wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform (Phosphorylase kinase alpha M subunit) (Q64649)
Organism: Rattus norvegicus (Rat)
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The alpha chain may bind calmodulin.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Phosphorylase b kinase gamma catalytic chain, skeletal muscle/heart isoform
- Phosphorylase b kinase gamma catalytic chain, liver/testis isoform
- Phosphorylase b kinase regulatory subunit
- Calmodulin-1
- Calmodulin-like protein 3
- Phosphorylase b kinase regulatory subunit
- Calmodulin-like protein 4
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Glycogen phosphorylase, muscle form
Sequence:
MRSRSNSGVRLDSYARLVQQHTILCHQNPVTGLLPASYDQKDAWVRDNVYSILAVWGLGLAYRKNADRDEDKAKAYELEQSVVKLMRGLLHCMIRQVDKVESFKYSQSTKDSLHAKYNTKTCATVVGDDQWGHLQLDATSVYLLFLAQMTASGLHIIHSLDEVNFIQNLVFYIEAAYKTADFGIWERGDKTNQGISELNACSVGMAKAALEALDELDLFGVKGGPQSVIHVLADEVQHCQSILNTLLPRASTSKEVDASLLSVISFPAFAVEDSKLVEITKQEIITKLQGRYGCCRFLRDGYKTPKEDPNRLYYEPAELKLFENIECEWPLFWTYFILDGIFSGNTEQVQEYREALDAVLIKGKNGVPLLPELYSVPPDRVDEEYQNPHTVDRVPMGKLPHMWGQSLYILGNLMAEGFLAPGEIDPLNRRFSTVPKPDVVVQVSILAETEEIKAILKDKGIDVETIAEVYPIRVQPARILSHIYSSLGCNSRMKLSGRPYRLMGVLGTSKLYDIRKTIYTFTPQFIDQQQFYLALDNQMIVEMLRTDLSYLCSRWRMTGQPTITFPISHTMLDEDGASLNSSILAALRKMQDGYFGGARIQTGKLSEFLTTSCCTHLSFMDPGPEGKLYSEDYDEDYDDELDSGNWMDSYDSTRNARCGDEVARYLDHLLAHTGPHPKLTPTSRKGGLDRFRAAVQTTCDLMSLVAKAKELHIQNVHMYLPTKLFQPSRPSLNLLDSPESPQDSQVPSVRVEVHLPRDQSGEVDFQSLVSQLKETSSLQEQADILYMLYTMKGPDWNTELYEEGGSTVRELLSELYVKVGEIRHWGLIRYISGILRKKVEALDEACTDLLSYQKHLTVGLPPEPREKTISAPLPYEALTKLIDEASEGDMNISTLTQEIMVYLAMYMRTQPGLFAEMFRLRIGLIIQVMATELAHSLRCSAEEATEGLMNLSPSAMRNLLHHILSGKEFGVERSVRPTDSNVSPAISIHEIGAVGATKTERTGIMQLKSEIKQVEFRRLSVSPESQTSGGHPSSIDLMSPTFLSPAACISASSGSFPTVCEPQTSKDSRQGQWQRRRRLDGALNRVPIGFYQKVWKILQKCHGLSVEGFVLPSSSTREMTPGEIKFSVHVESVLNRVPQPEYRQLLVEAILVLTMLADIEIHSIGSIIAVEKIVHIANDLFLQEKKTLGADDIMLAKDPASGICTLLYDSAPSGRFGTMTYLSKAAATYVQEFLPHSLCAVQ
Protein: FI18195p1 (Lethal (3) 76BDm, isoform A) (Lethal (3) 76BDm, isoform B) (Q9VW22)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Probable trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 11
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2-like protein
- RE19263p
- Trafficking protein particle complex subunit 10
Sequence:
MLHLTGQSYNARDIIRNIFSPLIGVLSSPQADEICHRNNLSFVELLQPFAKLPNDAHFRDVSGTSVSVRGLRLNFCDVDWRPPQTILARKMLNESVTNAHNDKTRLATIAGIDLELPTSEPWFEQWRETFLTVQFPADHEFTRHLLSCLLVLSSADPQIVETAHKLGQRVQQMQSITPQKLPKWFHPTEVLNSYVVLHEASQGDLSKAQQGFELLKSTFGDSKCFLVSINSMDSQGAAEVPDHWATFIKRQPKSDPNLPSTDLSAPKSPQEAVSVISMPAMQMSQLLEGVSAQDSDLAMLHPLSPMQESATEAINSKFSISSESIASQTINPNVWGNELEADAPHGGCLTSRDIDNLRHFVQDYAVRALIPYIEHLVAILAEGVTNKKGVSKSLLSATKRWFVTSKPGAGANNQNAVIYTNESAELQTRKLGDLYFMFGHYNLAFQSYHQAKRDFNADSAWQYYAGALEMAALSAFMLGTAQRKTYDYMEDAIVCYLTVCKLQQFATRATLLSMECLKTARLYSEVAKQLIRMTNEESDLRSALLLEQAAYCFLVTQPPMHRKYAFHIVLAGNRYSRAGQRKHAYRCYRQAYQVFQKREWSLAEDHIQYTVAKQAYMLKQLEEASRSFAHLLRPGSLQSAQQQTSFLKEYIQTQNELVKRSPELGLLPHALPQVVQSSVRVLTLVQSPSAVAPHVPATNIDINSNLTADEPIWNKIEEMLVITAANNKPFVFKPSRYLYTKQQPALETPVAVQGEPIELAVTLSNSVQCRIALSEIDLLWKLTLDNDEVLSNACTYEESSDSANKIAVGAAIKTSCMASIKLAEQAEETLHFKLTPKLTGRLSILGVVCRVAAGADPAASLLGTLQFETQKIRPHNAKQSSQTVMDNRLTIKLVPQLPAMNVSFTPVPNRLLAGEIVPVHVTLRNMGIAPIEEIYLGCDNPRCVSLLDQHSQMPLAMMSSLRNLSNDKLVKDKEIRGQRVYRLLNRPGLAALDAQQVQTISLWVQAPHQAGPFTLRLLFYYSLPTVANSPIKYRLVRHIWQLQVESCLQADSTCVVSNAVTNELGLDVNVRNQHAVEGTEVYINSISLYSTEFKLNPDRLHIMNSMGVSPGQAGAQCLKSSICCNFQCRLLEKETQEEYKDIPSIKTLLHSRLSHLKILPAQHAQQVEQHMPPIHDPHSFLTNEETVYFNTNISTEEFNASVADYVPHATLVLSWSALVAREEGQRLACGLHFIKLYKLFETGHCPAAPTASFLRRRHSSDDTLDNRREFPLPEGALNNEDAWQPLADADEEDYWEPNENYVGQRCLLEDESFVMAVKA
Protein: Dynein axonemal assembly factor 1 homolog (Defective transmitter-recycling protein) (Leucine-rich repeat-containing protein 50 homolog) (Q9VQV7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Centriolar coiled coil protein 110kDa, isoform B
- Asterless
- Centrosomal protein 135kDa, isoform B
- Serine/threonine-protein kinase PLK4
- Anastral spindle 2, isoform A
- Anastral spindle 1, isoform A
- Spindle assembly abnormal 4
Sequence:
MSGDESGEEKHVLNLSKQKLKKVPKQDDAHSIRQLILDENELQKIDNIDSYLKIETLSLARNQLLRMYGVCRLHCLRELNLSFNGILSIEGLKECIHLRVLNLEGNNIKTIEHLNTNVNLECLNLADNSIGSISDMSYLRNLKELYLHGNRLTHLRQCDKCLPTSLETLTLAKNSINDLNEICTLSHLSNLLSISIADNPCVTMINSLDGFDYRPFVLNWCMSLKYIDGFVVDPIESLKAEWLYSQGRGRQFRVGEQQGLAKYLSSVCPLVGKALENENDRKLRLILSKAQHHQRQLQEEIMDNANSSASTSPSSHRKKPTSRIQSPRFSRLSGRQGSPESMVNSYHGNSSNNSIVSDNGSTNHSLQMSISLIENIKNDGEGFSLAGSGMSSSVTTKTYNSTESTPRNITPNPYNDQTFISQTPSGGPLAAASKMVPVPETLMSPDVCPAAVAQRVTVTALNPQLHKTKINKNKDNKLNLPRVRSPQLKRNQSPTSSPRRMANKCSADNMQAPEKLQQSAVLADSGGFSTDDDGEQINIEKLRAIRKMAAQKQQQMHQEQLKQQVDNNLNCQDRLIEHVTESSAVTIQKMWRGYHTRKKTNKDIAERLQRRRTQEYIEQLGKDMLLTKAQLENERKIQQLQMQAINALWKKVSTMEVDPKGIPAAAEQGEDSNGGGSGHLSLDQNSAAVVNDLAKRCTMLTDQVQMLQSSIGTIVNCLTMVCNLPQDAIKKQAEIIDCSSTQTDLIAVHTPQIEDLTNFPFTKTRPSTLALESKHEAALACPKIDELNDVDLKETQEDSENLDKDP
Protein: D-galactonate dehydratase family member ManD (EC 4.2.1.-) (D-gluconate dehydratase) (EC 4.2.1.39) (D-mannonate dehydratase) (EC 4.2.1.8) (Q1QT89)
Organism: Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11)
Function: Has low dehydratase activity with D-mannonate and D-gluconate, suggesting that these are not physiological substrates and that it has no significant role in the in vivo degradation of these compounds. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Interaction partners:
- Fructuronate reductase
- Mannonate dehydratase
- Altronate dehydratase
- Transcriptional regulator, GntR family
- Alcohol dehydrogenase GroES-like protein
- PfkB
- 6-phosphogluconate dehydrogenase
- Sugar-phosphate isomerase, RpiB/LacA/LacB family
- Ribose-5-phosphate isomerase
- Ribose-5-phosphate isomerase A
Sequence:
MKIRDAYTIVTCPGRNFVTLKIVTESGTHGIGDATLNGREMAVAAYLDEHVVPALIGRDAGRIEDTWQYLYRGAYWRRGPVTMTAIAAVDMALWDIKAKAAGMPLYQLLGGKSRERVMTYAHCTGQTIEDCLGEVARHVELGYRAVRVQSGVPGIETTYGVAKTPGERYEPADSSLPAEHVWSTEKYLNHAPKLFAAVRERFGDDLHVLHDVHHRLTPIEAARLGKAVEPYHLFWLEDCVPAENQESLRLIREHTTTPLAIGEVFNSIHDCRELIQNQWIDYIRMPLTHGGGITAMRRVADLASLYHVRTGFHGPTDLSPVCLGAAIHFDTWVPNFGIQEHMPHTDETDAVFPHDYRFEDGHFLAGESPGHGVDIDEELAAKYPYERASLPVNRLEDGTLWHW
Protein: Oxidation resistance protein 1 (Protein C7) (Q4KMM3)
Organism: Mus musculus (Mouse)
Function: May be involved in protection from oxidative damage.
Subcellular location: Mitochondrion {ECO:0000250}. Nucleus, nucleolus {ECO:0000269|PubMed:11237729}. Note=According to PubMed:11237729 it is nucleolar.
Interaction partners:
- Hypocretin neuropeptide precursor
- Orexin receptor type 2
- V-type proton ATPase subunit B, kidney isoform
Sequence:
MSVSNLSWLKKKSQSVDITAPGFNPLGGAGKQAPQASKPPAPKTPIIEEEQNNSANTQKHPSRKSELKRFYTIDTGQKKTLDKKDGRRMSFQKPKGTIEYTVESRDSLNSIALKFDTTPNELVQLNKLFSRAVVTGQVLYVPDPEYVSSVESSPSLSPVSPLSPTSSEAEFDKTTTPDVAHPKEAPPASTVSGIRPARVVSSTSEEEEAFTEKFLKINCKYITIGKGTVSGVLLVTPNNIMFDPHKTDPLVQENGCEEYGIMCPMEEVMSAAMYKEILDSKIKESLPIELDQLSGRGSCHSKKATGVSAEDADPRARDQGNDSASTAPRSTEESLSEDAFTESELSPIREELLSSEPRQEKSSDASSESVQTVSQMEVQSLTATSEAANVPDRTSSNPGALSHETGLSGLETATKGGDKATESLQEVSGPKEQSTEVKGQDNQDSSHQESSLQQEAGEDSVSSGETVELKEKPAVLKDQQGQELKRDSETEVEELRKLWKTHSMQQAKQQRDTIQQVSQRESKHSSAAADAHGEGSSLLKEKRRHRLHKFLCLRVGKPMRKTFVSQASATMQQYAQRDKKHEYWFAVPQERTDHLYAFFIQWSPEIYAEDSGEYTREPGFIVVKKMDESEANEAPAGEAAAREWEVVSVAEYHRRIDALNTEELRTLCRRLQITTREDINSKQVAPAKADLEPESFRPNLSDPSELLLPDQIEKLTKHLPPRTIGYPWTLVYGTGKHGTSLKTLYRTMTGLDTPVLMVIKDSDGQVFGALASEPFKVSDGFYGTGETFVFTFCPEFEVFKWTGDNMFFIKGDMDSLAFGGGGGEFALWLDGDLYHGRSHSCKTFGNHTLSKKEDFFIQDIEIWAFE
Protein: DnaJ homolog subfamily B member 7 (Q7Z6W7)
Organism: Homo sapiens (Human)
Function: Probably acts as a co-chaperone.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Carbonic anhydrase 9
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 6
- MAU2 chromatid cohesion factor homolog
Sequence:
MVDYYEVLGLQRYASPEDIKKAYHKVALKWHPDKNPENKEEAERKFKEVAEAYEVLSNDEKRDIYDKYGTEGLNGGGSHFDDECEYGFTFHKPDDVFKEIFHERDPFSFHFFEDSLEDLLNRPGSSYGNRNRDAGYFFSTASEYPIFEKFSSYDTGYTSQGSLGHEGLTSFSSLAFDNSGMDNYISVTTSDKIVNGRNINTKKIIESDQEREAEDNGELTFFLVNSVANEEGFAKECSWRTQSFNNYSPNSHSSKHVSQYTFVDNDEGGISWVTSNRDPPIFSAGVKEGGKRKKKKRKEVQKKSTKRNC
Protein: P-element somatic inhibitor, isoform A (A1ZAK9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSGSGGGGGGGGGPGGASITQAIAQAAAVAARLAASAGTSCEEQIRLPESVAGAFMGRSSNDTITHIQAESGVKVQVMQDQDRVIMLRGQRDTVTKGREMIQNMANRAGGGQVEVLLTINMPPPGPSGYPPYQEIMIPGAKVGLVIGKGGDTIKQLQEKTGAKMIIIQDGPNQELIKPLRISGEAQKIEHAKQMVLDLIAQKDAQGQQQGGRGGGGGGGGPGMGFNNFNNGNGGESTEVFVPKIAVGVVIGKGGDMIRKIQTECGCKLQFIQGKNDEMGDRRCVIQGTRQQVDDAKRTIDGLIENVMQRNGMNRNGNGGGGGPGGDSGNSNYGYGYGVNHAQGGREEITFLVPASKCGIVIGRGGETIKLINQQSGAHTEMDRNASNPPNEKLFKSKGTTDQVEAARQMISEKINMELNVISRKPIGGGPGGGGGNSGGGQNNSHHNQQQGGYGGQNQMQGGDPNSGAGYQQQPWGGPYGQQGWDPSGQQQQMAMANQGGSAAGGASGGQDYSAQWIEYYKQMGCHREAEMIEQQMKAKQAGGSSGPVQQQQPQQQQQSQQQTGGAGAGGADYSAQWAEYYRSVGKIEEAEAIEKTLKNKQNGSGGQSSTPNPSQGGSGQQQPNPAAAAAAAAAAAAAAGGYGQSMTPTQYAQYSQYYAAAAAAGGQPQGAPQPGGGQSGGPPGNYPGNYPGAGYGGYPGAPGQQQQKSHKNDNH
Protein: Mitogen-activated protein kinase 14A (MAP kinase 14A) (MAPK 14A) (EC 2.7.11.24) (Mitogen-activated protein kinase p38a) (MAP kinase p38a) (zp38a) (Q9DGE2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Mapk14a is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. Required for cytokinesis on the future dorsal side of the blastodisc, suggesting a role in symmetrical and synchronous blastomere cleavage.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 6
- Transcription factor Jun
- Cellular tumor antigen p53
- Myocyte enhancer factor 2cb.
- MAP kinase-activated protein kinase 5
- Myocyte enhancer factor 2ca
- ETS transcription factor ELK1.
- M-phase inducer phosphatase
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase kinase kinase 7.
Sequence:
MSQKERPTFYRQEVNKTIWEVPVQYQNLSPVGSGAYGSVCSAFDAKTGFKVAVKKLSRPFQSIIHAKRTYRELRLLKHMRHENVIGLLDVFTPATSLKEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNVTVDIWSVGCIMAELLTGRTLFPGTDHINQLQQIMRLTGTPPSSLISRMPSHEARTYISSLPQMPKRNFADVFIGANPQAVDLLEKMLVLDTDKRITAAEALAHPYFAQYHDPDDEPEAEPFDQSFESRELDIEEWKRQTYEEMISFEPPVFDVDEMES
Protein: Cbp/p300-interacting transactivator 4 (MSG1-related protein 2) (MRG-2) (Q9WUL8)
Organism: Mus musculus (Mouse)
Function: Acts as transcriptional coactivator for TFAP2/AP-2. Enhances estrogen-dependent transactivation mediated by estrogen receptors. May function as an inhibitor of transactivation by HIF1A by disrupting HIF1A interaction with CREBBP. May be involved in regulation of gene expression during development and differentiation of blood cells, endothelial cells and mammary epithelial cells.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q96RK1}.
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- Histone acetyltransferase p300
- Transcription factor AP-2-alpha
Sequence:
MADHLMLAEGYCLLQVPPHTHGPHAPRTLQPYAGPGMDSGLRPRGAPLGPPPPPGTLAYGSFGSPVSFQPFPVSQSPGAGSTHLQSAATPSPGRIPAPPAAAGGPSPLQPAPGAAASLPPPPPPPALGCMDTELIDEEALTSLELELGLHRVRELPELFLGQSEFDCFSDLGSAPAAGSVSC
Protein: SufE-like protein 1, chloroplastic/mitochondrial (Chloroplastic SufE) (CpSufE) (Protein EMBRYO DEFECTIVE 1374) (Protein SULFUR E) (AtSUFE) (Protein SULFUR E 1) (AtSUFE1) (Q84W65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Participates in cysteine desulfurization mediated by NFS2 in chloroplast and NIFS1 in mitochondrion. Activates the cysteine desulfurase activity of NFS2. Cysteine desulfurization mobilizes sulfur from L-cysteine to yield L-alanine and supplies the inorganic sulfur for iron-sulfur (Fe-S) cluster formation. Glutaredoxins regulate SUFE1 activity by inducing its reduction and deglutathionylation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16437155, ECO:0000269|PubMed:16455656}. Mitochondrion {ECO:0000269|PubMed:16437155}.
Interaction partners:
- Protein BOLA2
- Monothiol glutaredoxin-S14, chloroplastic
- Bifunctional monothiol glutaredoxin-S16, chloroplastic
- Monothiol glutaredoxin-S17
- Monothiol glutaredoxin-S15, mitochondrial
- Cysteine desulfurase, mitochondrial
- Cysteine desulfurase 1, chloroplastic
- NifU-like protein 4, mitochondrial
- Fe-S cluster assembly factor HCF101, chloroplastic
- Protein BOLA4, chloroplastic/mitochondrial
Sequence:
MAAAMSSSCCASSLRLIPFKRTLFSSIHYPAKTLLLRPLKPSEVPSFRRTIITFQKISTGIVPPPSASSSPSSYGDLQPIEELPPKLQEIVKLFQSVQEPKAKYEQLMFYGKNLTPLDSQFKTRENKVEGCVSQVWVRAFFDEERNVVYEADSDSVLTKGLAALLVKGLSGRPVPEILRITPDFAVLLGLQQSLSPSRNNGLLNMLKLMQKKALHLEVKGEEDSSSGESSESSFVSIPETKDEANVPEVDLESKPDLVEDLGTEKIDDSESGSNVVALGSRGMRIREKLEKELDPVELEVEDVSYQHAGHAAVRGSAGDDGETHFNLRIVSDAFQGKSLVKRHRLIYDLLQDELKSGLHALSIVAKTPAEV
Protein: Small ribosomal subunit protein uS11A (40S ribosomal protein S14-A) (RP59A) (P06367)
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. uS11 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS19
- Protein LTV1
- Small ribosomal subunit protein eS27B
- Small ribosomal subunit protein uS14A
- Small ribosomal subunit protein eS30A
- Periodic tryptophan protein 2
- Small ribosomal subunit protein uS8B
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS17A
Sequence:
MSNVVQARDNSQVFGVARIYASFNDTFVHVTDLSGKETIARVTGGMKVKADRDESSPYAAMLAAQDVAAKCKEVGITAVHVKIRATGGTRTKTPGPGGQAALRALARSGLRIGRIEDVTPVPSDSTRKKGGRRGRRL
Protein: Thymidine kinase 2, mitochondrial (EC 2.7.1.21) (2'-deoxyuridine kinase TK2) (EC 2.7.1.74) (Deoxycytidine kinase TK2) (EC 2.7.1.-) (Mt-TK) (O00142)
Organism: Homo sapiens (Human)
Function: Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK. Widely used as target of antiviral and chemotherapeutic agents.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:9989599}.
Interaction partners:
- Thymidylate synthase
- Thymidylate kinase
- Thymidine phosphorylase
- Cytidine deaminase
- Deoxycytidylate deaminase
- Thymidine kinase, cytosolic
- 5'
- Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
- Uridine phosphorylase 2
- Uridine phosphorylase 1
Sequence:
MLLWPLRGWAARALRCFGPGSRGSPASGPGPRRVQRRAWPPDKEQEKEKKSVICVEGNIASGKTTCLEFFSNATDVEVLTEPVSKWRNVRGHNPLGLMYHDASRWGLTLQTYVQLTMLDRHTRPQVSSVRLMERSIHSARYIFVENLYRSGKMPEVDYVVLSEWFDWILRNMDVSVDLIVYLRTNPETCYQRLKKRCREEEKVIPLEYLEAIHHLHEEWLIKGSLFPMAAPVLVIEADHHMERMLELFEQNRDRILTPENRKHCP
Protein: Sidestep (Q967X6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MQLLLPTSGMPTNTLETETPAMQTTYWPRQTGNSKSKSNTNCKCNINTHRKSRTRCPDNGKTIWAVGFTLVLLTCLQQLKSVSADEESQDFQKNIPARLVWAALGKTVELPCDLTPPTSQDSVKLLLWFKDTTGIPLYSLDSRGGNVKLAPHAAIASDLGQRLFFSIGDNPKDSRLQINDVKPEDGGVYRCRVDFFNSPTRNFRHNLTLVVPPEEPRIFDAQGKEISQMAGPFREGYELFLCCQVRGGRPPPKVTWWRDDTELIGTSHTSVEEGATVMVNQLLIGTTTRDFYGIRIECRAQGTRLVDPVRKDVTVQVYLKPVRVKIATPNELLTAGQPMPIRCESWGSYPAAKITWLLDGEPIRNAEVTVHSDKEDGNITTSILTLKVTSENDNAELTCRATNPWFSGGAIEDKRIIRVAYPPTVSVHLANEDPSRLVTRAEGQNVTFKCRADARPPVTSYSWFKNGMRMSGESTEIMHLTQLERESAGAYSCGATNTEGETRSSSLTLKVQFSPRCKSGTEQTSIGAVSLHSILVKCEVDADPPDSVRFSWTYNNTRNVSPVLNSRIQSNGLASTVTYLPQTDSELITLACWASNAVGRQTTPCLVHILPANTPEAPKACELRNDTVLEVVCVAGSDGGLSQYFMLEVVGGDPLYSGDPGGSAGQGRGQFSEAIGLGDNEISTLNDQATSAPIFRMQENSPQFRLNNLEPGREYQFLVYAVNAKGRSEPPVVIENVRVAAQLGPYDESILSEDPTPAETTHHGGGGVGGSGSSSGLGTGASTGSGPEKQSTLLILAAVVVIGAVVVTSIIVAGIVVVCRHRPRPPEPQEVRKSMRPARNDVPSMYIEEDELNELEEGGGRAADIRARVAPPNSHLCGGGGMPMPGGVGSSGGAIVGVAGPHHYISESFIQYAQPSLNDPDLILPRGELEFTTLDPTLK
Protein: Sorting nexin-19 (Q92543)
Organism: Homo sapiens (Human)
Function: Plays a role in intracellular vesicle trafficking and exocytosis. May play a role in maintaining insulin-containing dense core vesicles in pancreatic beta-cells and in preventing their degradation. May play a role in insulin secretion. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) (By similarity).
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:Q6P4T1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6P4T1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q6P4T1}. Cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MKTETVPPFQETPAGSSCHLNNLLSSRKLMAVGVLLGWLLVIHLLVNVWLLCLLSALLVVLGGWLGSSLAGVASGRLHLERFIPLATCPPCPEAERQLEREINRTIQMIIRDFVLSWYRSVSQEPAFEEEMEAAMKGLVQELRRRMSVMDSHAVAQSVLTLCGCHLQSYIQAKEATAGKNGPVEPSHLWEAYCRATAPHPAVHSPSAEVTYTRGVVNLLLQGLVPKPHLETRTGRHVVVELITCNVILPLISRLSDPDWIHLVLVGIFSKARDPAPCPASAPEQPSVPTSLPLIAEVEQLPEGRASPVAAPVFLSYSEPEGSAGPSPEVEEGHEAVEGDLGGMCEERKVGNNSSHFLQPNVRGPLFLCEDSELESPLSELGKETIMLMTPGSFLSDRIQDALCALESSQALEPKDGEASEGAEAEEGPGTETETGLPVSTLNSCPEIHIDTADKEIEQGDVTASVTALLEGPEKTCPSRPSCLEKDLTNDVSSLDPTLPPVLLSSSPPGPLSSATFSFEPLSSPDGPVIIQNLRITGTITAREHSGTGFHPYTLYTVKYETALDGENSSGLQQLAYHTVNRRYREFLNLQTRLEEKPDLRKFIKNVKGPKKLFPDLPLGNMDSDRVEARKSLLESFLKQLCAIPEIANSEEVQEFLALNTDARIAFVKKPFMVSRIDKMVVSAIVDTLKTAFPRSEPQSPTEELSEAETESKPQTEGKKASKSRLRFSSSKISPALSVTEAQDKILYCLQEGNVESETLSMSAMESFIEKQTKLLEMQPTKAPEKDPEQPPKGRVDSCVSDAAVPAQDPSNSDPGTETELADTALDLLLLLLTEQWKWLCTENMQKFLRLIFGTLVQRWLEVQVANLTSPQRWVQYLLLLQESIWPGGVLPKFPRPVRTQEQKLAAEKQALQSLMGVLPDLVVEILGVNKCRLSWGLVLESLQQPLINRHLIYCLGDIILEFLDLSASVEESAATTSASDTPGNSKRMGVSS
Protein: Sucrose transport protein SUC3 (AtSUC3) (Sucrose permease 3) (Sucrose transporter 2) (Sucrose-proton symporter 3) (O80605)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport maltose at a lesser rate. May also transport biotin. Probably involved in carpel maturation that leads to pod shatter and seed dispersal.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sugar transport protein 1
- Bidirectional sugar transporter SWEET11
- At2g39500/F12L6.16
- Monosaccharide-sensing protein 1
- Sugar transport protein 13
- Monosaccharide-sensing protein 2
- Bidirectional sugar transporter SWEET12
Sequence:
MSDSVSISVPYRNLRKEIELETVTKHRQNESGSSSFSESASPSNHSDSADGESVSKNCSLVTLVLSCTVAAGVQFGWALQLSLLTPYIQTLGISHAFSSFIWLCGPITGLVVQPFVGIWSDKCTSKYGRRRPFILVGSFMISIAVIIIGFSADIGYLLGDSKEHCSTFKGTRTRAAVVFIIGFWLLDLANNTVQGPARALLADLSGPDQRNTANAVFCLWMAIGNILGFSAGASGKWQEWFPFLTSRACCAACGNLKAAFLLAVVFLTICTLVTIYFAKEIPFTSNKPTRIQDSAPLLDDLQSKGLEHSKLNNGTANGIKYERVERDTDEQFGNSENEHQDETYVDGPGSVLVNLLTSLRHLPPAMHSVLIVMALTWLSWFPFFLFDTDWMGREVYHGDPTGDSLHMELYDQGVREGALGLLLNSVVLGISSFLIEPMCQRMGARVVWALSNFTVFACMAGTAVISLMSLSDDKNGIEYIMRGNETTRTAAVIVFALLGFPLAITYSVPFSVTAEVTADSGGGQGLAIGVLNLAIVIPQMIVSLGAGPWDQLFGGGNLPAFVLASVAAFAAGVIALQRLPTLSSSFKSTGFHIG
Protein: Glucan endo-1,3-beta-D-glucosidase (Endo-1,3-beta-glucanase) (EC 3.2.1.39) (CtLam81A) (Laminarinase) (A3DD66)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Function: Cleaves internal linkages in 1,3-beta-glucan. May contribute to plant biomass degradation (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q47N06}.
Interaction partners:
- Carbohydrate binding family 6
Sequence:
MPPGAKVPQAEIYKTSNLQGAVPTNSWESSILWNQYSLPIYAHPLTFKFKAEGIEVGKPALGGSGIAYFGAHKNDFTVGHSSVYTFPDARADKISDFAVDAVMASGSGSIKATLMKGSPYAYFVFTGGNPRIDFSGTPTVFYGDSGSQCLGVTINGVNYGLFAPSGSKWQGIGTGTITCILPAGKNYFSIAVLPDNTVSTLTYYKDYAYCFVTDTKVEWSYNETESTLTTTFTAEVSVKEGTNKGTILALYPHQWRNNPHILPLPYTYSTLRGIMKTIQGTSFKTVYRYHGILPNLPDKGTYDREALNRYINELALQADAPVAVDTYWFGKHLGKLSCALPIAEQLGNISAKDRFISFMKSSLEDWFTAKEGETAKLFYYDSNWGTLIGYPSSYGSDEELNDHHFHYGYFLHAAAQIALRDPQWASRDNWGAMVELLIKDIANWDRNDTRFPFLRNFDPYEGHSWASGHAGFADGNNQESSSEAINAWQAIILWGEATGNKTIRDLGIYLYTTEVEAVCNYWFDLYKDIFSPSYGHNYASMVWGGKYCHEIWWNGTNSEKHGINFLPITAASLYLGKDPNYIKQNYEEMLRECGTSQPPNWKDIQYMYYALYDPAAAKNMWNESIVPEDGESKAHTYHWICNLDSLGLPDFSVTADTPLYSVFNKNNIRTYVVYNASSSAKKVTFSDGKVMTVGPHSMAVSTGSESEVLAGDLNGDGKINSTDISLMKRYLLKQIVDLPVEDDIKAADINKDGKVNSTDMSILKRVILRNYPL
Protein: MHC class I H2-TL-T10-b mRNA (b haplotype) (Q31205)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSWVLRAAVVCALLLQLDARPSWTRIPLGSHSLRYFYTAVSRPGLGEPWFIIVGYVDDMQVLRFSSKEETPRMAPWLEQEEADDWEQQTRIVTIQGQLSERNLMTLVHFYNKSMDDSHTLQWLQGCDVEPDRHLCLWYNQLAYDSEDLPTLSENPSSCTVGKQWETALYLRSLSTWRATAQICCRNTWKKGRRGCCVQTPQRHM
Protein: Geranylgeranyl transferase type-2 subunit beta (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta) (GGTase-II-beta) (Rab geranyl-geranyltransferase subunit beta) (Rab GG transferase beta) (Rab GGTase beta) (Rab geranylgeranyltransferase subunit beta) (Type II protein geranyl-geranyltransferase subunit beta) (P53611)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Interaction partners:
- Protein prenyltransferase alpha subunit repeat-containing protein 1
- Geranylgeranyl transferase type-2 subunit alpha
- F-box/LRR-repeat protein 2
- Rab proteins geranylgeranyltransferase component A 2
- Protein tyrosine phosphatase type IVA 2
- Synaptobrevin homolog YKT6
- Ras-related protein Rab-1A
- Rab proteins geranylgeranyltransferase component A 1
- Ras-related protein Rab-3A
- Ras-related protein Rab-40C
Sequence:
MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRVNVQPELVS