wanglab/gogpt-training-data huggingface dataset:
Protein: Tyrosine-protein kinase Mer (EC 2.7.10.1) (Proto-oncogene c-Mer) (Receptor tyrosine kinase MerTK) (Q60805)
Organism: Mus musculus (Mouse)
Function: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment. Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q12866}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth arrest-specific protein 6
- Vitamin K-dependent protein S
- Galectin-3
- Tubby-related protein 1
- Multiple epidermal growth factor-like domains protein 10
- Integrin alpha-M
- P2Y purinoceptor 12
- Triggering receptor expressed on myeloid cells 2
- High affinity immunoglobulin gamma Fc receptor I
- Transmembrane protein 119
Sequence:
MVLAPLLLGLLLLPALWSGGTAEKWEETELDQLFSGPLPGRLPVNHRPFSAPHSSRDQLPPPQTGRSHPAHTAAPQVTSTASKLLPPVAFNHTIGHIVLSEHKNVKFNCSINIPNTYQETAGISWWKDGKELLGAHHSITQFYPDEEGVSIIALFSIASVQRSDNGSYFCKMKVNNREIVSDPIYVEVQGLPYFIKQPESVNVTRNTAFNLTCQAVGPPEPVNIFWVQNSSRVNEKPERSPSVLTVPGLTETAVFSCEAHNDKGLTVSKGVHINIKVIPSPPTEVHILNSTAHSILVSWVPGFDGYSPLQNCSIQVKEADRLSNGSVMVFNTSASPHLYEIQQLQALANYSIAVSCRNEIGWSAVSPWILASTTEGAPSVAPLNITVFLNESNNILDIRWTKPPIKRQDGELVGYRISHVWESAGTYKELSEEVSQNGSWAQIPVQIHNATCTVRIAAITKGGIGPFSEPVNIIIPEHSKVDYAPSSTPAPGNTDSMFIILGCFCGFILIGLILCISLALRRRVQETKFGGAFSEEDSQLVVNYRAKKSFCRRAIELTLQSLGVSEELQNKLEDVVIDRNLLVLGKVLGEGEFGSVMEGNLKQEDGTSQKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCIELSSQGIPKPMVILPFMKYGDLHTFLLYSRLNTGPKYIHLQTLLKFMMDIAQGMEYLSNRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAIESLADRVYTSKSDVWAFGVTMWEITTRGMTPYPGVQNHEMYDYLLHGHRLKQPEDCLDELYDIMYSCWSADPLDRPTFSVLRLQLEKLSESLPDAQDKESIIYINTQLLESCEGIANGPSLTGLDMNIDPDSIIASCTPGAAVSVVTAEVHENNLREERYILNGGNEEWEDVSSTPFAAVTPEKDGVLPEDRLTKNGVSWSHHSTLPLGSPSPDELLFVDDSLEDSEVLM
Protein: Actin-related protein 2/3 complex subunit 5 (Arp2/3 complex 16 kDa subunit) (p16-ARC) (Q4KLF8)
Organism: Rattus norvegicus (Rat)
Function: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15511}. Cell projection {ECO:0000250|UniProtKB:O15511}. Nucleus {ECO:0000250|UniProtKB:O15511}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1A
- Actin nucleation-promoting factor WAS
- Actin nucleation-promoting factor WASL
- Actin-binding protein WASF1
Sequence:
MSKNTVSSARFRKVDVDEYDENKFVDEEDGGDGQAGPDEGEVDSCLRQGNMTAALQAALKNPPINTKSQAVKDRAGSIVLKVLISFKANDIEKAVQSLDKNGVDLLMKYIYKGFESPSDNSSAMLLQWHEKALAAGGVGSIVRVLTARKTV
Protein: Beta-glucosidase 19 (AtBGLU19) (EC 3.2.1.21) (Q9LIF9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- At3g47000
- Beta-D-glucan exohydrolase-like protein
- Glycosyl hydrolase family protein
- Beta-D-glucan exohydrolase-like protein
- beta-glucosidase
- Glycosyl hydrolase family protein
- Glycosyl hydrolase family protein
- L-type lectin-domain containing receptor kinase I.7
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
Sequence:
MKIPLLGLLLLISLVGSPTRAEEGPVCPKTETLSRASFPEGFMFGTATAAFQVEGAVNEGCRGPSLWDIYTKKFPHRVKNHNADEAVDFYHRYKEDIQLMKKLNTDGFRLSISWPRIFPHGRMEKGISKEGVQFYHDLIDELLKNDITPLVTVFHWDTPADLEDEYGGFLSERIVPDFVEYANFTFHEYGDKVKNWITFNEPWVFSRSGYDVGKKAPGRCSPYVKEFGKLCQDGRSGFEPYVVSHNLLVGHAEAVDAFRKCEKCKGGKIGIAHSPAWFEPEDVEGGQATVNRVLDFVIGWHLDPTTFGDYPQSMKDAVGSRLPRFTKAQKAKLKDSTDFVGINYYTSFFAKADQKVDSRNPTWATDALVEFEPKTVDGSIKIGSQPNTAKMAVYAKGLRKLMKYIKDRYNSPEIIITENGYGEDLGDKDTDLSVALNDHNRKYYLQRHLLALNEAICEDKVNVTSYFLWSLMDNFEWQDGYTARFGVYYIDFKNNLTRMEKESAKWLSEFLKPGLKPSKSSKLHEEL
Protein: Centrin 3 (E5RJF8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLALRSELVVDKTKRKKRRELSEEQKQEIKDAFELFDTDKDEAIDYHELKVAMRALGFDVKKADVLKILKDYDREATGKITFEDFNEVVTDWILERDPHEEILKAFKLFDDDDSGKISLRNLRRVARELGENMSDEELRAMIEEFDKDGDGEILKNILLLPIWSRCLSLNREFFSEVNQEEFIAIMTGDI
Protein: Ribonucleoside-diphosphate reductase large chain (EC 1.17.4.1) (Ribonucleotide reductase) (P36602)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Interaction partners:
- Ribonucleoside-diphosphate reductase small chain
- Adenylate kinase
- Thymidylate kinase
- Nucleoside diphosphate kinase
- Uridylate kinase
- Guanylate kinase
- Adenylate kinase isoenzyme 6 homolog
- Cell division control protein 18
- Probable thymidylate synthase
- Golgi apyrase
Sequence:
MFVYKRDGRQEKVAFDKITARVSRLCYGLDSDHVDPVEITQKVISGVYPGVTTIELDNLAAETAATMTTKHPDYAILAARIAVSNLHKQTEKVFSTVVQQLHDYVNPKTDKPAPMISDKIYDIVMKHKDELDSAIIYDRDFTYNFFGFKTLERSYLLRIDGKVAERPQHMIMRVAVGIHGEDIEAAIETYNLMSQRYFTHASPTLFNAGTPRPQLSSCFLVTMKDDSIEGIYDTLKMCAMISKTAGGIGINIHNIRATGSYIAGTNGTSNGIVPMIRVYNNTARYVDQGGNKRPGAFAAYLEPWHADVMDFLELRKTHGNEDFRAREMFYALWIPDLFMQRVERNEQWTFFCPNEAPGLADVWGDEFVALYEKYEKENRGRRSLPAQKVWYAILQSQVETGNPFMLYKDSCNRKSNQKNVGTIRCSNLCTEIVEYSSPDEVAVCNLASVALPTFIKDGKYNFQKLHDVVKVVTRNLNKIIDVNYYPVPEARRSNMRHRPVGLGVQGLADAFFALRLPFESAGAKKLNIQIFETIYHAALEASCEIAQVEGTYESYEGSPASQGILQYDMWNVNPTDLWDWAELKEKIAKHGIRNSLLVAPMPTASTSQILGFNECFEPYTSNMYQRRVLSGEFQIVNPWLLKDLVERDLWNEDMKNKLVMLDGSIQAIPEIPQDLKDLYKTVWEISQKTVIDYAADRGPFIDQSQSLNIHLKDPSYGKITSMHFYGWKKGLKTGMYYLRTMAASAAIKFTVDPVALRARNEESNEENKKPVIKNGKAEISAEPTKEEIDIYNEKVLACSIKNPEACEMCSA
Protein: Lysosomal-associated transmembrane protein 5 (Lysosomal-associated multitransmembrane protein 5) (Retinoic acid-inducible E3 protein) (Q13571)
Organism: Homo sapiens (Human)
Function: May have a special functional role during embryogenesis and in adult hematopoietic cells.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:8661146}; Multi-pass membrane protein {ECO:0000269|PubMed:8661146}.
Interaction partners:
- Leukocyte surface antigen CD53
- Lysosomal-associated transmembrane protein 4B
- Lysosomal-associated transmembrane protein 4A
- Nck-associated protein 1-like
- Integrin beta-2
- Hematopoietic lineage cell-specific protein
- E3 ubiquitin-protein ligase NEDD4
- Rho GDP-dissociation inhibitor 2
- Plastin-2
- Syndecan-3
Sequence:
MDPRLSTVRQTCCCFNVRIATTALAIYHVIMSVLLFIEHSVEVAHGKASCKLSQMGYLRIADLISSFLLITMLFIISLSLLIGVVKNREKYLLPFLSLQIMDYLLCLLTLLGSYIELPAYLKLASRSRASSSKFPLMTLQLLDFCLSILTLCSSYMEVPTYLNFKSMNHMNYLPSQEDMPHNQFIKMMIIFSIAFITVLIFKVYMFKCVWRCYRLIKCMNSVEEKRNSKMLQKVVLPSYEEALSLPSKTPEGGPAPPPYSEV
Protein: Glycophorin HeP2 (Q12832)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MYGKIIFVLLLSEIVSISAWSTSGVAMHTSTSSSVTKSYISSQTNGEMGQLVHRFTVPGMRMWPACCLILPRTGCTCCSLVYANWLHLLFLCLCPYPWLS
Protein: Globin domain-containing protein (Q18311)
Organism: Caenorhabditis elegans
Interaction partners:
- GLOBIN domain-containing protein
- Globin domain-containing protein
- Globin family profile domain-containing protein
- GLOBIN domain-containing protein
- Globin domain-containing protein
- Heme transporter hrg-5
- Globin-like protein 9
- Globin domain-containing protein
- GLOBIN domain-containing protein
- GLOBIN domain-containing protein
Sequence:
MMGLLSTIRGKKEPVVGNGIGSAQVGPLNAKTKKLVIQEWPRVLAQCPELFTEIWHKSATRSTSIKLAFGIAENESPMQNAAFLGLSSTIQAFFYKLIITYELNDDQVREACEQLGARHVDFISRGFNSHFWDIFLVCMAEKIDETLSAYIPDEDKRNEMILAWQRVINSIVHQMRNGYSDRRKQQLGGTKGGSNNGF
Protein: Spermidine synthase (SPDSY) (EC 2.5.1.16) (Putrescine aminopropyltransferase) (Q64674)
Organism: Mus musculus (Mouse)
Function: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate, and has very low activity towards 1,3-diaminopropane. Has extremely low activity towards spermidine (By similarity).
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme 1
- Ornithine decarboxylase
- S-adenosylmethionine decarboxylase proenzyme 2
- Gene model 853
- Guanidino acid hydrolase, mitochondrial
- S-methyl-5'-thioadenosine phosphorylase
- Diamine acetyltransferase 1
- Spermine synthase
- Thialysine N-epsilon-acetyltransferase
- Amine oxidase
Sequence:
MEPGPDGPAAPGPAAIREGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIEVSKKFLPGMAVGFSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGILCCQGECQWLHLDLIKEMRHFCKSLFPVVDYAYCSIPTYPSGQIGFMLCSKNPSTNFREPVQQLTQAQVEQMQLKYYNSDMHRAAFVLPEFTRKALNDIS
Protein: Ensconsin, isoform A (LD09626p) (Q9I7T2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASLGGQHGNISTNPEVENTAKRPESREGSAERKAHAFAPAKISGCSAGATLHWFAQVGGQISASEDDSQASKDREEKLKYARDRQNEERHRKIEELRAQAEAAQRYREQKEEERRRRIEEIRTRDTEKRHQVEERKKAIFEAEKERREYILKKNQERESRIEVKKRDRNSIGFAFGSSTPRLLDVPADYGLVSPSAFWGQRRSTSISNVAGASLTRRSSERELADSGAKKRASSSTDRQDGSRSGNATPGGHFNNSRPGSAMSTSTNMSTSGLVPRRPATAPRKPRPASIAGTGMSLEEINKLKRDQKPPVKTTAASPSAQTTPKRTANLMSTSLIVTSSSSRLSSAEKKTPSKREPPVPKAASASKALPSRTASSERISRLTKEPKTKDTSAMTRSMIVTSSSTSTITKPAPAPVAPTSAPVPEQNGVAKEVEKTTADEPVPEAEVPTEAPVVVPSVSKAEKEALNTEKTEEGARQEEEQILAVESVPEALVTSINVEEKSDEGNEKEVPKPQEQAAPKKPSRSKENSEVRELTPPEGADLMTASMMAKKITTEEEAKAALAERRRLAREEAERQAELERQRLEAERLAEIKAQEEEAERQRLFEEESTRLAEEQRRGEEERLRKAIEEAQQREEEEKRRREEEEKQRVEREEAEKKAKEEAEKQRVEVAERLKREEKEREERRKRVEAIMLRTRKGGAATTPSKDANDKAAPAATAPENNSSSNSSVTGSSNNSAEGSPSAADSTPAPTATETVQEAPNSQAMYEQSVLDKENSLINSFSTMIIDENAKNLQQVSNGKLLVDFESTNTVPAVANGNGHIENVNNKNDINLLQDVVAPVATQLIDLSIESQDLHLNNNNSLLTSTAATTTLVTADSHENKDISLL
Protein: Popeye domain-containing protein 2 (Popeye protein 2) (Q9HBU9)
Organism: Homo sapiens (Human)
Function: Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density.
Subcellular location: Membrane {ECO:0000269|PubMed:26642364}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26642364}.
Interaction partners:
- Potassium channel subfamily K member 2
Sequence:
MSANSSRVGQLLLQGSACIRWKQDVEGAVYHLANCLLLLGFMGGSGVYGCFYLFGFLSAGYLCCVLWGWFSACGLDIVLWSFLLAVVCLLQLAHLVYRLREDTLPEEFDLLYKTLCLPLQVPLQTYKEIVHCCEEQVLTLATEQTYAVEGETPINRLSLLLSGRVRVSQDGQFLHYIFPYQFMDSPEWESLQPSEEGVFQVTLTAETSCSYISWPRKSLHLLLTKERYISCLFSALLGYDISEKLYTLNDKLFAKFGLRFDIRLPSLYHVLGPTAADAGPESEKGDEEVCEPAVSPPQATPTSLQQTPPCSTPPATTNFPAPPTRARLSRPDSGILASRIPLQSYSQVISRGQAPLAPTHTPEL
Protein: V-type proton ATPase subunit H (V-ATPase subunit H) (Vacuolar proton pump subunit H) (Q8BVE3)
Organism: Mus musculus (Mouse)
Function: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:O46563}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit D
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit F
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit d 2
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit E 1
Sequence:
MTKMDIRGAVDAAVPTNIIAAKAAEVRANKVNWQSYLQGQMISAEDCEFIQRFEMKRSSEDKQEMLQTEGSQCAKTFINLMTHISKEQTVQYILTMVDDMLQENHQRVSIFFDYAKRSKSTAWPYFLPMLNRQDPFTVHMAARIIAKLAAWGKELMEGSDLNYYFNWIKTQLSSQKLRGSGVAVETGTISSSDSSQYVQCVAGCLQLMLRVNEYRFAWVEADGVNCIMGVLSNKCGFQLQYQMIFSIWLLAFSPQMCEHLRRYNIIPVLSDILQESVKEKVTRIILAAFRNFLEKSTERETRQEYALAMIQCKVLKQLENLEQQKYDDEDISEDIKFLLEKLGESVQDLSSFDEYSSELKSGRLEWSPVHKSEKFWRENAVRLNEKNYELLKILTKLLEVSDDPQVLAVAAHDVGEYVRHYPRGKRVIEQLGGKQLVMNHMHHEDQQVRYNALLAVQKLMVHNWEYLGKQLQSEQPQTAAARS
Protein: Ankyrin repeat domain 23 (A0A8I6B0D0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDFISIQQLVSGERVGRKALEFGRGVPDPGGWPSGWTLGPQEAVAWEKLKLEEEKRKKLERFNSSRLTLDNLTDLENLIQRRRKKRQRHKVPPREPESGAEPQPQVPLEPVGLEMFLKAAAENQEALIDKYLADGGDPNAHDKLHRTALHWACLKGHRQLVNKLLAAGAAIETRDLLDRTPVFWACRGGHLDILKQLLNQGAQINAQDKIWSTPLHVAVRMGHSDCLEHLIECGAHINAQDKEGDTALHEAVRYGHHKATKLLLLYGAKLGMKNGASLTPVQLARDWQRGIREALQAHVGHPRTRC
Protein: Epididymis secretory sperm binding protein (A0A384NPK6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTPGTQSPFFLLLLLTVLTATTAPKPATVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAFNSSLEDPSTDYYQELQRDISEMAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL
Protein: Antimicrobial peptide 1 (ToAMP1) (B3EWQ1)
Organism: Taraxacum officinale (Common dandelion) (Leontodon taraxacum)
Function: Antimicrobial peptide. Active against fungal species B.cinerea (IC(50)=5.8 uM) and A.niger (IC(50)=5.6 uM) but not against F.oxysporum, F.graminearum, B.sorokinina and P.debaryanum at concentrations below 10 uM. Active against bacterial species P.syringae, B.subtilis and X.campestris.
Interaction partners:
Sequence:
VAKCTEESGGKYFVFCCYKPTRICYMNEQKCESTCIGK
Protein: Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acetyl-CoA synthetase 2) (AceCS2) (Acyl-CoA synthetase short-chain family member 1) (Propionate--CoA ligase) (EC 6.2.1.17) (Q9NUB1)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate. Can also utilize propionate with a much lower affinity (By similarity). Provides acetyl-CoA that is utilized mainly for oxidation under ketogenic conditions (By similarity). Involved in thermogenesis under ketogenic conditions, using acetate as a vital fuel when carbohydrate availability is insufficient (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16788062}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial
- Citrate synthase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Acetyl-CoA carboxylase 1
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-coenzyme A thioesterase
- Peroxisomal acyl-coenzyme A oxidase 3
- Acetyl-CoA acetyltransferase, cytosolic
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase, mitochondrial
Sequence:
MAARTLGRGVGRLLGSLRGLSGQPARPPCGVSAPRRAASGPSGSAPAVAAAAAQPGSYPALSAQAAREPAAFWGPLARDTLVWDTPYHTVWDCDFSTGKIGWFLGGQLNVSVNCLDQHVRKSPESVALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAVHTVIFAGFSAESLAGRINDAKCKVVITFNQGLRGGRVVELKKIVDEAVKHCPTVQHVLVAHRTDNKVHMGDLDVPLEQEMAKEDPVCAPESMGSEDMLFMLYTSGSTGMPKGIVHTQAGYLLYAALTHKLVFDHQPGDIFGCVADIGWITGHSYVVYGPLCNGATSVLFESTPVYPNAGRYWETVERLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINCEAWEWLHRVVGDSRCTLVDTWWQTETGGICIAPRPSEEGAEILPAMAMRPFFGIVPVLMDEKGSVVEGSNVSGALCISQAWPGMARTIYGDHQRFVDAYFKAYPGYYFTGDGAYRTEGGYYQITGRMDDVINISGHRLGTAEIEDAIADHPAVPESAVIGYPHDIKGEAAFAFIVVKDSAGDSDVVVQELKSMVATKIAKYAVPDEILVVKRLPKTRSGKVMRRLLRKIITSEAQELGDTTTLEDPSIIAEILSVYQKCKDKQAAAK
Protein: Aspartyl beta-hydroxylase, isoform H (EC 1.14.11.16) (A0A0B4K7C1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGDVQPRKRKDKRRKRDDRKSEGDVTVLRQSSFQDDDESSHGVHITKMGNEDLHLHVHHDHGTGGHWCAKIIFFALMAVLLGLVGLIIMENRGLEDLDTPLSESRFSKVFDGWVDEHRDEHDGHDVQEPSGEALDDHDEHDDHDDHEDEDEEPLTEELEEELEEEEEPTEEDEPAADEEYEEDEDEENNAGENITAEDAEEEEEEEDNDDEGTVEATVEATTEATTEATGEYEAEEDDEDEAAADDDAVESTEAPLSKAEEQEDDEDEDEEEQEIEESVEPERSQYAAQSAPAKDNNDDDDDDDQDKNDADDGDDDEFESLAQQFENDPEDTVPAKAVESEEQDQDQADEEEPKEEGSSWLASQIKPKEAAPAPAEKEDPFEQELRKANEEMIRENYAQALRSFNTLTTNFAHEPSAHLGRARLLELLAKKERSNQRLWEAIDAYKRYLAFGELVASNQEFQTAGESCIENLRFLGHHRQATTIHELLINRLPEDPRLRNQLSLTYLMVNNLQQVEKVAVETLKLWPNNAVAQLHYGLALRQFHADYAKALPYLKYAVESGEEGTQEAFFYLSLGETMQRLSMKSEALEVYGKGVAKGFFASLYQRSLYNEPRLRAQPFWQPKETGYERQLEKLTLNWRAIRDEGLALLGRSGFFEDEAELLRDKGVWQQYELYAQGRRVKDNCRRAPITCSLLEEFPESAGCRRGQVKFSVMQAKTHVWPHCGPTNCRLRAHLTLAAPEPEKASLRVAEQERTWREGELFIFDDSFEHEVWHNGSQSRLVLILDMWHPQLSAAQRRSLSPI
Protein: Nebulin-related-anchoring protein (N-RAP) (Q86VF7)
Organism: Homo sapiens (Human)
Function: May be involved in anchoring the terminal actin filaments in the myofibril to the membrane and in transmitting tension from the myofibrils to the extracellular matrix.
Subcellular location: Note=Localized at the myotendinous junction in skeletal muscle and at the intercalated disk in cardiac muscle. {ECO:0000269|PubMed:12789664}.
Interaction partners:
- Kelch-like protein 41
- Cysteine and glycine-rich protein 3
- Xin actin-binding repeat-containing protein 2
- Alpha-actinin-2
- Kelch-like protein 40
- Leiomodin-2
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- E3 ubiquitin-protein ligase TRIM63
- Myozenin-2
Sequence:
MNVQPCSRCGYGVYPAEKISCIDQIWHKACFHCEVCKMMLSVNNFVSHQKKPYCHAHNPKNNTFTSVYHTPLNLNVRTFPEAISGIHDQEDGEQCKSVFHWDMKSKDKEGAPNRQPLANERAYWTGYGEGNAWCPGALPDPEIVRMVEARKSLGEEYTEDYEQPRGKGSFPAMITPAYQRAKKANQLASQVEYKRGHDERISRFSTVVDTPELLRSKAGAQLQSDVRYTEDYEQQRGKGSFPAMITPAYQIAKRANELASDVRYHQQYQKEMRGMAGPAIGAEGILTRECADQYGQGYPEEYEEHRGKGSFPAMITPAYQNAKKAHELASDIKYRQDFNKMKGAAHYHSLPAQDNLVLKQAQSVNKLVSEVEYKKDLESSRGHSINYCETPQFRNVSKISKFTSDNKYKENYQNHMRGRYEGVGMDRRTLHAMKVGSLASNVAYKADYKHDIVDYNYPATLTPSYQTAMKLVPLKDANYRQSIDKLKYSSVTDTPQIVQAKINAQQLSHVNYRADYEKNKLNYTLPQDVPQLVKAKTNAKLFSEVKYKEGWEKTKGKGFEMKLDAMSLLAAKASGELASNIKYKEEYEKTKGKAMGTADSRLLHSLQIAKMSSEVEYKKGFEESKTRFHLPMDMVNIRHAKKAQTLASDLDYRKKLHEYTVLPEDMKTQWAKKAYGLQSELQYKADLAWMKGVGWLTEGSLNLEQAKKAGQLVSEKNYRQRVDELKFTSVTDSSQMEHAKKSQELQSGVAYKAGNEQSVHQYTISKDEPLFLQARANAANLSEKLYKSSWENQKAKGFELRLDSLTFLAAKAKRDLASEVKYKEDYERSRGKLIGAKDVQGDSQMSHSLQMSKLQSELEYKKGFEDTKSQCHVSLDMVHLVHARKAQHLATDVGYKTAEHHFTALPTDMKVEWAKKAYGLQSDNQYRADVKWMKGMGWVATGSLNVEQAKKAGELISEKKYRQHPDALKFTSIKDTPEMVQARISYTQAVDRLYREQGENIKHHYTPTADLPEVLLAKLNAMNISETRYKESWSKLRDGGYKLRLDALPFQAAKASGEIISDYKYKEAFEKMKGQMLGSRSLEDDISLAHSVYATSLQSDVNYKKGFEHSKAQFHLPLDMAALVHAKKAQTLASNQDYKHPLPQYTSLAEDLRLSCAKKAHKLQSENLYRSDLNFMRGVACVIPGTLEIEGRKKASELISESKYRQHPHSFKYTAVTDTPNLLHAKFSNQITNERLYKAAGEDARHEYTMTLGLPEFIRAKTNAANLSDARYKESWRNLRAQGYKLTIEALPFQAARASGDIASDFLYRHDFVKERGKLIGPQSVRDDPRIQHCRRMGQLQSELQYRRGATSSQAQFHLPMDMVHLVHAKNAQALASDHDYRTQYHKFTALPEDLKMAWAKKAHALQSELRYKSDLIGMKGIGWLALRSPQMESAKKAGELISETKYRKKPDSIKFTTVVDSPDLVHAKNSYMHCNERMYRSGDAESLHRYTLIPDHPDFTRARLNALHLSDKVYRNSWEQTRAGSYDFRLDAIPFQTARASREIASDFRYKEAFLRDRGLQIGYRSVDDDPRMKHFLNVGRLQSDNEYKKDFAKSRSQFHSSTDQPGLLQAKRSQQLASDVHYRQPLPQPTCDPEQLGLRHAQKAHQLQSDVKYKSDLNLTRGVGWTPPGSYKVEMARRAAELANARGLGLQGAYRGAEAVEAGDHQSGEVNPDATEILHVKKKKALLL
Protein: Structural maintenance of chromosomes protein 6A (Q9FLR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of the SMC5-SMC6 complex that promotes sister chromatid alignment after DNA damage and facilitates double-stranded DNA breaks (DSBs) repair via homologous recombination between sister chromatids.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Note=Associates with chromatin. {ECO:0000250}.
Interaction partners:
- Non-structural maintenance of chromosomes element 4 homolog B
- Non-structural maintenance of chromosomes element 4 homolog A
- Structural maintenance of chromosomes protein 5
- E3 SUMO-protein ligase MMS21
- Non-structural maintenance of chromosomes element 1 homolog
- Sister chromatid cohesion protein SCC2
- Structural maintenance of chromosomes protein 3
- Condensin-1 complex subunit CAP-D2
- Sister chromatid cohesion 1 protein 1
- ARM repeat superfamily protein
Sequence:
MDEHGDHRQSNPFNDQQTSSGKILRIRLENFMCHSNLEIEFGDWVNFITGQNGSGKSAILTALCVAFGCRARGTQRAATLKDFIKTGCSYALVYVELKNQGEDAFKPEIYGDTLIIERRISDSTSLTVLKDHQGRKISSRKEELRELVEHYNIDVENPCVIMSQDKSREFLHSGNDKDKFKFFYKATLLQQVDDILQSIGTKLNSANALLDEMEKTIKPIEKEINELLEKIKNMEHVEEITQQVLHLKKKLAWSWVYDVDRQLKEQNEKIVKFKERVPTCQNKIDRKLGEVESLRVSLTEKKAQVACLIDESTAMKRELECLRQSMKKAAREKIALEEEYHHKCSNIQKIKDRVRRLERQIEDINEMTIRSTQVEQSEIEGKLNQLTVEVEKAESLVSSLKEEENMVMEKASAGGKEKEHIEEMIRDHEKKQRNMNAHINDLKKHQTNKVTAFGGDKVINLLRAIERHHRRFKMPPIGPIGAHVTLINGNRWASAVEQALGNLLNAFIVTDHKDLVALRDCGKEAKYNNLKIIIYDFSRPRLDIPRHMIPQTEHPTILSVLHSENTTVLNVLVDVSCVERHVLAENYEVGKIIAFERRLSHLKDVFTIDGYRMFSRGPVQTTLPPRPRRPTRLCASFDDQIKDLEIEASREQSEIQECRGQKREAEMNLEGLESTMRRLKKQRTQLEKDLTRKELEMQDLKNSVASETKASPTSSVNELHLEIMKFQKEIEEKESLLEKLQDSLKEAELKANELKASYENLYESAKGEIEALEKAEDELKEKEDELHSAETEKNHYEDIMKDKVLPEIKQAETIYKELEMKRQESNKKASIICPESEIKALGPWDGPTPLQLSAQINKINHRLKRENENYSESIDDLRIMHGEKEQKIGKKRKTYKSCREKLKVCKDAVDSRWNKLQRNKDLLKRELTWQFNHHLGKKGISGNIRVSYEDKTLSIEVKMPQDATNSAVRDTRGLSGGERSFSTLCFTLALQNMTEAPIRAMDEFDVFMDAVSRKISLDTLIDFALKQGSQWMFITPHDISMVKSHEKIKKQQMAAPRS
Protein: Angiopoietin-related protein 2 (Angiopoietin-like protein 2) (Q9UKU9)
Organism: Homo sapiens (Human)
Function: Induces sprouting in endothelial cells through an autocrine and paracrine action.
Subcellular location: Secreted.
Interaction partners:
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- Angiopoietin-1 receptor
- Tyrosine-protein kinase receptor Tie-1
Sequence:
MRPLCVTCWWLGLLAAMGAVAGQEDGFEGTEEGSPREFIYLNRYKRAGESQDKCTYTFIVPQQRVTGAICVNSKEPEVLLENRVHKQELELLNNELLKQKRQIETLQQLVEVDGGIVSEVKLLRKESRNMNSRVTQLYMQLLHEIIRKRDNALELSQLENRILNQTADMLQLASKYKDLEHKYQHLATLAHNQSEIIAQLEEHCQRVPSARPVPQPPPAAPPRVYQPPTYNRIINQISTNEIQSDQNLKVLPPPLPTMPTLTSLPSSTDKPSGPWRDCLQALEDGHDTSSIYLVKPENTNRLMQVWCDQRHDPGGWTVIQRRLDGSVNFFRNWETYKQGFGNIDGEYWLGLENIYWLTNQGNYKLLVTMEDWSGRKVFAEYASFRLEPESEYYKLRLGRYHGNAGDSFTWHNGKQFTTLDRDHDVYTGNCAHYQKGGWWYNACAHSNLNGVWYRGGHYRSRYQDGVYWAEFRGGSYSLKKVVMMIRPNPNTFH
Protein: Down syndrome critical region protein 8 (Cancer/testis antigen 25) (CT25) (DCR1-24.0) (Malignant melanoma-associated protein 1) (MMA-1) (Protein MTAG2) (Q96T75)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKEPGPNFVTVRKGLHSFKMAFVKHLLLFLSPRLECSGSITDHCSLHLPVQEILMSQPPEQLGLQTNLGNQESSGMMKLFMPRPKVLAQYESIQFMP