wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein eS10 (40S ribosomal protein S10A) (A0A1D8PI15)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein RACK1
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein eL18
Sequence:
MLIPKEDRKKIHQYLFQEGVVVAKKDFNQPKHDEIDTRNLFVIKALQSLTSKGYVKTQFSWQYYYYTLTDEGVEFLRTELNIPEGILPLTRLKNAPAERPRPSRGGPRRGGYRGRARD
Protein: Phytase AppA (EC 3.1.3.-) (6-phytase) (Histidine acid phosphatase phytase) (HAP phytase) (Myo-inositol hexakisphosphate phosphohydrolase) (Phosphoanhydride phosphatase) (EC 3.6.1.-) (pH 2.5 acid phosphatase) (Acid phosphatase) (EC 3.1.3.-) (P07102)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of phytate (or myo-inositol hexakisphosphate, an indigestible organic form of phosphorus that is found in many plant tissues) to myo-inositol and inorganic phosphate. Dephosphorylates phytate in a stereospecific way by sequential removal of phosphate groups to produce myo-inositol 2-monophosphate. Also shows phosphoanhydride phosphatase activity and hydrolyzes the distal phosphoryl residues of GTP, the 5'-beta-phosphoryl residue of the regulatory nucleotide ppGpp and tripolyphosphates. Does not split most phosphomonoesters with the exception of the synthetic substrate p-nitrophenyl phosphate (pNPP), 2,3-bisphosphoglycerate and fructose 1,6-bisphosphate.
Subcellular location: Periplasm {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904}.
Interaction partners:
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Phosphoenolpyruvate synthase regulatory protein
- Riboflavin synthase
- 5-amino-6-
- FMN reductase
- Class B acid phosphatase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- NAD
- 5-amino-6-
Sequence:
MKAILIPFLSLLIPLTPQSAFAQSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTWPVKLGWLTPRGGELIAYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADVDERTRKTGEAFAAGLAPDCAITVHTQADTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTGHRQTAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKVSADNVSLTGAVSLASMLTEIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFYLLQRTPEVARSRATPLLDLIKTALTPHPPQKQAYGVTLPTSVLFIAGHDTNLANLGGALELNWTLPGQPDNTPPGGELVFERWRRLSDNSQWIQVSLVFQTLQQMRDKTPLSLNTPPGEVKLTLAGCEERNAQGMCSLAGFTQIVNEARIPACSL
Protein: Insulin-like growth factor 2 mRNA-binding protein 3 (IGF2 mRNA-binding protein 3) (IMP-3) (mIMP-3) (IGF-II mRNA-binding protein 3) (VICKZ family member 3) (Q9CPN8)
Organism: Mus musculus (Mouse)
Function: RNA-binding factor that may recruit target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation (By similarity). Binds to beta-actin/ACTB and MYC transcripts (By similarity). Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:11288142, ECO:0000269|PubMed:12921532}. Cytoplasm {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:O00425}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:O00425}. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules. {ECO:0000250}.
Interaction partners:
- Insulin-like growth factor 2
- YTH domain-containing family protein 1
- Insulin-like growth factor 2 mRNA-binding protein 1
- YTH domain-containing protein 1
- Heterogeneous nuclear ribonucleoproteins A2/B1
- N
- N
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Alpha-ketoglutarate-dependent dioxygenase FTO
- ELAV-like protein 1
Sequence:
MNKLYIGNLSDHAGPADLESVFKDAKIPVAGPFLVKTGYAFVDCPDEGWALKAIEALSGKMELHGKPMEVEHSVPKRQRIRKLQIRNIPPHLQWEVLDSLLVQYGVVESCEQVNTDSETAVVNVTYSSKDQARQALDKLNGFQLENFTLKVAYIPDETAAQQNPSPQLRGRRGPGQRGSSRQASPGSVSKQKPCDLPLRLLVPTQFVGAIIGKEGATIRNITKQTQSKIDVHRKENTGAAEKSITILSTPEGTSAACKSILEIMHKEAQDIKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQELTLYNPERTITVKGSVETCAKAEEEIMKKIRESYENDIASMNLQAHLIPGLNLNALGLFPPTSGMPPPTSGPPSTLTPPYPQFEQSETETVHLFIPALSVGAIIGKQGQHIKQLSRFAGASIKIAPAEAPDAKVRMVIITGPPEAQFKAQGRIYGKIKEENFVSPKEEVKLEAHIRVPSFAAGRVIGKGGKTVNELQSLSSAEVVVPRDQTPDENDQVVVKITGHFYACQVAQRKIQEILTQVKQHQQQKALQSGPPQSRRK
Protein: Centromere protein O (CENP-O) (Interphase centromere complex protein 36) (Q9BU64)
Organism: Homo sapiens (Human)
Function: Component of the CENPA-CAD (nucleosome distal) complex, a complex recruited to centromeres which is involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. May be involved in incorporation of newly synthesized CENPA into centromeres via its interaction with the CENPA-NAC complex. Modulates the kinetochore-bound levels of NDC80 complex.
Subcellular location: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex.
Interaction partners:
- Centromere protein Q
- Centromere protein H
- Centromere protein R
- Centromere protein U
- Centromere protein K
- Centromere protein T
- Centromere protein I
- Centromere protein L
- Centromere protein N
- Centromere protein P
Sequence:
MEQANPLRPDGESKGGVLAHLERLETQVSRSRKQSEELQSVQAQEGALGTKIHKLRRLRDELRAVVRHRRASVKACIANVEPNQTVEINEQEALEEKLENVKAILQAYHFTGLSGKLTSRGVCVCISTAFEGNLLDSYFVDLVIQKPLRIHHHSVPVFIPLEEIAAKYLQTNIQHFLFSLCEYLNAYSGRKYQADRLQSDFAALLTGPLQRNPLCNLLSFTYKLDPGGQSFPFCARLLYKDLTATLPTDVTVTCQGVEVLSTSWEEQRASHETLFCTKPLHQVFASFTRKGEKLDMSLVS
Protein: Protein huluwa (A0A1L8I316)
Organism: Xenopus laevis (African clawed frog)
Function: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1). Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degradation of axin (axin1 and axin2). Axin degradation results in stabilization and nuclear translocation of beta-catenin (ctnnb1) for activating organizer-specific target gene expression (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:E9QDC5}; Single-pass membrane protein {ECO:0000255}. Note=Enriched on the plasma membrane of blastomeres only in a small region in which the dorsal organizer will form. {ECO:0000250|UniProtKB:E9QDC5}.
Interaction partners:
- SH2B adapter protein 2
- SH2B adapter protein 2
Sequence:
MVTLSPAYLPSDGGTQAASAAPSVEENWVVQPSLTLLVLLLVPCVLLLFFLNCFLLFHRLPAFSLRKRASRRKVGQYPCVRVGHSGQARLEPPYMLSPGVVLREGRLGSDTISQGFEATLALEEGVCGRQNTPQSRGSCCQGGSIPSDQICCSPRPRCATPLPCCAPRRAWNAPAYVKKRLRPKVWKVREDELGSSCELDTRHNHVPPNTPAADNALGVTPKVKFCHTSSTQRKSHVGMVPFTLGGSELLEDPSVIPREDTAEHLDASSSLPGPGLDSDFGVSAGISLHILSSDSDSGSQSWTSGMEWDYYDPCYMRRNRLRRDARHNRHLPMMCSKQYWI
Protein: Lymphokine-activated killer T-cell-originated protein kinase (EC 2.7.12.2) (Cancer/testis antigen 84) (CT84) (MAPKK-like protein kinase) (Nori-3) (PDZ-binding kinase) (Spermatogenesis-related protein kinase) (SPK) (T-LAK cell-originated protein kinase) (Q96KB5)
Organism: Homo sapiens (Human)
Function: Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage.
Interaction partners:
- Cyclin-dependent kinase 1
- Disks large-associated protein 5
- Baculoviral IAP repeat-containing protein 5
- Dual specificity protein kinase TTK
- Maternal embryonic leucine zipper kinase
- G2/mitotic-specific cyclin-B1
- Kinetochore protein Nuf2
- Cell division cycle protein 20 homolog
- DNA topoisomerase 2-alpha
- Centrosomal protein of 55 kDa
Sequence:
MEGISNFKTPSKLSEKKKSVLCSTPTINIPASPFMQKLGFGTGVNVYLMKRSPRGLSHSPWAVKKINPICNDHYRSVYQKRLMDEAKILKSLHHPNIVGYRAFTEANDGSLCLAMEYGGEKSLNDLIEERYKASQDPFPAAIILKVALNMARGLKYLHQEKKLLHGDIKSSNVVIKGDFETIKICDVGVSLPLDENMTVTDPEACYIGTEPWKPKEAVEENGVITDKADIFAFGLTLWEMMTLSIPHINLSNDDDDEDKTFDESDFDDEAYYAALGTRPPINMEELDESYQKVIELFSVCTNEDPKDRPSAAHIVEALETDV
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 2 (PP4R2) (P38193)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the histone H2A phosphatase complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator 2
- Serine/threonine-protein phosphatase PP1-1
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Protein phosphatase PP2A regulatory subunit A
- Serine/threonine-protein phosphatase PP2A-like PPG1
- Protein phosphatase PP2A regulatory subunit B
- Serine/threonine-protein phosphatase 2A activator 1
- Serine/threonine-protein phosphatase 2B catalytic subunit A2
Sequence:
MSSTMLDDVDNNMMGIKSISLYELLSDVVKQGDKTRLVTAGPEQVLPDLIRHITETIPFDLFINLKNEMNDARNLVTRLNWLGKFLNDNFLQNHTFPFTILRICELCYDPFKYYKINELEKFVNALEKCCMVTSSWQVFDKTHGEKQEDDKEKDINFIKNQEDVSLMKIPWMTENNTRELAPFIREIDSIMSVNLGYDDEDEEEGFFDGDEDREMGNKSKRNVLLKDENFMVEEYYEDDCGINDDNSDNKGQNCQSDVTKNNSDDEDDDDNDDDYREDGADEDDEDDDHMGSTDDDEDDDEDRQAGESTKVQNFDKKNETPRKRKPTDLDNFEYDESPSFTNMDLTTPKKYKHTATGRFSIIESPSSSLLNAMDGSNEISSSQEEEKEDAHENHEGRSEGLLPGDELVSPSMSSSQEDKMVAIAGITYRENISSPLGKKSR
Protein: Sarcolipin (O00631)
Organism: Homo sapiens (Human)
Function: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesis (By similarity).
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Phospholamban
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Sarcoplasmic/endoplasmic reticulum calcium ATPase regulator DWORF
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 11
- Myosin-7
- Creatine kinase M-type
Sequence:
MGINTRELFLNFTIVLITVILMWLLVRSYQY
Protein: Hematopoietic cell-specific Lyn substrate 1 (E7EVW7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MWKSVVGHDVSVSVETQGDDWDTDPDFVNDISEKEQRWGAKTIEGSGRTEHINIHQLRNKVSEEHDVLRKKEMESGPKASHGYGGRFGVERDRMDKSAVGHEYVAEVEKHSSQTDAAKGFGGKYGVERDRADKSAVGFDYKGEVEKHTSQKDYAKGFGGQYGIQKDRVDKSAVGFNEMEAPTTAYKKTTPIEAASSGTRGLKAKFESMAEEKRKREEEEKAQQVARRQQERKAVTKRSPEAPQPVIAMEEPAVPAPLPKKISSEAWPPVGTPPSSESEPVRTSREHPVPLLPIRQTLPEDNEEPPALPPRTLEGLQVEEEPVYEAEPEPEPEPEPEPENDYEDVEEMDRHEQEDEPEGDYEEVLEPEDSSFSSALAGSSGCPAGAGAGAVALGISAVAVYDYQGEGSDELSFDPDDVITDIEMVDEGWWRGRCHGHFGLFPANYVKLLE
Protein: Transforming acidic coiled-coil protein, isoform E (Transforming acidic coiled-coil protein, isoform F) (Transforming acidic coiled-coil protein, isoform G) (Transforming acidic coiled-coil protein, isoform H) (Q86BB4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: Recombination initiation protein NBS1, putative (Q57X11)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Endo/exonuclease Mre11
- Protein artemis
- DNA repair protein RAD50
- non-specific serine/threonine protein kinase
- Exonuclease, putative
- BRCT domain-containing protein
- FHA domain-containing protein
- Replication Factor A 28 kDa subunit, putative
- Helicase-like protein
- Helicase, putative
Sequence:
MHIIEVNHGAGELHRYLLLPDAAYTVGRKECHILLPTGDPSISRHHANIQVGVMQSRALTDPSVLTAEVSLQDNSKHGTLVNDEHVGRGNCRYIYTEDSIKFGKKVTARVVSVRIVLVESSQLLHDERKALRNVALLLGALIVQEPAPLLLDFFDMRLCCTAFLYITHNGYTVTPETLLAQQRGYHITTVKYLQSLENALSEDCARGMEELPQPTAAQPGDTSFQVTEYMRPAKVFYDIHEFLLSKPLPNKLLRSYTFVFPDVEIMEKYEVLLKHCGAVVAHQPGECPSEWQSLDPDSTSVIVAGDDMFFKVKRVALTKPERNGTPESEETNGGNRRASALGEDPKTSVYVSLYENGFVIIPEKNIMRAAFTGNPLEINGRPSAPYLARSERDTFRSPSPMVRAPSHGRTSNNHVGTLPCRGASADPVVMAAEGDEKPPRFTVSPPPRRASSVSDGAAKSTGVRVLQELEGNILRVVDVNRLGGEGENDGNACLSKSTSSFGGGGGGTSEVTPTSRKKHKRKPSASRASEEGSQVRAASVDSSSARSQGQYRDKSPEGLCPSWEKQGAVVVHTAEQLWKTEGGRISSSRARMSAYKMSRQSSFLTSATPSSVGAKPHVSTEKHGSEDGQPSQPRSTPSRSMRSVSPLTKRSVVGQSASRRLAPRQALTKLFPCDELGSHSTLGGTSIFDVTFCHTARCESSGRHAKRQLLTHWHRTVAKDKVRETKSARLPASPLRSFSPLFQRYNSGTGSSRRGAGSRGSSAQKADGGRGERYAGLFSSSVSSSNGASAALLAQQQDVTIRKRCEEFLRKVLTPLNTEVDTICKLIMKQGYLDAESKKKLEIGTESLIKFLTYIQRVETSIPPAQSTESTRTVTNQVRQKSLLLRRRIKGAYESVKAEIPPWMNQLREVLSVRPLVV
Protein: Cytochrome P450 90A3 (OsCYP90A3) (EC 1.14.99.-) (Protein CONSTITUTIVE PHOTOMORPHOGENESIS AND DWARFISM 1) (OsCPD1) (Steroid 23-alpha-hydroxylase) (Q2RAP4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the C23-alpha-hydroxylation step in brassinosteroid biosynthesis (Probable). Converts 6-deoxocathasterone (6-deoxoCT) to 6-deoxoteasterone (6-deoxoTE) in the late C6-oxidation pathway and cathasterone (CT) to teasterone (TE) in the early C6-oxidation pathway of brassinolide (BL) biosynthesis (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Os10g0397400 protein
- Cytochrome P450 724B1
- Steroid
- Steroid 5-alpha-reductase DET2
- Steroid 5-alpha-reductase DET2
- Nitrate reductase
- Nitrate reductase 1
- Nitrate reductase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Cytochrome P450 90D2
Sequence:
MAAAALLLLAAAAAIVVVAMVLRWLLLLGGPAAGRLGKRALMPPGSTGLPLIGETLRLISAYKTPNPEPFIDERVARHGGVFTTHVFGERTVFSADPAFNRLLLAAEGRAVHSSYPSSIATLLGARSLLLTRGAAHKRLHSLTLTRLGRPASPPLLAHIDRLVLATMRQWEPAATVRLMDEAKKITFNLTVKQLVSIEPGPWTESLRREYVKLIDGFFSIPFPLANLLPFTTYGQALKARKKVAGALREVIKKRMEEKAENGGSIGDDEGKKEKKDMVEELLEAEGGSFSEEEMVDFCLSLLVAGYETTSMLMTLAVKFLTETPAALAELKEEHANIRDMKGKKQPLEWSDYKSMPFTQCVINETLRVGNIISGVFRRANTDIHYKDYTIPKGCKIFASFRAVHLNNEHYENARTFNPWRWQINNKLQNAVGANIFTPFGGGPRLCPGYELARVVVSIFLHHLVTRFSWEETEEDRLVFFPTTRTLKGYPINLRLLSESIC
Protein: Phosphatidylinositol-glycan biosynthesis class W protein (PIG-W) (EC 2.3.-.-) (Q7Z7B1)
Organism: Homo sapiens (Human)
Function: Required for the transport of GPI-anchored proteins to the plasma membrane. Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7TSN4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TSN4}.
Interaction partners:
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
- Phosphatidylinositol-glycan-specific phospholipase D
- GPI alpha-1,6-mannosyltransferase 2
- GPI ethanolamine phosphate transferase 3, catalytic subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
- Acyltransferase PGAP2
- GPI alpha-1,2-mannosyltransferase 3
- GPI-anchor transamidase component PIGT
Sequence:
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTDFVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNISLESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAMVCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFFTIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLNANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVNVEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTNKKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVVNLYMFSNCLIVYVLYLQDKTVQFW
Protein: Pappalysin-2 (EC 3.4.24.-) (Pregnancy-associated plasma protein A2) (PAPP-A2) (Pregnancy-associated plasma protein E1) (PAPP-E) (Q9BXP8)
Organism: Homo sapiens (Human)
Function: Metalloproteinase which specifically cleaves insulin-like growth factor binding protein (IGFBP)-5 at the '163-Ser-|-Lys-164' bond. Shows limited proteolysis toward IGFBP-3.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Insulin-like growth factor-binding protein 5
- Insulin-like growth factor-binding protein 4
- Insulin-like growth factor 1
- Insulin-like growth factor 2
Sequence:
MMCLKILRISLAILAGWALCSANSELGWTRKKSLVEREHLNQVLLEGERCWLGAKVRRPRASPQHHLFGVYPSRAGNYLRPYPVGEQEIHHTGRSKPDTEGNAVSLVPPDLTENPAGLRGAVEEPAAPWVGDSPIGQSELLGDDDAYLGNQRSKESLGEAGIQKGSAMAATTTTAIFTTLNEPKPETQRRGWAKSRQRRQVWKRRAEDGQGDSGISSHFQPWPKHSLKHRVKKSPPEESNQNGGEGSYREAETFNSQVGLPILYFSGRRERLLLRPEVLAEIPREAFTVEAWVKPEGGQNNPAIIAGVFDNCSHTVSDKGWALGIRSGKDKGKRDARFFFSLCTDRVKKATILISHSRYQPGTWTHVAATYDGRHMALYVDGTQVASSLDQSGPLNSPFMASCRSLLLGGDSSEDGHYFRGHLGTLVFWSTALPQSHFQHSSQHSSGEEEATDLVLTASFEPVNTEWVPFRDEKYPRLEVLQGFEPEPEILSPLQPPLCGQTVCDNVELISQYNGYWPLRGEKVIRYQVVNICDDEGLNPIVSEEQIRLQHEALNEAFSRYNISWQLSVHQVHNSTLRHRVVLVNCEPSKIGNDHCDPECEHPLTGYDGGDCRLQGRCYSWNRRDGLCHVECNNMLNDFDDGDCCDPQVADVRKTCFDPDSPKRAYMSVKELKEALQLNSTHFLNIYFASSVREDLAGAATWPWDKDAVTHLGGIVLSPAYYGMPGHTDTMIHEVGHVLGLYHVFKGVSERESCNDPCKETVPSMETGDLCADTAPTPKSELCREPEPTSDTCGFTRFPGAPFTNYMSYTDDNCTDNFTPNQVARMHCYLDLVYQQWTESRKPTPIPIPPMVIGQTNKSLTIHWLPPISGVVYDRASGSLCGACTEDGTFRQYVHTASSRRVCDSSGYWTPEEAVGPPDVDQPCEPSLQAWSPEVHLYHMNMTVPCPTEGCSLELLFQHPVQADTLTLWVTSFFMESSQVLFDTEILLENKESVHLGPLDTFCDIPLTIKLHVDGKVSGVKVYTFDERIEIDAALLTSQPHSPLCSGCRPVRYQVLRDPPFASGLPVVVTHSHRKFTDVEVTPGQMYQYQVLAEAGGELGEASPPLNHIHGAPYCGDGKVSERLGEECDDGDLVSGDGCSKVCELEEGFNCVGEPSLCYMYEGDGICEPFERKTSIVDCGIYTPKGYLDQWATRAYSSHEDKKKCPVSLVTGEPHSLICTSYHPDLPNHRPLTGWFPCVASENETQDDRSEQPEGSLKKEDEVWLKVCFNRPGEARAIFIFLTTDGLVPGEHQQPTVTLYLTDVRGSNHSLGTYGLSCQHNPLIINVTHHQNVLFHHTTSVLLNFSSPRVGISAVALRTSSRIGLSAPSNCISEDEGQNHQGQSCIHRPCGKQDSCPSLLLDHADVVNCTSIGPGLMKCAITCQRGFALQASSGQYIRPMQKEILLTCSSGHWDQNVSCLPVDCGVPDPSLVNYANFSCSEGTKFLKRCSISCVPPAKLQGLSPWLTCLEDGLWSLPEVYCKLECDAPPIILNANLLLPHCLQDNHDVGTICKYECKPGYYVAESAEGKVRNKLLKIQCLEGGIWEQGSCIPVVCEPPPPVFEGMYECTNGFSLDSQCVLNCNQEREKLPILCTKEGLWTQEFKLCENLQGECPPPPSELNSVEYKCEQGYGIGAVCSPLCVIPPSDPVMLPENITADTLEHWMEPVKVQSIVCTGRRQWHPDPVLVHCIQSCEPFQADGWCDTINNRAYCHYDGGDCCSSTLSSKKVIPFAADCDLDECTCRDPKAEENQ
Protein: Sad1 and UNC84 domain containing 1 (Unc-84 homolog A (C. elegans)) (Q5U2W0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus inner membrane {ECO:0000256|ARBA:ARBA00004540}.
Interaction partners:
Sequence:
MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHRLEPVFDSPRMSRRSLRLITTTAAYSSGDGQTVDTHISTSRATPAKGRETRTVKQRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAVHGPTSRVYSRDRTLRPRKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGFSLWGQGNFFSLLPMLNWTAMQPAQRVDNPKDMHRPGPLSPSPPLKVDPMASQWPQESDMGQKIASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKDMVGQHLQEIGSIEPPDAKTDFLTLHHDHEVRLSSLEDVLRKLTEKSEAIQKELEETKLRAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLRSSCEQADARIQETVQLMFSEDQPGGSLEWLLQKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAMSQAGISGITEAQAHIIVNNALRLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPRDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQGFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
Protein: tRNA(His) guanylyltransferase (EC 2.7.7.79) (tRNA-histidine guanylyltransferase) (P53215)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage.
Interaction partners:
- Histidine--tRNA ligase, mitochondrial
- CCA tRNA nucleotidyltransferase, mitochondrial
- Methionine--tRNA ligase, mitochondrial
- Multisite-specific tRNA:
Sequence:
MANSKFGYVRQFETHDVILPQCYIVVRIDGKKFHEFSKFYEFAKPNDENALKLMNACAKNLVLKYKNDIILAFGESDEYSFILKSSTTLFNRRKDKLATLFGSFFTSNYVALWAKFFPEKPLNIKHLPYFDSRCVAYPNLQTIKDYLSWRYVDTHINNLYNTTFWQLIIKCGLTPQESEKKLCGTFSNEKQEILFSECGINYNNEPEMFKKGSLVTRKGEILHINVIAQIDELFEGY
Protein: Branchpoint-bridging protein (Mud synthetic-lethal 5 protein) (Splicing factor 1) (Zinc finger protein BBP) (Q12186)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have been defined. CC1 is a basal complex dependent only on the 5'-splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5'-splice site region. This protein is involved in CC2 formation where it binds to the snRNP U1-associated protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the MSL5-associated branch point 3' intron splice site. Involved in nuclear retention of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- 56 kDa U1 small nuclear ribonucleoprotein component
- Protein NAM8
- Pre-mRNA-processing protein PRP40
- Pre-mRNA-processing ATP-dependent RNA helicase PRP5
- Splicing factor MUD2
- Pre-mRNA-splicing factor PRP11
- Pre-mRNA-splicing factor PRP21
- Pre-mRNA-splicing factor PRP9
- U1 small nuclear ribonucleoprotein C
- Nuclear cap-binding protein subunit 2
Sequence:
MSFRRINSRYFENRKGSSMEEKKAKVPPNVNLSLWRKNTVESDVHRFNSLPSKISGALTREQIYSYQVMFRIQEITIKLRTNDFVPPSRKNRSPSPPPVYDAQGKRTNTREQRYRKKLEDERIKLVEIALKTIPYFVPPDDYKRPTKFQDKYYIPVDQYPDVNFVGLLLGPRGRTLRKLQEDSNCKIAIRGRGSVKEGKNASDLPPGAMNFEDPLHCLIIADSEDKIQKGIKVCQNIVIKAVTSPEGQNDLKRGQLRELAELNGTLREDNRPCPICGLKDHKRYDCPNRKIPNIQGIVCKICGQTGHFSRDCNSSSQRMSRFDRNATVNNSAPIQSNDVHYNSNTHPIQAPKRSRYDNNSTEPPLKFPASSRYAPSPSPPASHISRQAQNVTPTPPPGLTSSSFSSGVPGIAPPPLQSPPESEQPKFSLPPPPGMTTVQSSIAPPPGLSGPPGFSNNMGNDINKPTPPGLQGPPGL