wanglab/gogpt-training-data huggingface dataset:
Protein: Protein BUD31 homolog (O97454)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein crooked neck
- Puff-specific protein Bx42
- RE31520p
- Pre-mRNA-splicing factor syf1 homolog
- Pre-mRNA-splicing factor RBM22
- Protein CWC15 homolog
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor CWC22 homolog
- Pleiotropic regulator 1
- Probable small nuclear ribonucleoprotein G
Sequence:
MPKVRRSRKPPPDGWELIEPTLEELEQKMREAETEPHEGKRITESLWPIFKIHHQKTRYIYDLFYRRKAISRELYDYCLKEKIADGNLIAKWKKSGYENLCCLRCIQTRDTNFGTNCICRVPKCKLEEGRIVECVHCGCRGCSG
Protein: Protein fem-1 homolog C (FEM1c) (FEM1-gamma) (Q96JP0)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1C) complex specifically recognizes proteins with an arginine at the C-terminus: recognizes and binds proteins ending with -Lys/Arg-Xaa-Arg and -Lys/Arg-Xaa-Xaa-Arg C-degrons, such as SIL1 or OR51B2, leading to their ubiquitination and degradation. The CRL2(FEM1C) complex mediates ubiquitination and degradation of truncated MSRB1/SEPX1 selenoproteins produced by failed UGA/Sec decoding. Promotes ubiquitination and degradation of SLBP.
Interaction partners:
- Cullin-2
- Amyloid protein-binding protein 2
- Kelch domain-containing protein 2
- Kelch domain-containing protein 3
- PRAME family member 6
- Kelch domain-containing protein 10
- Elongin-B
- demerged
- Protein zer-1 homolog
- Protein fem-1 homolog B
Sequence:
MDLKTAVFNAARDGKLRLLTKLLASKSKEEVSSLISEKTNGATPLLMAARYGHLDMVEFLLEQCSASIEVGGSVNFDGETIEGAPPLWAASAAGHLKVVQSLLNHGASVNNTTLTNSTPLRAACFDGHLEIVKYLVEHKADLEVSNRHGHTCLMISCYKGHKEIAQYLLEKGADVNRKSVKGNTALHDCAESGSLDIMKMLLMYCAKMEKDGYGMTPLLSASVTGHTNIVDFLTHHAQTSKTERINALELLGATFVDKKRDLLGALKYWKKAMNMRYSDRTNIISKPVPQTLIMAYDYAKEVNSAEELEGLIADPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFKRCINLWKYALDMQQSNLDPLSPMTASSLLSFAELFSFMLQDRAKGLLGTTVTFDDLMGILCKSVLEIERAIKQTQCPADPLQLNKALSIILHLICLLEKVPCTLEQDHFKKQTIYRFLKLHPRGKNNFSPLHLAVDKNTTCVGRYPVCKFPSLQVTAILIECGADVNVRDSDDNSPLHIAALNNHPDIMNLLIKSGAHFDATNLHKQTASDLLDEKEIAKNLIQPINHTTLQCLAARVIVNHRIYYKGHIPEKLETFVSLHR
Protein: Alpha-1A adrenergic receptor (Alpha-1A adrenoreceptor) (Alpha-1C adrenergic receptor) (B0ZBD3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane, caveola {ECO:0000256|ARBA:ARBA00004345}. Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}.
Interaction partners:
Sequence:
MVFLSGNASDSSNCTQPPAPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEVLGYWAFGRVFCNIWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQRRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYLPLAIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAPAGGSGMASAKTKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFKPSETVFKIVFWLGYLNSCINPIIYPCSSQEFKKAFQNVLRIQCLCRKQSSKHALGYTLHPPSQAVEGQHKDMVRIPVGSRETFYRISKTDGVCEWKFFSSMPRGSARITVSKDQSSCTTARTKSRSVTRLECSGMILAHCNLRLPGSRDSPASASQAAGTTGMCHQADATRPS
Protein: Lanosterol synthase (EC 5.4.99.7) (2,3-epoxysqualene--lanosterol cyclase) (Oxidosqualene--lanosterol cyclase) (OSC) (hOSC) (P48449)
Organism: Homo sapiens (Human)
Function: Key enzyme in the cholesterol biosynthesis pathway. Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. Through the production of lanosterol may regulate lens protein aggregation and increase transparency.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14766201, ECO:0000269|PubMed:15525992, ECO:0000269|PubMed:30401459}; Peripheral membrane protein {ECO:0000269|PubMed:14766201, ECO:0000269|PubMed:15525992}.
Interaction partners:
- Squalene monooxygenase
- Lanosterol 14-alpha demethylase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Squalene synthase
- Lathosterol oxidase
- Delta
- Ergosterol biosynthetic protein 28 homolog
- Isopentenyl-diphosphate Delta-isomerase 1
- Methylsterol monooxygenase 1
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
Sequence:
MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYLQSAQSQIHNTCWAMMGLMAVRHPDIEAQERGVRCLLEKQLPNGDWPQENIAGVFNKSCAISYTSYRNIFPIWALGRFSQLYPERALAGHP
Protein: Vitamin B12-binding protein (P37028)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC.
Subcellular location: Periplasm {ECO:0000255|HAMAP-Rule:MF_01000, ECO:0000269|PubMed:11790740}.
Interaction partners:
- Vitamin B12 import ATP-binding protein BtuD
- Vitamin B12 import system permease protein BtuC
- Fe
- Vitamin B12 transporter BtuB
- Fe
- UPF0126 inner membrane protein YadS
- Ferric enterobactin transport system permease protein FepD
- Iron
- Iron
- Fe
Sequence:
MAKSLFRALVALSFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKIEQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALRQLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVLEVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLTSDWFERASPRIILAAQQLCNALSQVD
Protein: Zinc finger protein 587 (Q96SQ5)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAAAVPRRPTQQGTVTFEDVAVNFSQEEWCLLSEAQRCLYRDVMLENLALISSLGCWCGSKDEEAPCKQRISVQRESQSRTPRAGVSPKKAHPCEMCGLILEDVFHFADHQETHHKQKLNRSGACGKNLDDTAYLHQHQKQHIGEKFYRKSVREASFVKKRKLRVSQEPFVFREFGKDVLPSSGLCQEEAAVEKTDSETMHGPPFQEGKTNYSCGKRTKAFSTKHSVIPHQKLFTRDGCYVCSDCGKSFSRYVSFSNHQRDHTAKGPYDCGECGKSYSRKSSLIQHQRVHTGQTAYPCEECGKSFSQKGSLISHQLVHTGEGPYECRECGKSFGQKGNLIQHQQGHTGERAYHCGECGKSFRQKFCFINHQRVHTGERPYKCGECGKSFGQKGNLVHHQRGHTGERPYECKECGKSFRYRSHLTEHQRLHTGERPYNCRECGKLFNRKYHLLVHERVHTGERPYACEVCGKLFGNKHSVTIHQRIHTGERPYECSECGKSFLSSSALHVHKRVHSGQKPYKCSECGKSFSECSSLIKHRRIHTGERPYECTKCGKTFQRSSTLLHHQSSHRRKAL
Protein: RNA-binding (RRM-RBD-RNP motif) domain nuclear transport factor 2 family protein (F4JED3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 24
- Homeodomain-like superfamily protein
- Nuclear transport factor 2 family protein
- RuvB-like helicase
- Seed dormancy control protein
- Myosin heavy chain-related protein
- Ethylene-responsive transcription factor ERF020
- Putative F-box protein At1g26510
- Protein SPIRRIG
- Farnesoic acid carboxyl-O-methyltransferase
Sequence:
MDPRPNTAKVGDEFARQYYNTLQNAPENLYKLYKDKSTISRPGLDGTMRVFTLSKDLKWRSPGSFDSVKITSVTSQDSLKQGILVVVYGYLTFNERPARHFTQVFFLVPQEKGYIVCTDMFRFVDIPEANAAIPPANDVIEEKVPETEGAALRVSEPNHGFDNVPKLSCASEGAAICAKKLPLDATIAFVENAFKQFGEIRRGGVEVRINWHCTGKYAYVEFEEAEAANRAIMASPISIDGYRTYVEKKYAYNKSADTGNGNSQDSQAITEDAHIRVKDLPPNATVALVESVFKQFGPIKKGRIRVINPANSNYWYAFVEFEEADAAKRAIQASPLNVDGHTTYVEQKQPYYEGYYESPSDGPGNIKRGEGVRGSLGNPICNWQKMEEVRGTDVYDLQNWQKIMNQSEEQMKFQEEEGRQYNQNRYTSEEVRGTEGVGLEEEEEEEENQNWEEQRKIQEEEGTESHEASVFLKRLPLDVTFALIEDALKKFGPINAISIIKSGPLYKFAFVDFEKADVANRAIMASPVRICEKNVNVQKKLSAGAGKRYTRPTCRDTSVPLGAESGHREQGSQNRYGSEQVRGTEAFDFWDWQWQKSKEEQSKLQEEEGEIQVDHSWEEEHSKVLEEESKLQEEAVETQVDHSWDYEQIMEEQEEEESKQNQTSYIEDIAAFFSGVL
Protein: Kallikrein related-peptidase 6 (Klk6 protein) (Neurosin) (Q91Y82)
Organism: Mus musculus (Mouse)
Interaction partners:
- Amyloid-beta precursor protein
Sequence:
MPMKMLTMKMLALCLVLAKSAWSEEQEKVVHGGPCLKDSHPFQAALYTSGHLLCGGVLIDPQWVLTAAHCKKPNLQVILGKHNLRQTETFQRQISVDRTIVHPRYNPETHDNDIMMVHLKNPVKFSKKIQPLPLKNDCSEENPNCQILGWGKMENGDFPDTIQCADVHLVPREQCERAYPGKITQSMVCAGDMKEGNDSCQGDSGGPLVCGGRLRGLVSWGDMPCGSKEKPGVYTDVCTHIRWIQNILRNKWL
Protein: HAUS augmin-like complex subunit 6 (Q7Z4H7)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. Promotes the nucleation of microtubules from the spindle through recruitment of NEDD1 and gamma-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18443220, ECO:0000269|PubMed:19029337}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19029337, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 7
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 4
- HAUS augmin-like complex subunit 3
- Protein NEDD1
- Tubulin gamma-1 chain
- Nuclear mitotic apparatus protein 1
Sequence:
MSSASVTAFEKEHLWMYLQALGFEPGPATIACGKIVSHTHLGVNMFDKLNRDAFHIISYFLFQVLDQSLTKEVFKFCWPPFDQKSDTEFRKHCCEWIKRISGECGSSFPQVVGSLFLSPGGPKFIHLMYHFARFVAMKYIKSNSKNSSHHFVETFNIKPQDLHKCIARCHFARSRFLQILQRQDCVTQKYQENAQLSVKQVRNLRSECIGLENQIKKMEPYDDHSNMEEKIQKVRSLWASVNETLMFLEKEREVVSSVLSLVNQYALDGTNVAINIPRLLLDKIEKQMFQLHIGNVYEAGKLNLLTVIQLLNEVLKVMKYERCQADQARLTVDLHYLEKETKFQKERLSDLKHMRYRIKDDLTTIRHSVVEKQGEWHKKWKEFLGLSPFSLIKGWTPSVDLLPPMSPLSFDPASEEVYAKSILCQYPASLPDAHKQHNQENGCRGDSDTLGALHDLANSPASFLSQSVSSSDRNSVTVLEKDTKMGTPKEKNEAISKKIPEFEVENSPLSDVAKNTESSAFGGSLPAKKSDPFQKEQDHLVEEVARAVLSDSPQLSEGKEIKLEELIDSLGSNPFLTRNQIPRTPENLITEIRSSWRKAIEMEENRTKEPIQMDAEHREVLPESLPVLHNQREFSMADFLLETTVSDFGQSHLTEEKVISDCECVPQKHVLTSHIDEPPTQNQSDLLNKKVICKQDLECLAFTKLSETSRMETFSPAVGNRIDVMGGSEEEFMKILDHLEVSCNKPSTNKTMLWNSFQISSGISSKSFKDNDFGILHETLPEEVGHLSFNSSSSSEANFKLEPNSPMHGGTLLEDVVGGRQTTPESDFNLQALRSRYEALKKSLSKKREESYLSNSQTPERHKPELSPTPQNVQTDDTLNFLDTCDLHTEHIKPSLRTSIGERKRSLSPLIKFSPVEQRLRTTIACSLGELPNLKEEDILNKSLDAKEPPSDLTR
Protein: Heat stress transcription factor B-2b (AtHsfB2b) (AtHsf-11) (Heat shock factor protein 7) (HSF 7) (Heat shock transcription factor 7) (HSTF 7) (Q9T0D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Multiprotein-bridging factor 1c
- Chaperone protein ClpB1
- Heat shock protein 90-1
- Dehydration-responsive element-binding protein 2A
Sequence:
MPGEQTGETPTVAGVGGGGAGCSAGNSGGSSGCGAGGGGGGSGGGGGGGGDSQRSIPTPFLTKTYQLVEDPVYDELISWNEDGTTFIVWRPAEFARDLLPKYFKHNNFSSFVRQLNTYGFRKVVPDRWEFSNDCFKRGEKILLRDIQRRKISQPAMAAAAAAAAAAVAASAVTVAAVPVVAHIVSPSNSGEEQVISSNSSPAAAAAAIGGVVGGGSLQRTTSCTTAPELVEENERLRKDNERLRKEMTKLKGLYANIYTLMANFTPGQEDCAHLLPEGKPLDLLPERQEMSEAIMASEIETGIGLKLGEDLTPRLFGVSIGVKRARREEELGAAEEEDDDRREAAAQEGEQSSDVKAEPMEENNSGNHNGSWLELGK
Protein: Homeobox protein vab-15 (Variable abnormal morphology protein 15) (Q09604)
Organism: Caenorhabditis elegans
Function: Probable transcription factor needed for the proper production of touch cell precursors. Involved in specification of lateral neuroblasts. Essential for embryonic morphogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:11333230}.
Interaction partners:
- Protein lin-32
Sequence:
MVSKDEKPKQSGLFSVESLLETPKQKCREDLPKPTPITPKTPMLIPGLHPMTPYFGAQLDPVMIYFAQTGNRLPIVSSDSSPESCASSPLSMQHSLQWLSSQREDSPTSDDAKIQIGLSKCMLRKHKNNRKPRTPFSTQQLISLERKFQSKQYLSIAERAEFSASLQLTETQVKIWFQNRRAKSKRLQEAEVEKVKFAQASAYAAAAVGGAPDPSSILAFYQPQW
Protein: Negative modulator of initiation of replication (P0AFY8)
Organism: Escherichia coli (strain K12)
Function: Negative regulator of replication initiation, which contributes to regulation of DNA replication and ensures that replication initiation occurs exactly once per chromosome per cell cycle. Binds to pairs of hemimethylated GATC sequences in the oriC region, thus preventing assembly of replication proteins and re-initiation at newly replicated origins. Repression is relieved when the region becomes fully methylated. Can also bind to hemimethylated GATC sequences outside of oriC region. Binds, with less affinity, to fully methylated GATC sites and affects timing of replication. May play a role in chromosome organization and gene regulation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00908, ECO:0000269|PubMed:9660922}. Note=Localization is cell cycle-dependent. Localizes at midcell in newborn cells, then migrates in opposite directions toward cell quarter sites and remains tethered there until the cell divides.
Interaction partners:
- Chromosome partition protein MukB
- DNA mismatch repair protein MutH
- Chromosomal replication initiator protein DnaA
- Phosphoglucomutase
- Macrodomain Ter protein
- DnaA regulatory inactivator Hda
- Nucleoid occlusion factor SlmA
- DNA adenine methylase
- Protein MioC
- UPF0208 membrane protein YfbV
Sequence:
MKTIEVDDELYSYIASHTKHIGESASDILRRMLKFSAASQPAAPVTKEVRVASPAIVEAKPVKTIKDKVRAMRELLLSDEYAEQKRAVNRFMLLLSTLYSLDAQAFAEATESLHGRTRVYFAADEQTLLKNGNQTKPKHVPGTPYWVITNTNTGRKCSMIEHIMQSMQFPAELIEKVCGTI
Protein: IP10875p (Transition protein-like 94D, isoform A) (Q8IMZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Histone-like protein 18C
- Testis-enriched HMG-box-containing protein 2, isoform B
- Testis-enriched HMG-box-containing protein 1
- GH11850p
- Protamine A, isoform A
- Protamine-like protein 99C
Sequence:
MGSVLSRSDQPRDSVAYRNFLTVYRNQHKQMSSNDALLSASREWGTLSQAQRNRYANMKDSPKRGTKNITENAAARRKITKKNSRSKRISQRRIQDKGSAYKPLTLNRSYVIRKSLVPSRGFLNLVQFFQEIHSEMPRSLAVKEAVSSWCAMNADQRGIFISDL
Protein: Dof zinc finger protein DOF1.7 (AtDOF1.7) (O82155)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds specifically to a 5'-AA[AG]G-3' consensus core sequence.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Phosphoenolpyruvate carboxylase 3
- At2g34340
- Protein NLP7
- Phosphoenolpyruvate carboxylase 1
- Phosphoenolpyruvate carboxylase 2
- Phosphoenolpyruvate carboxylase 4
Sequence:
MQDLTSAAAYYHQSMMMTTAKQNQPELPEQEQLKCPRCDSPNTKFCYYNNYNLSQPRHFCKNCRRYWTKGGALRNIPVGGGTRKSNKRSGSSPSSNLKNQTVAEKPDHHGSGSEEKEERVSGQEMNPTRMLYGLPVGDPNGASFSSLLASNMQMGGLVYESGSRWLPGMDLGLGSVRRSDDTWTDLAMNRMEKN
Protein: Adenylate kinase 4, mitochondrial (EC 2.7.4.4) (EC 2.7.4.6) (Adenylate kinase 3-like) (GTP:AMP phosphotransferase AK4) (Q9WUR9)
Organism: Mus musculus (Mouse)
Function: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates (By similarity). Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor (By similarity). Also displays broad nucleoside diphosphate kinase activity (By similarity). Plays a role in controlling cellular ATP levels by regulating phosphorylation and activation of the energy sensor protein kinase AMPK (By similarity). Plays a protective role in the cellular response to oxidative stress (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P27144, ECO:0000255|HAMAP-Rule:MF_03170}.
Interaction partners:
- Adenylate kinase 7
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenosine kinase
- Adenylate kinase 9
- Adenylate kinase isoenzyme 5
- Adenylate kinase isoenzyme 1
- Ectonucleoside triphosphate diphosphohydrolase 8
- Ectonucleoside triphosphate diphosphohydrolase 3
- Adenylate kinase 2, mitochondrial
Sequence:
MASKLLRAVILGPPGSGKGTVCERIAQNFGLQHLSSGHLLRENLKTGTEVGDVAKQYLEKGLLVPDHVITRLMMSELETRSAQHWLLDGFPRTLVQAEALDGICDVDLVISLNIPFETLKDRLSRRWIHPSSGRVYNLDFNPPQVQGIDDITGEPLVQQEDDKPEAVAARLRRYKDAAKPVIELYKSRGVLHQFSGTETNRIWPYVYTLFSNKITPIQSKEAY
Protein: Protein KRTCAP2 homolog (Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2) (Oligosaccharyl transferase subunit KCP2) (Q5Q995)
Organism: Ixodes scapularis (Black-legged tick) (Deer tick)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAVSSGTSGMLATCLFMLLFATMQIYKSQLTSSQPMAIVGGFLGSVLFILILTAISNFETHFFGRNFQTKLIPEVVIALVIAMAASGMVHRVCITTCLIFSIVALYYVSRISIKVHGSGAGTATAIPVTKGKKGK
Protein: Mevalonate kinase (MK) (EC 2.7.1.36) (B2RDU6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU363087}.
Interaction partners:
Sequence:
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKRAWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSICRKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKEDLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVPRNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDMNQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQALTSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
Protein: PHD finger protein ALFIN-LIKE 4 (Protein AL4) (O81488)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:19154204}.
Interaction partners:
- Tudor/PWWP/MBT superfamily protein
- Centromere protein O
- AT2G45990 protein
- Uncharacterized protein At4g24700
- Protein trichome birefringence-like 12
- Serine/Threonine-kinase
- Nucleic acid-binding protein
- Cytomatrix protein-like protein
- Protein BIG GRAIN 1-like B
- AT5g05210/K2A11_8
Sequence:
MEAGGAYNPRTVEEVFRDFKGRRAGMIKALTTDVQEFFRLCDPEKENLCLYGHPNEHWEVNLPAEEVPPELPEPVLGINFARDGMAEKDWLSLVAVHSDAWLLAVAFFFGARFGFDKADRKRLFNMVNDLPTIFEVVAGTAKKQGKDKSSVSNNSSNRSKSSSKRGSESRAKFSKPEPKDDEEEEEEGVEEEDEDEQGETQCGACGESYAADEFWICCDLCEMWFHGKCVKITPARAEHIKQYKCPSCSNKRARS
Protein: Hydrophobic surface binding protein A (Q2UGK8)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MEKGGSVFSSRVWGIKRGSNSRFFFGSREARIILSNTQSARRNLTCIQFDLNTMLAKHVLAVLLSVGASAIPFDKRDASAVLADFNTLSTDLSALGSAISSFDGTLNGALGVQQKEGQVETALKQTVSDVKASTAFSAADSTSVTNAVTGLEPSIVNVLNDLVSKKSGFDSVGVTSIVVSDLNSLHDLTGQLSTELQSKVTSGDASTISDEAARLDAEYKKAIAAYS
Protein: Met repressor (Met regulon regulatory protein MetJ) (P0A8U6)
Organism: Escherichia coli (strain K12)
Function: This regulatory protein, when combined with SAM (S-adenosylmethionine) represses the expression of the methionine regulon and of enzymes involved in SAM synthesis. It is also autoregulated.
Subcellular location: Cytoplasm.
Interaction partners:
- Cystathionine gamma-synthase
- 5,10-methylenetetrahydrofolate reductase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- HTH-type transcriptional regulator MetR
- S-adenosylmethionine synthase
- Arginine repressor
- Homoserine O-succinyltransferase
- D-methionine transport system permease protein MetI
- Cystathionine beta-lyase MetC
- Fatty acid metabolism regulator protein
Sequence:
MAEWSGEYISPYAEHGKKSEQVKKITVSIPLKVLKILTDERTRRQVNNLRHATNSELLCEAFLHAFTGQPLPDDADLRKERSDEIPEAAKEIMREMGINPETWEY
Protein: Alpha-mannosidase 2x (EC 3.2.1.114) (Alpha-mannosidase IIx) (Man IIx) (Mannosidase alpha class 2A member 2) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) (Q8BRK9)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Alpha-mannosidase 2
- alpha-1,2-Mannosidase
Sequence:
MKLKKQVTVCGAAIFCVAVFSLYLMLDRVQHDPARHQNGGNFPRSQISVLQNRIEQLEQLLEENHDIISRIKDSVLELTANAEGPPALLPYHTANGSWAVLPEPRPSFFSVSPQDCQFALGGRGQKPELQMLTVSEDLPFDNVEGGVWRQGFDISYSPNDWDTEDLQVFVVPHSHNDPGWIKTFDKYYTEQTQHILNSMVSKLQEDPRRRFLWAEVSFFAKWWDNISAQKRAAVRRLVGNGQLEIATGGWVMPDEANSHYFALVDQLIEGHQWLERNLGATPRSGWAVDPFGHSSTMPYLLRRANLTSMLIQRVHYAIKKHFAATHSLEFMWRQMWDSDSSTDIFCHMMPFYSYDVPHTCGPDPKICCQFDFKRLPGGRINCPWKVPPRAITEANVADRAALLLDQYRKKSRLFRSNVLLVPLGDDFRYDKPQEWDAQFFNYQRLFDFLNSKPEFHVQAQFGTLSEYFDALYKRTGVEPGARPPGFPVLSGDFFSYADREDHYWTGYYTSRPFYKSLDRVLEAHLRGAEILYSLALAHARRSGLAGQYPLSDFALLTEARRTLGLFQHHDAITGTAKEAVVVDYGVRLLRSLVSLKQVIINAAHYLVLGDQETYSFDPGTPFLQMDDSRVSHDALPERTVIRLDSSPRFVVVFNPLEQERLSVVSLLVNSPRVRVLSEEGQPLSVQISVHWSSATDMVPDVYQVSVPVRLPGLGLGVLQLQPDLDGPYTLQSSVRVYLNGVKLSVSRQSAFPVRVVDSGASDFAISNRYMQVWFSGLTGLLKSIRRVDEEQEQQMELEFLVYGTRTSKDKSGAYLFLPDSEAKPYVPKKPPVLRVTEGPFFSEVAVYYEHFHQVIRLYNLPGVEGLSLDMSFQVDIRDYVNKELALRIHTDIDSQGTFFTDLNGFQIQPRQYLKKLPLQANFYPMPVMAYIQDSQRRLTLHTAQALGVSSLGNGQLEVILDRRLMQDDNRGLGQGLKDNKITCNRFRLLLERRTTMSPEVHQEQERSTSYPSLLSHLTSMYLSTPPLVLPVAKRQGTSPALRSFHPLASPLPCDFHLLNLRMLPAEDTLPATDSALILHRKGFDCGLEAKNLGFNCTTSQGKLALGSLFHGLDVTFLQPTSLTLLYPLASPSNSTDISLEPMEISTFRLRLG
Protein: Fermitin family homolog 1 (Kindlin-1) (Unc-112-related protein 1) (P59113)
Organism: Mus musculus (Mouse)
Function: Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Colocalizes with filamentous actin. Constituent of focal adhesions (By similarity). Localized at the basal aspect of skin keratinocytes, close to the cell membrane (By similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By similarity). {ECO:0000250}.
Interaction partners:
- Scaffold protein ILK
- Filamin-binding LIM protein 1
- Integrin beta-1
Sequence:
MLSSGDLTSASWELVVRVDHANGEQQTEITLRVSGDLHIGGVMLKLVEQMNIAQDWSDYALWWEQKRCWLLKTHWTLDKCGVQADANLLFTPQHKMLRLRLPNAKTVRLRVSFSAVVFKAVADICKVLNIRRPEELSLLKPSSDYCKKKKKKEKNSKEPVIEDILNLESSSTSSGSPVSPGLYSKTMTPTYDPINGTPALSTMTWFGDSPLTEQNCSVLAFSQPPPSPDVLADMFQPRSLVDKAKMNAGWLDSSRSLMEQSIQEDEQLQLRFKYYTFFDLNPKYDAVRINQLYEQARWAVLLEEIDCTEEEMLIFAALQYHISKLSQCAEIQDFATKSEVDEVEAALSSLEVTLEGGKADNTLEDITDIPKLADYLKLFRPKKLMLKACKQYWFVFKDTSIAYFKNKELEQGEPIEKLNLRGCEIVPDVNVSGRKFGIKLLIPVADGMNEVYLRCDHEDQYARWMAACILASKGKTMADSSYQPEVISILSFLKMKNRNSSPLVASSLENMDMNPECLVSPCCAKKHKSKQLAARILEAHHNVAQMPLVEAKLQFIQAWQSLPEFGLTYYLVRFKGSKKDDILGVAYNRLIRIDAVTGIPVTTWRFANMKQWNVNWEIRQVAIEFDQNVSIAFTCLSADCKIVHEYIGGYIFLSTRSKDQNETLDEDLFHKLTGGQD