence:
MAKQGQEAMKKAIQNARGAGVGLGLVAAAGAAVYGVAQSMFTVEAGHRAIMFNRIGGLSTDLYKEGLHFRIPWFQYPIIYDIRARPNQIRSPTGSKDLQMVNIGLRVLSRPNPEHLVHIYRTLGQNWEERVLPSICNEVLKGVVAKFNASQLITQRQQVSMLVRKTLIERALDFNIILDDVSLTELAFSPQYSAAVEAKQVAAQEAQRATFYVERAKQQKQEKIVQAEGEAESAKLLGEAMKNDPGFLKLRKIRAAQKIARIVSESGNKTYLPTGGLMLNIADTDYLNVTDKRR
Protein: Ribosomal protein L5 (F7DSA5)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLVRLDLESPLLSRNDSGFVKVVKNKAYFKRYQVKFRRRREGKTDYYARKRLVIQDKNKYNTPKYRMIVRVTNRDIICQIAYARIEGDMIVCAAYAHELTKYGVKVGLTNYAAAYCTGLLLARRLLNKFGLDKVYEGQVEVTGDEYNVESIDGEPGAFTCYLDAGLTRTTTGNKVFGALKGAVDGGLSIPHSTKRFPGYDSESKEFNAEVHRKHIFGQNIAEYMRLLTEEDEDAFKKQFSQYIKNGVTADQMEDIYKKAHAGIRENPVHEKKPKKEVKKKRWNRAKLSLAQKKDRVAQKKASFLRAQEKADS
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-) (P97857)
Organism: Mus musculus (Mouse)
Function: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-Glu-|-Leu-1692' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover. Has angiogenic inhibitor activity (By similarity). Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Aggrecan core protein
- Fibulin-1
- Metalloproteinase inhibitor 3
- Versican core protein
- Metalloproteinase inhibitor 1
- Collagenase 3
- Cartilage oligomeric matrix protein
- Metalloproteinase inhibitor 2
- Stromelysin-1
- Fibronectin
Sequence:
MQPKVPLGSRKQKPCSDMGDVQRAARSRGSLSAHMLLLLLASITMLLCARGAHGRPTEEDEELVLPSLERAPGHDSTTTRLRLDAFGQQLHLKLQPDSGFLAPGFTLQTVGRSPGSEAQHLDPTGDLAHCFYSGTVNGDPGSAAALSLCEGVRGAFYLQGEEFFIQPAPGVATERLAPAVPEEESSARPQFHILRRRRRGSGGAKCGVMDDETLPTSDSRPESQNTRNQWPVRDPTPQDAGKPSGPGSIRKKRFVSSPRYVETMLVADQSMADFHGSGLKHYLLTLFSVAARFYKHPSIRNSISLVVVKILVIYEEQKGPEVTSNAALTLRNFCSWQKQHNSPSDRDPEHYDTAILFTRQDLCGSHTCDTLGMADVGTVCDPSRSCSVIEDDGLQAAFTTAHELGHVFNMPHDDAKHCASLNGVSGDSHLMASMLSSLDHSQPWSPCSAYMVTSFLDNGHGECLMDKPQNPIKLPSDLPGTLYDANRQCQFTFGEESKHCPDAASTCTTLWCTGTSGGLLVCQTKHFPWADGTSCGEGKWCVSGKCVNKTDMKHFATPVHGSWGPWGPWGDCSRTCGGGVQYTMRECDNPVPKNGGKYCEGKRVRYRSCNIEDCPDNNGKTFREEQCEAHNEFSKASFGNEPTVEWTPKYAGVSPKDRCKLTCEAKGIGYFFVLQPKVVDGTPCSPDSTSVCVQGQCVKAGCDRIIDSKKKFDKCGVCGGNGSTCKKMSGIVTSTRPGYHDIVTIPAGATNIEVKHRNQRGSRNNGSFLAIRAADGTYILNGNFTLSTLEQDLTYKGTVLRYSGSSAALERIRSFSPLKEPLTIQVLMVGHALRPKIKFTYFMKKKTESFNAIPTFSEWVIEEWGECSKTCGSGWQRRVVQCRDINGHPASECAKEVKPASTRPCADLPCPHWQVGDWSPCSKTCGKGYKKRTLKCVSHDGGVLSNESCDPLKKPKHYIDFCTLTQCS
Protein: Uncharacterized protein (F4KC44)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEGTKRSSLGARKKLKRKKCRRLVRSIVTYLKSDTYLFAPLFSNFPPLTTEIDTPPPSNSKPSTVDDISMEGFESLGIEKLIKKRRMSEKVKEYLKSDCYMYSPMISSPPKLGSSVKGKMQITMEVSTKLSTTTMKEDDSGYRNLRSDIAEQTLHKGRINSPKPALVILEGQRTGLGRETDLSPAFSSPTGLLIDCTNHGMKMEFVRRFFKHWITK
Protein: Synapse-associated protein 1 (BSD domain-containing signal transducer and Akt interactor protein) (BSTA) (Q96A49)
Organism: Homo sapiens (Human)
Function: Plays a role in adipocyte differentiation by promoting mTORC2-mediated phosphorylation of AKT1 at 'Ser-473' after growth factor stimulation.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9D5V6}. Golgi apparatus {ECO:0000250|UniProtKB:Q9D5V6}. Perikaryon {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, axon {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9D5V6}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9D5V6}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9D5V6}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9D5V6}. Membrane {ECO:0000269|PubMed:23300339}. Note=Localizes to cholinergic neuromuscular junctions and in actin-rich growth cone regions (By similarity). Membrane-associated in a epidermal growth factor (EGF)-dependent manner (PubMed:23300339). {ECO:0000250|UniProtKB:Q9D5V6, ECO:0000269|PubMed:23300339}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Sequence:
MFRGLSSWLGLQQPVAGGGQPNGDAPPEQPSETVAESAEEELQQAGDQELLHQAKDFGNYLFNFASAATKKITESVAETAQTIKKSVEEGKIDGIIDKTIIGDFQKEQKKFVEEQHTKKSEAAVPPWVDTNDEETIQQQILALSADKRNFLRDPPAGVQFNFDFDQMYPVALVMLQEDELLSKMRFALVPKLVKEEVFWRNYFYRVSLIKQSAQLTALAAQQQAAGKEEKSNGREQDLPLAEAVRPKTPPVVIKSQLKTQEDEEEISTSPGVSEFVSDAFDACNLNQEDLRKEMEQLVLDKKQEETAVLEEDSADWEKELQQELQEYEVVTESEKRDENWDKEIEKMLQEEN