wanglab/gogpt-training-data huggingface dataset:
Protein: Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1) (Q8K4M9)
Organism: Rattus norvegicus (Rat)
Function: Binds phospholipids; exhibits strong binding to phosphatidic acid and weak binding to phosphatidylinositol 3-phosphate. Stabilizes GTP-bound RAB7A on late endosomes/lysosomes and alters functional properties of late endocytic compartments via its interaction with RAB7A. Binds 25-hydroxycholesterol and cholesterol.
Subcellular location: Late endosome {ECO:0000250|UniProtKB:Q9BXW6}. Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes. {ECO:0000250|UniProtKB:Q9BXW6}.
Interaction partners:
- Ras-related protein Rab-7a
- Motile sperm domain-containing protein 2
- Uncharacterized protein.
- Vesicle-associated membrane protein-associated protein A
- Vesicle-associated membrane protein-associated protein B
- StAR-related lipid transfer protein 3
Sequence:
MNTEAEQQLLHHARNGNAEEVRKLLEAMARAEVVADIDCKGRSKSNLGWTPLHLACYFGHKQVVQDLLKAGAKVNMLNDMGDTPLHRAAFTGRKELVMLLLEYNADTTVVNGSGQTAKEATHDKEIRQMLEAVERTQQRKLEELLLGAAREGRTAEVSALLSRPNPPDVNCSDQLGNTPLHCAAYRAHKQCVLKLLRSGADPSLKNKNDQKPLDLAHGTEMKHILVGNKVVHKALKRFEGPLWKSSRFFGWKLFWVVLEHGVLSWYRKQPDAVHNSYRQGCKHLTQAVCTVKPTDGCLFSVRCFDDTVHGFRVPKNSLQQSREKWLEAIEEHSAYSTHYCSQDQVTDDEEEDVASAMDLKESLARAQTCQQRLDREIYNFLKMIKECDVAKDMLPSFLQKADVLSEASRETCVALSDCLNLFTKQEGVRNFKLEQEQEKNKILSEALETLATEHHELERSLVEGSPPVSILSEDEFYDALSGSESEGSLTCLEAVTARAFEENEVPANSGKHRMSEGKDCGGGDALSNGIKKHRTSLPSPMFSRNDFSIWSILRKCIGMELSKITMPVIFNEPLSFLQRLTEYMEHTYLIHKASSFSDPVERMQCVAAFAVSAVASQWERTGKPFNPLLGETYELVRDDLGFRLISEQVSHHPPISAFHAEGLNNDFIFHGSIYPKLKFWGKSVEAEPKGTITLELLEHNEAYTWTNPTCCVHNIIVGKLWIEQYGNVEIINHKTGDKCVLNFKPCGLFGKELHKVEGYIQDKSKKKLCALYGKWTECLYSVDPATFDAYKKNDKKNTEEKKTSKQASTSEESDEMPVPDSESVFVIPGSALLWRIAPRPPNSAQMYNFTSFAMVLNEVDKEMETVIPKTDCRLRPDIRAMENGEIDQASEEKKRLEEKQRAARKNRSKSEEDWKTRWFHQGPNPYSGAQDWIYSGSYWDRNYFNLPDIY
Protein: 4-hydroxyphenylpyruvate dioxygenase-like protein (HPD-like protein) (HPDL) (EC 1.13.11.46) (Glyoxalase domain-containing protein 1) (Q96IR7)
Organism: Homo sapiens (Human)
Function: May have dioxygenase activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:32707086, ECO:0000269|PubMed:34471290}.
Interaction partners:
- Homogentisate 1,2-dioxygenase
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Xylulose kinase
- Tyrosine aminotransferase
- Pyruvate carboxylase, mitochondrial
- Negative elongation factor C/D
Sequence:
MAAPALRLCHIAFHVPAGQPLARNLQRLFGFQPLASREVDGWRQLALRSGDAVFLVNEGAGSGEPLYGLDPRHAVPSATNLCFDVADAGAATRELAALGCSVPVPPVRVRDAQGAATYAVVSSPAGILSLTLLERAGYRGPFLPGFRPVSSAPGPGWVSRVDHLTLACTPGSSPTLLRWFHDCLGFCHLPLSPGEDPELGLEMTAGFGLGGLRLTALQAQPGSIVPTLVLAESLPGATTRQDQVEQFLARHKGPGLQHVGLYTPNIVEATEGVATAGGQFLAPPGAYYQQPGKERQIRAAGHEPHLLARQGILLDGDKGKFLLQVFTKSLFTEDTFFLELIQRQGATGFGQGNIRALWQSVQEQSARSQEA
Protein: Bromodomain PHD finger transcription factor (A0A8I6GFZ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVPNEHIMNVIAIYEVVRNFGNVLRLSPFCFEDFCAALVSQEQCTLMAEMHVALLKAVLREEDTSNTTFGPADLKDSVNSTLYFIDGMTWPEVLRVYCESDKEYHHVLPYQEAEDYPYGPVESKIKVLQFLVDQFLTTNIAREELMSEGVIQYDDHCRVCHKLGDLLCCETCSAVYHLECVKPPLEEVPEDEWQCEVCVAHKVPGVTDCVAEVQKNKPYVRHEPIGYDRSRRKYWFLNRRLIIEEDTENENEKKVWYYSTKVQLAELIDCLDKDYWEAELCRVLEDIREEMQQHMDVTEDLTNKARGSNKSFLAAANEEILDSLRIKRGEDIDCDQNPEDTEKDKNEGENDSSKGAEKSREESEDQSPDKDADGKVLEEEPGQGKPEEPTEVGDKGNSVPANLGDNTRNASSEETPCEGRSPEGWLSETHDSSTAEKKVASELPPDVPEDSHKTCDSSNTSATTASSQPNLENCSSSSSSSELTSSQSDSAKAADDPDIGERDSHTPVSVQEEIGDFRLDKSNGEVSESPGTGKGTSGSTRIITRLRNPESKLSQLKSQQVAAAAHEANKLFKEGKEVLVVNSQGEVSRLSTKKEVVMKGNINNYFKLGQEGKYRVYHNQYSTNSFALNKHQHREDHDKRRHLAHKFCLTPAGEFKWNGSVHGSKVLTISTLRLTITQLESNIPSSFLHPNWASHRANWIKAVQMCSKPREFALALAILECAVKPVVMLPIWRESLGHTRLHRMTSIEREEKEKVKKKEKKQEEEETMQQATWVKYTFPVRHQVWKQKGEEYRVTGYGGWSWISKTHVYRFLPKLPGNTNVNYRKPLEGVKNNMDENKDESDKRKSPRSPKKMKTECDSEKGEARDADSTAGATAGTMELSKLPEKEEHDVKELLDPDNDKPFKEEPMEIDDSVKTESHMNSEESAQVDVVNVSEGFHLRTSYKKKTKSSKLDGLLERRIRQFTLEEKQRLEKLKLESGVKGAGKPPTGAVKSSSEPPVSTKADEGHQGDLLRQEQRSTPSQAGTADLGLGASQSDPLVLGISPPSLSTGKPDPKGQVLDDVSIQSPGPACQGQNSVESDLDARISEATSKGLELSQTKTKVTDSLTDDSKPTSADEGSTLICKSKKPLPQDDCSTAVSSSSKSTLPAPVPKSPRDRDARAFPKAMDLDGRLGGDSEYNSTLENNSGTMYMRDSSEEDMVVQNSNDTTSKRFITPDQGMESTEPTKCQLVSKSTENCDNRLQGKVTEANGKKLGQHQKPEERAVNRCADQVSLRHSADRKNSEARESEKRGQKANKFQINGKDSKAKGYLKGPGMKDVSDGKVMSGAVEPKVNNINKVIPGNIKSLAGKESAVKPFVNGDIIMEEFSEQNTSETNSYSLSSSDAKGNHQDGLHTLPSTKDSASTQVIIPPAPCPDRNSLNQVEDMETEGPEVKKVTPSPITTGEDSNLGKDVMDENGLPSSKDENVNGESQRKTVITEVTTMTSTVATESKTVIKVAKGDKQTVVSSTENCARSTVTTTTTTVTKLSTPSPDSDVDTVSVKEQSKTVVTTTVTDSLSTAGSTLVTSMTVSREYSTRDRVKLMKFSRPKKTRSGTALPSYRKFVTKSSKKSIFVLPNDDLKKLARKGGIREVPCFNYNAKPALDIWPYPSPRPTFGITWRYRLQTVKSLAGVSLMLRLLWASLRWDDMAAKAPPGGGSTRTETSETEITTTEIIKRRDVGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVVIESWVAEEELELWEIRAFAERVEKEKAQAVEQQTKKRLEQQKPAVIAASTTSPTNSTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSATSTAATSATTIASTGQTLHITGSPVTMAGKVITKLPLPANSKIVAVNVPATQGGVVQVQQKVLGIIPSTAGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGMTVIRAPLQQPALGKAVIRTPVTMQPGAPQQVVTQIIRGQPVSTAISASSTASSAPVQKGLTPGAAAGTLQPSAPHSPRPQQGQVKLTMAQLTQLTQGHGGNQGLTVVIQGQGQTTGQLQLIPQGMTVLPGPGQQLMQAAMPNGTVQRFLFTPLSTPVTAVSSSSSSSSTNATATGSGEQKQSKLSPQTQVQPATTLAPTQSSSVSPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAASSHVPSETQPSQAQSSKPLVATQCQPQSSVQGQSPVRVQSPPLTRIRPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILKKRALLDKELQMQVQEELKRDLKMKREREMAQVVQANAAAGPTPSVPAPVPAPAPAPAAPPAPPSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDLCTNWYHGDCVGITEKEAKKMDVYICNDCKRAQEGSSEELYCICRTPYDESQFYIGCDRCQNWFHGRCVGILQSEAELIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPSDSPFYQCAEVLESFFVQKLKGFKASR
Protein: Alpha/beta-glucosidase agdC (EC 3.2.1.20) (EC 3.2.1.21) (Q5AWI5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Glucosidase involved in the degradation of cellulosic biomass. Has both alpha- and beta-glucosidase activity.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Glucoamylase
- Glucoamylase
- Alpha-glucosidase
- Phosphotransferase
- Hexokinase
- Phosphotransferase
- Alpha-glucosidase
- Glycosyl hydrolases family 32 superfamily
- Alpha/beta-glucosidase agdC
- Probable alpha/beta-glucosidase agdC
Sequence:
MAGTLLSWTPLALALMARALSQLPLTDCPGYRVINVEERPRGLTADLTLAGTPCNVYGVDIENLRLETDYDTNQRLHVKIYDADENVYQVPDSVFPRPVVNDQACADENTPELRFSYAEDPFSFAVSRASNDETLFNTTGHNLIFQSQYVNLRTSLPQNPNLYGLGEHSDPLRLNTINYTRTLWNRDAYTIPAGTNLYGAHPMYIDHRGEAGTHGVFLLNSNGMDIKIDKNSDNIQFLEYNILGGVLDFYFFAGPSPKDVSVQYAEVAGLPAMVPYWGLGFHQCRYGYRDIFEVAAVVHNYSEARIPLETMWTDIDYMDHRKVFTLDRERFPLDTVRALVQYLHQRDQHYIVMVDPAVAHSENGAFTRGLEKDVFMRKQDGTLYQGAVWPGATVFPDWFHPNTSDYWINEFALFFNAESGVDIDALWIDMNEAANFCDWPCTDPVAYAEENNLPPEPPAVRPNPSSLPGFPAEFQPVNSNNNNSSRKRETQVVIAARQGFVKVGNDNGNGRRLGLQGRELIDPPYKIANAAGSLSNKTMNTDIFHANGLAEYDTHNLYGTMMSSLSRDAMLYRRPEKRPLVITRSTFAGAGSYVGHWLGDNASTWTKYRISIAQMLAFASIFQIPMVGSDACGFTGNTTEELCSRWATLAAFNPFFRNHNEYGMVSQEFYRWNSVAEAARKAISIRYSLLDYLYTEFHEQTVTGEPFLLPLFFVYPNDPNVVGIDSQFFYGDAILVSPVIEEGKTEVHAYFPGDLFYDWYTGLPLRGNGEVITLTDIGYTDIPLHVRGGKIVPVRTGSAGMNTTTEVRKSGFRLVIAPGLDGRAAGRLYIDDGESLEQTAMVDVVFTYEDGRVSVDGVFTLQTDLRVEAVTVFGDNVVERTIDLPLSGPGGVEL
Protein: Large ribosomal subunit protein uL22B (60S ribosomal protein L17-B) (L20) (YL17) (P46990)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL37B
- Large ribosomal subunit protein eL37A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL34A
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
Sequence:
MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLDQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRISA
Protein: ATP synthase subunit c, chloroplastic (ATP synthase F(0) sector subunit c) (ATPase subunit III) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) (P0C300)
Organism: Oryza sativa subsp. indica (Rice)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
Interaction partners:
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit alpha
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit alpha, chloroplastic
- ATP synthase CF0 subunit I
- ATP synthase subunit b, chloroplastic
- V-type proton ATPase subunit
- ATP synthase subunit beta, chloroplastic
- Uncharacterized protein
- V-ATPase proteolipid subunit C-like domain-containing protein
Sequence:
MNPLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQPEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV
Protein: Peptidyl carrier protein PltL (Q4KCZ1)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- NADH-quinone oxidoreductase subunit C/D
- L-proline--[L-prolyl-carrier protein] ligase
- 1H-pyrrole-2-carbonyl-[peptidyl-carrier protein] chlorinase
- AMP-binding enzyme
- Polyketide synthase PltB
- Non-ribosomal peptide synthetase PvdL
- L-prolyl-[peptidyl-carrier protein] dehydrogenase
- Polyketide synthase PltC
- NADH-quinone oxidoreductase subunit B
- Polyketide synthase/nonribosomal peptide synthetase hybrid RzxA
Sequence:
MDGEEVKEKIRRYIMEDLIGPSAKEDELDDQTPLLEWGILNSMNIVKLMVYIRDEMGVSIPSTHITGKYFKDLNAISRTVEQLKAECA
Protein: C-X-C motif chemokine (A3DTN6)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361149}.
Interaction partners:
Sequence:
MNGKLGAVLALLLVSAALSQGRTLVKMGNELRCQCISTHSKFIHPKSIQDVKLTPSGPHCKNVEIIATLKDGREVCLDPTAPWVQLIVKALMAKAQLNSDAPL
Protein: Cyclin-dependent kinase inhibitor 1 (CDK-interacting protein 1) (Melanoma differentiation-associated protein) (p21) (P39689)
Organism: Mus musculus (Mouse)
Function: May be involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (By similarity). Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36689330}. Nucleus {ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:36689330}.
Interaction partners:
- Cyclin-dependent kinase 2
- G1/S-specific cyclin-D1
- G1/S-specific cyclin-E1
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Cyclin-A2
- Cellular tumor antigen p53
- Cyclin-A1
- Forkhead box protein O3
- G1/S-specific cyclin-E2
Sequence:
MSNPGDVRPVPHRSKVCRCLFGPVDSEQLRRDCDALMAGCLQEARERWNFDFVTETPLEGNFVWERVRSLGLPKVYLSPGSRSRDDLGGDKRPSTSSALLQGPAPEDHVALSLSCTLVSERPEDSPGGPGTSQGRKRRQTSLTDFYHSKRRLVFCKRKP
Protein: LD16758p (Q95RP9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPHTYFIGDHKQMFPHLKERIIVCDKQQSSVVDNVTVINATDLSPLVENTDVKEIKEVVNAQKPVEITHKVAELPNTTQIVSMIATGQVQTSLNGVVVQNGLATTQTNNKAATGEEVPQNIVITTRRQYMLPDDAVVYCNFNQLYKIDPQTLESWVEILKNVPKSVLWLLRFPAVGEQNIKKTVSDFGISPDRVIFSNVAAKEEHVRRGQLADICLDTPLCNGHTTSMDVLWTGTPVVTLPGETLASRVAASQLATLGCPELIARTREEYQNIAIRLGTKKEYLKALRAKVWKARVESPLFDCSQYAKGLEKLFLRMWEKYENGELPDHISAV
Protein: T-complex protein 1 subunit epsilon (TCP-1-epsilon) (CCT-epsilon) (Q9UTM4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Probable T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- Probable T-complex protein 1 subunit eta
- Probable T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit zeta
- Guanine nucleotide-binding protein subunit beta
- Phosducin-like protein C2A9.09
- Probable prefoldin subunit 4
Sequence:
MAGLDNAVMVRDDQGNPFILVRDQEKKRRLHGIDAVKSHILATKTVANIVRTSLGPRGLDKILISPDGEITVTNDGATILDQMEVEHQIAKLLVQLSKSQDDEIGDGTTGVVVLAGALLEQAEALIDKGIHPIRIADGYEKACQVAVKHLDAISDVVDFSPENTTNLFRSAKTSLGSKVVSKAHDHFANIAVDAVLSVADLQRKDVDFELIKVDGKVGGSVDDTKLVKGVVVDKDMSHPQMPHRIENAKIAILTCPFEPPKPKTKHKLDITSVSEFEALQAYEKEKFQEMIKHVKDAGANLVICQWGFDDEANHLLLQNNLPAVRWVGGPEIELIAIATNGRIVPRFEDLSSDKLGSAGIVREVSFGTTRDKILVIEKCANSRAVTVFVRGSNKMIVDEAKRALHDALCVVRNLIRDNRVVYGGGAAEISCSLAVTKEAEKIPGIDQYSMGAFADALDTIPLALAENSGLSSIEALTAVKARHVKENKAYLGIDCLQTGSNDMRKQFVIDPLIGKKQQLLLATQLCRMVLKVNDIIVAGSKDDDYN
Protein: Alkaline serine protease (Q873R3)
Organism: Bionectria ochroleuca (Gliocladium roseum)
Interaction partners:
Sequence:
ATQSNAQHNSTQWLSFRVVPPVASSRMTLGLPVGAVMNCADNSGARNLYIISVKGIGARLNRLPAGGVGDMVMATVKKGKPELRKKVHPAVIVRQAKPWKRFDGVFLYFEDNAGVIVNPKGEMKGSAITGPVGKEAAELWPRIASNSGVVMGDFTUIKGKTEVEVWFGIPHAIRLESARKNAHTPCLHSRLGPQNDGTGIFSVAGLACSAFGLRRVRMIHNRASHQNTLK
Protein: V(D)J recombination-activating protein 1 (RAG-1) [Includes: Endonuclease RAG1 (EC 3.1.-.-); E3 ubiquitin-protein ligase RAG1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase RAG1)] (O13033)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some cases D (diversity), and J (joining) gene segments. In the RAG complex, RAG1 mediates the DNA-binding to the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. RAG2 is not a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in 2 steps: a first nick is introduced in the top strand immediately upstream of the heptamer, generating a 3'-hydroxyl group that can attack the phosphodiester bond on the opposite strand in a direct transesterification reaction, thereby creating 4 DNA ends: 2 hairpin coding ends and 2 blunt, 5'-phosphorylated ends. In addition to its endonuclease activity, RAG1 also acts as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3. Histone H3 monoubiquitination is required for the joining step of V(D)J recombination (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820}.
Interaction partners:
- V
- Transcriptional activator Myb isoform 1
- Runt-related transcription factor
- IKAROS family zinc finger 1
- Cytochrome b
- Forkhead box N1
- CD4-1 molecule
- Tyrosine-protein kinase
- GATA-binding protein 1a.
- Plastin-2
Sequence:
MEKGRWSSEDAPRASMPDELSHPKFSEWKFKLFRVRSMEKAPVQNETPVEKENQPELAMEKTSSQGSVMRLCFGGKSKENVESARGRVDLKLQEIDTHMNLLKNMCRLCGIAIQKAKGPSHEVQGVLEESSRCALRRMGCKLVTWPEVILKVFKVDVTTDMETVHPSLFCHRCWTAAIRGGGFCSFTNTRIPDWKPHTSQCNLCFPKKSSFQRVGRKRTKPLKSAHILPKRFRRDSSESSRVWRQTTENPDGKEWLKLSVQRGQWVKNITRCQRDHLSTKLIPTEVPADLIRAVTCQVCDHLLSDPVQSPCRHLFCRLCIIRYTHALGPNCPTCNQHLNPSHLIKPAKFFLATLSSLPLLCPSEECSDWVRLDSFREHCLNHYREKESQEEQTPSEQNLDGYLPVNKGGRPRQHLLSLTRRAQKHRLRDLKNQVKTFAEKEEGGDVKSVCLTLFLLALRAGNEHKQADELEAMMQGRGFGLHPAVCLAIRVNTFLSCSQYHKMYRTVKATSGRQIFQPLHTLRNAEKELLPGFHQFEWQPALKNVSTSWDVGIIDGLSGWTVSVDDVPADTISRRFRYDVALVSALKDLEEDIMEGLRERALDDSMCTSGFTVVVKESCDGMGDVSEKHGSGPAVPEKAVRFSFTIMSISIRLEGEDDGITIFQEQKPNSELSCRPLCLMFVDESDHETLTAILGPVVAERKAMMESRLIISVGGLLRSFRFFFRGTGYDEKMVREMEGLEASGSTYICTLCDSTRAEASQNMVLHSITRSHDENLERYEIWRKNPFSESADELRDRVKGVSAKPFMETQPTLDALHCDIGNATEFYKIFQDEIGEVYQKPNPSREERRRWRSTLDKQLRKKMKLKPVMRMNGNYARRLMTREAVEAVCELVPSEERREALLKLMDLYLQMKPVWRSTCPSRDCPDQLCQYSYNSQQFADLLSSMFKYRYDGKITNYLHKTLAHVPEIVERDGSIGAWASEGNESGNKLFRRFRKMNARQSKTFELEDILKHHWLYTSKYLQKFMEAHKNSVKAMQATFNPEETPEEADNSLDVPDF
Protein: Large ribosomal subunit protein eL29 (60S ribosomal protein L29) (Cell surface heparin-binding protein HIP) (P47914)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL34
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein eL15
- Small ribosomal subunit protein RACK1
Sequence:
MAKSKNHTTHNQSRKWHRNGIKKPRSQRYESLKGVDPKFLRNMRFAKKHNKKGLKKMQANNAKAMSARAEAIKALVKPKEVKPKIPKGVSRKLDRLAYIAHPKLGKRARARIAKGLRLCRPKAKAKAKAKDQTKAQAAAPASVPAQAPKRTQAPTKASE
Protein: Diamine acetyltransferase 1 (EC 2.3.1.57) (Polyamine N-acetyltransferase 1) (Putrescine acetyltransferase) (Spermidine/spermine N(1)-acetyltransferase 1) (Q7TP41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Ornithine decarboxylase
- Antizyme inhibitor 2
- Spermidine synthase
- Guanidino acid hydrolase, mitochondrial
- Spermidine/spermine N1-acetyl transferase 2
- Amine oxidase
- Diamine oxidase [copper-containing]
- Amine oxidase
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
Sequence:
MTRSVRLELFRNKKLKETKDAHGLEQGPGAQREEKQKTKMAKFKIRPATASDCSDILRLIKELAKYEYMEDQVVLTEKDLLEDGFGEHPFYHCLVAEVPKEHWTPEGHSIVGFAMYYFTYDPWIGKLLYLEDFFVMSDYRGFGIGSEILKNLSQVAMKCRCSSMHFLVAEWNEPSINFYKRRGASDLSSEEGWRLFKIDKEYLLKMAAEE
Protein: Virulence factor mce family protein (O53539)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MIDRLAKIQLSIFAVITVITLSVMAIFYLRLPATFGIGTYGVSADFVAGGGLYKNANVTYRGVAVGRVESVGLNPNGVTAHMRLNSGTAIPSNVTATVRSVSAIGEQYIDLVPPENPSSTKLRNGFRIQRQNTRIGQDVADLLRQAETLLGSLGDTRLRELLHEAFIATNGAGPELARLIESARLLVDEANANYPQVSQLIDQAGPFLQAQIRAGGDIKSLADGLARFTWQLRAADPRLRDTLADAPDAIDEANTAFSGIRPSFPALAASLANLGRVGVIYHKSIEQLLVVFPALFAAIITSAGGVPQDEGAKLDFKIDLHDPPPCMTGFLPPPLVRSPADESVREIPRDMYCKTAQNDPSTVRGARNYPCQEFPGKRAPTVQLCRDPRGYVPVGTNPWRGPPIPYGTEVTDGRNILPPNKFPYIPPGADPDPGVPIVGPPPPGQVAGPGPAPHQPAQPAPPPNDNGPPPPFTSWMPPGYPPEPPQVPYPATIPPPPPPEGTGPPPGPAPGPQPQASGPAYTIYDQLSGAFADPAGGTGIFAPGMTGASSAENWVDLMRDPRQL
Protein: F-box/LRR-repeat protein 15 (D4ABB4)
Organism: Rattus norvegicus (Rat)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SMURF1, thereby acting as a positive regulator of the BMP signaling pathway. Required for dorsal/ventral pattern formation. Also mediates ubiquitination of SMURF2 and WWP2 (By similarity). Required for bone mass maintenance.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
Sequence:
MEPPMEQSGGEQEPGAVRLLDLPWEDVLLPHVLNWVPLRQLLRLQRVSRAFRALVQLHLARLRRFDAAQVGPQIPRAALVRLLRDAEGLQELALAPCHEWLLDEDLVPVLARNPQLRSVALAGCGQLSRRALGALAEGCPRLQRISLAHCDWVDGLALRGLADRCPALEELDLTACRQLKDEAIVYLAQRRGAGLRSLSLAVNANVGDTAVQELARNCPQLEHLDLTGCLRVGSDGVRTLAEYCPALRSLRVRHCHHVAEPSLSRLRKRGVDIDVEPPLHQALVLLQDMAGFAPFVNLQV
Protein: Guanine nucleotide-exchange factor SEC12 (Q8IIK2)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Small GTP-binding protein sar1
- Protein SEY1 homolog
- Syntaxin, Qa-SNARE family
- Protein transport protein SEC23
Sequence:
MNEMKVSYLNYPIYGIGSNKDYVVTSGGGGGKNYGIEDMLDINIFNEKEKKLEVVWSTTEQRGVVDSIIYVEKYNIWLGSVKNECILFEINEETGPNILLTFVTDFNERNARQVVVKFSSKDDLILTGGEDKTLRLWKLNFVKREKENKDDIKGDNKKGNDNKTNEDNKKDNDKKTNEDKKKDNDNKTNEDKKKDNDNKTDDDNYIAVNNNLYLDKNKSVEHLGDFVGHDDSIKDCDISFDEKIVCTCSSDHSLKIWDTNSFVNLHTEQMKSPQNKNDKLNFRCCKFLNHSNSFKDFTYTLLTTAYTPRGSSYLIIWKVYYNDKKEQFTFTKDKFIWINDRPCCNIAVSTNQKFIALGFSTGALKIYNSKFYLLAHYKKHELPITAMCFIKDDNYLLSAGADYTISTLHINSFMFRYLRKFGRFIIYFLLLFFISIILLDSFNVGYDLRISSLFHNKAYTNITKKKRNYNVDPKKNKVIMDMDEL
Protein: Serine/threonine-protein kinase/endoribonuclease IRE1 (Endoplasmic reticulum-to-nucleus signaling 1) [Includes: Serine/threonine-protein kinase (EC 2.7.11.1); Endoribonuclease (EC 3.1.26.-)] (P32361)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:8358794}; Single-pass type I membrane protein {ECO:0000269|PubMed:8358794}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Transcriptional activator HAC1
- tRNA ligase
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- Phosphatase DCR2
- Heat shock protein 70 homolog LHS1
- Protein disulfide-isomerase
- DnaJ-related protein SCJ1
- Endoplasmic oxidoreductin-1
- Ubiquitin-conjugating enzyme E2 7
Sequence:
MRLLRRNMLVLTLLVCVFSSIISCSIPLSSRTSRRQIVEDEVASTKKLNFNYGVDKNINSPIPAPRTTEGLPNMKLSSYPTPNLLNTADNRRANKKGRRAANSISVPYLENRSLNELSLSDILIAADVEGGLHAVDRRNGHIIWSIEPENFQPLIEIQEPSRLETYETLIIEPFGDGNIYYFNAHQGLQKLPLSIRQLVSTSPLHLKTNIVVNDSGKIVEDEKVYTGSMRTIMYTINMLNGEIISAFGPGSKNGYFGSQSVDCSPEEKIKLQECENMIVIGKTIFELGIHSYDGASYNVTYSTWQQNVLDVPLALQNTFSKDGMCIAPFRDKSLLASDLDFRIARWVSPTFPGIIVGLFDVFNDLRTNENILVPHPFNPGDHESISSNKVYLDQTSNLSWFALSSQNFPSLVESAPISRYASSDRWRVSSIFEDETLFKNAIMGVHQIYNNEYDHLYENYEKTNSLDTTHKYPPLMIDSSVDTTDLHQNNEMNSLKEYMSPEDLEAYRKKIHEQISRELDEKNQNSLLLKFGSLVYRIIETGVFLLLFLIFCAILQRFKILPPLYVLLSKIGFMPEKEIPIVESKSLNCPSSSENVTKPFDMKSGKQVVFEGAVNDGSLKSEKDNDDADEDDEKSLDLTTEKKKRKRGSRGGKKGRKSRIANIPNFEQSLKNLVVSEKILGYGSSGTVVFQGSFQGRPVAVKRMLIDFCDIALMEIKLLTESDDHPNVIRYYCSETTDRFLYIALELCNLNLQDLVESKNVSDENLKLQKEYNPISLLRQIASGVAHLHSLKIIHRDLKPQNILVSTSSRFTADQQTGAENLRILISDFGLCKKLDSGQSSFRTNLNNPSGTSGWRAPELLEESNNLQCQVETEHSSSRHTVVSSDSFYDPFTKRRLTRSIDIFSMGCVFYYILSKGKHPFGDKYSRESNIIRGIFSLDEMKCLHDRSLIAEATDLISQMIDHDPLKRPTAMKVLRHPLFWPKSKKLEFLLKVSDRLEIENRDPPSALLMKFDAGSDFVIPSGDWTVKFDKTFMDNLERYRKYHSSKLMDLLRALRNKYHHFMDLPEDIAELMGPVPDGFYDYFTKRFPNLLIGVYMIVKENLSDDQILREFLYS