wanglab/gogpt-training-data huggingface dataset:
Protein: NXPE family member 4 (Protein FAM55D) (Q6UWF7)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- NXPE family member 1
Sequence:
MKISMINYKSLLALLFILASWIIFTVFQNSTKVWSALNLSISLHYWNNSTKSLFPKTPLISLKPLTETELRIKEIIEKLDQQIPPRPFTHVNTTTSATHSTATILNPRDTYCRGDQLHILLEVRDHLGRRKQYGGDFLRARMSSPALMAGASGKVTDFNNGTYLVSFTLFWEGQVSLSLLLIHPSEGVSALWSARNQGYDRVIFTGQFVNGTSQVHSECGLILNTNAELCQYLDNRDQEGFYCVRPQHMPCAALTHMYSKNKKVSYLSKQEKSLFERSNVGVEIMEKFNTISVSKCNKETVAMKEKCKFGMTSTIPSGHVWRNTWNPVSCSLATVKMKECLRGKLIYLMGDSTIRQWMEYFKASINTLKSVDLHESGKLQHQLAVDLDRNINIQWQKYCYPLIGSMTYSVKEMEYLTRAIDRTGGEKNTVIVISLGQHFRPFPIDVFIRRALNVHKAIQHLLLRSPDTMVIIKTENIREMYNDAERFSDFHGYIQYLIIKDIFQDLSVSIIDAWDITIAYGTNNVHPPQHVVGNQINILLNYIC
Protein: ECF sigma factor SigX (Q9I2W5)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Conserved cytoplasmic membrane protein, CmpX protein
- Outer membrane porin F
- CmaX protein
- CrfX protein
- FpvI
- Beta-ketoacyl-[acyl-carrier-protein] synthase FabY
- Sigma factor AlgU negative regulatory protein
Sequence:
MTRAYEELMRRYQRTLFNVCARYLGNDRDADDVCQEVMLKVLYGLKNFEGKSKFKTWLYSITYNECITQYRKERRKRRLMDALSLDPLEEASEEKSPKVEERGGLDRWLVHVNPIDREILVLRFVAELEFQEIADIMHMGLSATKMRYKRALDRLREKFSDATET
Protein: Protein Wnt (Q5NSW6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MHRNFRKWIFYVFLCFGVLYVKLGALSSVVALGANIICNKIPGLAPRQRAICQSRPDAIIVIGEGAQMGIDECQHQFRFGRWNCSALGEKTVFGQELRVGSREAAFTYAITAAGVAHAVTAACSQGNLSNCGCDREKQGYYNQAEGWKWGGCSADVRYGIDFSRRFVDAREIKKNARRLMNLHNNEAGRKVLEDRMKLECKCHGVSGSCTTKTCWTTLPKFREVGHLLKEKYNAAVQVEVVRASRLRQPTFLRIKQLRSYQKPMETDLVYIEKSPNYCEEDAATGSVGTQGRLCNRTSPGADGCDTMCCGRGYNTHQYTKVWQCNCKFHWCCFVKCNTCSERTEVFTCK
Protein: Prostaglandin E2 receptor EP4 subtype (PGE receptor EP4 subtype) (PGE2 receptor EP4 subtype) (Prostanoid EP4 receptor) (P32240)
Organism: Mus musculus (Mouse)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. Has a relaxing effect on smooth muscle. May play an important role in regulating renal hemodynamics, intestinal epithelial transport, adrenal aldosterone secretion, and uterine function.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Prostaglandin E2 receptor EP2 subtype
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Prostaglandin E synthase
Sequence:
MAEVGGTIPRSNRELQRCVLLTTTIMSIPGVNASFSSTPERLNSPVTIPAVMFIFGVVGNLVAIVVLCKSRKEQKETTFYTLVCGLAVTDLLGTLLVSPVTIATYMKGQWPGDQALCDYSTFILLFFGLSGLSIICAMSIERYLAINHAYFYSHYVDKRLAGLTLFAIYASNVLFCALPNMGLGRSERQYPGTWCFIDWTTNVTAYAAFSYMYAGFSSFLILATVLCNVLVCGALLRMHRQFMRRTSLGTEQHHAAAAAAVASVACRGHAGASPALQRLSDFRRRRSFRRIAGAEIQMVILLIATSLVVLICSIPLVVRVFINQLYQPNVVKDISRNPDLQAIRIASVNPILDPWIYILLRKTVLSKAIEKIKCLFCRIGGSGRDSSAQHCSESRRTSSAMSGHSRSFLARELKEISSTSQTLLYLPDLTESSLGGRNLLPGSHGMGLTQADTTSLRTLRISETSDSSQGQDSESVLLVDEVSGSHREEPASKGNSLQVTFPSETLKLSEKCI
Protein: Integration host factor, beta subunit (Q726Y3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Integration host factor subunit alpha
- Viral histone-like protein
- DNA-binding protein HU
Sequence:
MNKSELVKMLAENHEIPAEESSVIVNLFFDSVRDALLQGDRVEIRGFGSFKVKGYRGYKGRNPKTGDNVEVPPKRLPVFRAGKELKEIINP
Protein: GAS2-like protein 2A (growth arrest specific 2 like 2 A) (A0A1L8HFX9)
Organism: Xenopus laevis (African clawed frog)
Function: Together with gas2l2.S, regulates ciliary orientation and performance.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:30665704}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:30665704}.
Interaction partners:
Sequence:
MCIALSHSLAALNSGIMSTHQGGSVRSIRPFKSSEEYLYAMKEDLAEWLKDMYHLEIIVDNFTEILENGSVLCQHANNVTEVAREFSVQYPQLAEKLQLPKSGVKLNMMAQPGTFLARDNVSNFIQWCRKEMDIKDVLMFETEDLVLRKNEKNFVLCLLELARRASRFGMSAPMLIQMEEQIEEEIREEMDLPPPEIPVPKPQRKLCDFKNLDQMVQHLVSRCTCPVQFSMIKVSEGKYKVGESSTLIFVRILRKHVMVRVGGGWDTLEHYLDKHDPCRCTSLSHKPAIKLGSLQKQVSAVHEVKTRLTPRLDNPSKVETTLIVSRSQSPLPPVEWRSYSSGRTRTTSSSNSLDNNENSPTFKMSPSDRRSMSTSYRAHERSATPSRKLFTEDNPEPQQLGNPQSVNFRHHHSTSSLASQLTGSEEENSCLSEVFSESQSRRQMGRTTVMSLKEPAMKEAFLSHTQSAHRKVMSATEQNNIQQGSRIVNQSINSQDSRPKTPSRFIRPPSPSKQIHFFHNQQNKGVEQNPKTQINSCTRSPSPVKQTSLTYKQEFTKRPATPSRISSQYKDGDKSAATEIIPSQDHIKSKPSVSSEERTIRTGRSTPTIHLNKNGITYREVSNLPPRMQPKPDALELSHSIERDCMYTPLPIDPEQEKQIYRSLEDEILTNIKVLEGDSEENHPENDSHGFNMLEKSTLPLNASTLKNPSGQGSVPRSGVYINTTWQSGACYDDVITELTKGHVKLNRVDVENWISKIPSKGMVKEAEEAHTSQRNQVRENGHTGAVSQRTIVRKKTPSTEIKGSKPKQLPSQRARQLALENKKKTVDNVSENQASTFSGDSGETVQEKIKLSQGLKPKRTLKKPERVPSIYKLKLRPKIRPRRDNRPEKKPSRIPTPVSYRQMPSRNNGKAVKRTQSYQANKTSAPQTLNESQSSTVILEDLDSDDKTLEHSAPSQAVETPVTIGNDQSKTEEEEESWV
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9LFF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-processing-splicing factor 8A
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- Pre-mRNA-processing-splicing factor 8B
- Protein STABILIZED1
- DExH-box ATP-dependent RNA helicase DExH12
- SAC3 family protein C
- Nuclear protein-like
- Eukaryotic translation initiation factor 3 subunit J
- Eukaryotic translation initiation factor 3 subunit J
- Suppressor of mec-8 and unc-52 protein homolog 1
Sequence:
MVSDKIVESSHRKHRRSYSPSDEVVKSSKRHKHHHHKHRHSHHLDEDGNEKNVYPFLGNPGNDGELDLEEGENLKKKGSIDRESNRDNYRGRSSRDKARSSSRETGRENERERRKDQDRDRGRREDQSDQEIYKSGGDGYGEVRHDAEDDLDSLKSHKPNGETQGNVERSEVDNDDDGEDVVWGVEEQEAAEMKRIEESKRITQAILEKYKKKLEQSSTVADVQAKAGLDTEAVDGEVAKLSSAVGETPARLVISDSDMTLASAGSPKSDMFSDDIFGESPLADGTRKGNALVPFVRSGLNDNWDDAEGYYSYQLGELLDDRYEIMATHGKGVFSTVVRAKDTKPELGEPEEVAIKIIRKNETMHKAGQAEIRILKKLVCSDPENKHHCVRLLSTFEYRNHLCLVFESLHLNLREVVKKIGVNIGLKLYDVRVYAEQLFISLKHLKNCGVLHCDIKPDNILMNEGRNMLKLCDFGSAMFAGENQVTPYLVSRFYRAPEIILGLPYDHPLDIWSVGCCLYELYSGKIMFPGSTNNDMLRLHMELKGPFPKKMLRKGAFIDQHFDKDLCFYATEEDSVTGKTIRRIMVNVKPKDLGSVIRRRYEDEDPKVLVHFRNLLDKIFTLDPQKRLTVSQALAHPFITGK
Protein: ETS-related transcription factor Elf-5 (E74-like factor 5) (Epithelium-restricted ESE-1-related Ets factor) (Epithelium-specific Ets transcription factor 2) (ESE-2) (Q9UKW6)
Organism: Homo sapiens (Human)
Function: Transcriptionally activator that may play a role in regulating the later stages of keratinocytes terminal differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
Interaction partners:
- WAP four-disulfide core domain protein 5
- Homeobox protein CDX-2
- Trans-acting T-cell-specific transcription factor GATA-3
- Eomesodermin homolog
- Transcriptional enhancer factor TEF-3
Sequence:
MPSLPHSHRVMLDSVTHSTFLPNASFCDPLMSWTDLFSNEEYYPAFEHQTACDSYWTSVHPEYWTKRHVWEWLQFCCDQYKLDTNCISFCNFNISGLQLCSMTQEEFVEAAGLCGEYLYFILQNIRTQGYSFFNDAEESKATIKDYADSNCLKTSGIKSQDCHSHSRTSLQSSHLWEFVRDLLLSPEENCGILEWEDREQGIFRVVKSEALAKMWGQRKKNDRMTYEKLSRALRYYYKTGILERVDRRLVYKFGKNAHGWQEDKL
Protein: Retinol dehydrogenase 11 (EC 1.1.1.300) (Androgen-regulated short-chain dehydrogenase/reductase 1) (Cell line MC/9.IL4-derived protein 1) (M42C60) (Prostate short-chain dehydrogenase/reductase 1) (Retinal reductase 1) (RalR1) (Short-chain aldehyde dehydrogenase) (SCALD) (Q9QYF1)
Organism: Mus musculus (Mouse)
Function: Retinol dehydrogenase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinol, and to a lesser extent on 13-cis-retinol (By similarity). Exhibits also reductive activity towards toxic lipid peroxidation products such as medium-chain aldehydes trans-2-nonenal, nonanal, and cis-6-nonenal. Has no dehydrogenase activity towards steroid. Seems to be required for homeostasis of retinol in liver and testis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12807874}; Single-pass type II membrane protein {ECO:0000269|PubMed:12807874}.
Interaction partners:
- Lecithin retinol acyltransferase
- Retinol dehydrogenase 10
- Retinoid isomerohydrolase
- Retinol dehydrogenase 5
- Retinaldehyde dehydrogenase 3
- Beta,beta-carotene 15,15'-dioxygenase
- Cytochrome P450 26A1
- Aldehyde dehydrogenase 1A1
- Retinal dehydrogenase 2
- All-trans-retinol 13,14-reductase
Sequence:
MFGFLLLLSLPFILYLVTPKIRKMLSSGVCTSNVQLPGKVAIVTGANTGIGKETAKDLAQRGARVYLACRDVDKGELAAREIQAVTGNSQVFVRKLDLADTKSIRAFAKDFLAEEKHLHLLINNAGVMMCPYSKTADGFEMHIGVNHLGHFLLTHLLLEKLKESAPSRIVNLSSLGHHLGRIHFHNLQGEKFYSAGLAYCHSKLANILFTKELAKRLKGSGVTTYSVHPGTVHSELTRYSSIMRWLWQLFFVFIKTPQEGAQTSLYCALTEGLESLSGSHFSDCQLAWVSYQGRNEIIARRLWDVSCDLLGLPVDW
Protein: Transcriptional activator Myb (Proto-oncogene c-Myb) (P10242)
Organism: Homo sapiens (Human)
Function: Transcriptional activator; DNA-binding protein that specifically recognize the sequence 5'-YAAC[GT]G-3'. Plays an important role in the control of proliferation and differentiation of hematopoietic progenitor cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:19646965}.
Interaction partners:
- CREB-binding protein
- Histone acetyltransferase p300
- CCAAT/enhancer-binding protein beta
- Histone-lysine N-methyltransferase 2A
- Endothelial transcription factor GATA-2
- Runt-related transcription factor 1
- Transcription factor PU.1
- T-cell acute lymphocytic leukemia protein 1
- Myb-binding protein 1A
- Erythroid transcription factor
Sequence:
MARRPRHSIYSSDEDDEDFEMCDHDYDGLLPKSGKRHLGKTRWTREEDEKLKKLVEQNGTDDWKVIANYLPNRTDVQCQHRWQKVLNPELIKGPWTKEEDQRVIELVQKYGPKRWSVIAKHLKGRIGKQCRERWHNHLNPEVKKTSWTEEEDRIIYQAHKRLGNRWAEIAKLLPGRTDNAIKNHWNSTMRRKVEQEGYLQESSKASQPAVATSFQKNSHLMGFAQAPPTAQLPATGQPTVNNDYSYYHISEAQNVSSHVPYPVALHVNIVNVPQPAAAAIQRHYNDEDPEKEKRIKELELLLMSTENELKGQQVLPTQNHTCSYPGWHSTTIADHTRPHGDSAPVSCLGEHHSTPSLPADPGSLPEESASPARCMIVHQGTILDNVKNLLEFAETLQFIDSFLNTSSNHENSDLEMPSLTSTPLIGHKLTVTTPFHRDQTVKTQKENTVFRTPAIKRSILESSPRTPTPFKHALAAQEIKYGPLKMLPQTPSHLVEDLQDVIKQESDESGIVAEFQENGPPLLKKIKQEVESPTDKSGNFFCSHHWEGDSLNTQLFTQTSPVADAPNILTSSVLMAPASEDEDNVLKAFTVPKNRSLASPLQPCSSTWEPASCGKMEEQMTSSSQARKYVNAFSARTLVM
Protein: DUF4400 domain-containing protein (Membrane protein) (Q9L5M5)
Organism: Salmonella typhi
Interaction partners:
Sequence:
MAADNSARAIFIRGLLLLGMMLYLIYSLGFQNTDELKQQITQEVNASRSLISNDRWLSVIANSEATLSTLINDYKLIDYLNTILIPDTSTPARGMNYVAEKMTSVNYTVAKNLPLLIYQSIFRWNLILGWLILFSPYLIAMLADGMYQWKLKRYVFGNVTVQFYRIWFRAFWIIGALTFIYLSMPNMSLFNNIAQLFPPVALLILGIALNRLWSNFQKLM
Protein: Nodulin 41 (G1FTR5)
Organism: Phaseolus vulgaris (Kidney bean) (French bean)
Interaction partners:
Sequence:
MKPFVFFCLAFYSVSSLFSTEANESPSGFTVDLIHRDSPLSPFYNPSLTPSQRIINAALRSISRLNRVSNLLDQNNKLPQSVLILHNGEYLMRFYIGTPPVERLATADTGSDLIWVQCSPCASCFPQSTPLFQPLKSSTFMPTTCRSQPCTLLLPEQKGCGKSGECIYTYKYGDQYSFSEGLLSTETLRFDSQGGVQTVAFPNSFFGCGLYNNITVFPSYKLTGIMGLGAGPLSLVSQIGDQIGHKFSYCLLPLGSTSTSKLKFGNESIITGEGVVSTPMIIKPWLPTYYFLNLEAVTVAQKTVPTGSTDGNVIIDSGTLLTYLGESFYYNFAASLQESLAVELVQDVLSPLPFCFPYRDNFVFPEIAFQFTGARVSLKPANLFVMTEDRNTVCLMIAPSSVSGISIFGSFSQIDFQVEYDLEGKKVSFQPTDCSKV
Protein: Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC 3.1.3.27) (Protein-tyrosine phosphatase mitochondrial 1) (EC 3.1.3.16, EC 3.1.3.48) (P0C089)
Organism: Rattus norvegicus (Rat)
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG) (By similarity). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle (By similarity). Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells. May prevent intrinsic apoptosis, probably by regulating mitochondrial membrane integrity (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16039589}; Peripheral membrane protein {ECO:0000269|PubMed:16039589}; Matrix side {ECO:0000269|PubMed:16039589}.
Interaction partners:
- Phosphatidate cytidylyltransferase, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MAASAWLEAGLARVLFYPTLLYTVFRGRVGGPAHRDWYHRIDHTVLLGALPLRSMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKNVGVEQLRLSTVDMTGVPTLANLHRGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEILKEFHKEIAARAAKN
Protein: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2+)-ATPase 2) (EC 7.2.2.10) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2+) ATPase) (P11607)
Organism: Sus scrofa (Pig)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O55143}; Multi-pass membrane protein {ECO:0000269|PubMed:30777856}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:30777856}; Multi-pass membrane protein {ECO:0000269|PubMed:30777856}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER contact junction. {ECO:0000250|UniProtKB:O55143}.
Interaction partners:
- Histidine rich calcium binding protein
- Calcium-transporting ATPase
- Calcium-transporting ATPase
- RAR related orphan receptor A
- Ryanodine receptor 2
- Sarcolipin
Sequence:
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQMSVCRMFILDKVEGDTCSLNEFTITGSTYAPIGEVHKDDKPVKCHQYDGLVELATICALCNDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTELKGLSKIERANACNSVIKQLMKKEFTLEFSRDRKSMSVYCTPNKPSRTSMSKMFVKGAPEGVIDRCTHIRVGSTKVPMTPGVKQKIMSVIREWGSGSDTLRCLALATHDNPMRREEMNLEDSANFIKYETNLTFVGCVGMLDPPRIEVASSVKLCRQAGIRVIMITGDNKGTAVAICRRIGIFGQDEDVTSKAFTGREFDELNPSAQREACLNARCFARVEPSHKSKIVEFLQSFDEITAMTGDGVNDAPALKKSEIGIAMGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTAALGFPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMNKPPRNPKEPLISGWLFFRYLAIGCYVGAATVGAAAWWFIAADGGPRVTFYQLSHFLQCKEDNPDFEGVDCAVFESPYPMTMALSVLVTIEMCNALNSLSENQSLLRMPPWENIWLVGSICLSMSLHFLILYVEPLPLIFQITPLNLTQWLMVLKISLPVILMDETLKFVARNYLEPGKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS
Protein: Rac-like GTP-binding protein ARAC3 (AtRAC1) (GTPase protein ROP6) (Q38912)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inactive GDP-bound Rho GTPases reside in the cytosol, are found in a complex with Rho GDP-dissociation inhibitors (Rho GDIs), and are released from the GDI protein in order to translocate to membranes upon activation. Involved in cell polarity control during the actin-dependent tip growth of root hairs, thus regulating root hair length and root hair initiation. SPK1-dependent activation is required for auxin-mediated inhibition of PIN2 internalization during gravitropic responses.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q38937}. Cell membrane {ECO:0000269|PubMed:10798620, ECO:0000269|PubMed:27251533}; Peripheral membrane protein {ECO:0000255}. Note=The localization to the plasma membrane requires YIP4A and YIP4B (By similarity). Accumulates in a sterol-enriched, polar membrane domain during root hair initiation (PubMed:27251533). {ECO:0000250|UniProtKB:Q38919, ECO:0000269|PubMed:27251533}.
Interaction partners:
- Guanine nucleotide exchange factor SPIKE 1
- Rho GDP-dissociation inhibitor 1
- CRIB domain-containing protein RIC1
- CRIB domain-containing protein RIC4
- Auxin-binding protein 1
- KOW domain-containing protein
- Immunoglobulin E-set superfamily protein
- At1g12070
- Receptor protein kinase TMK1
- Brefeldin A-inhibited guanine nucleotide-exchange protein 5
Sequence:
MSASRFIKCVTVGDGAVGKTCLLISYTSNTFPTDYVPTVFDNFSANVIVDGNTINLGLWDTAGQEDYNRLRPLSYRGADVFLLAFSLVSKASYENVSKKWVPELRHYAPGVPIILVGTKLDLRDDKQFFAEHPGAVPISTAQGEELKKLIGAPAYIECSAKTQQNVKAVFDAAIKVVLQPPKNKKKKKRKSQKGCSIL
Protein: Wee1-like protein kinase 2 (EC 2.7.10.2) (Wee1-like protein kinase 1B) (Wee1B kinase) (P0C1S8)
Organism: Homo sapiens (Human)
Function: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1/CDC2 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11029659, ECO:0000269|PubMed:29606300}.
Interaction partners:
- Serine/threonine-protein kinase Chk1
- Cyclin-dependent kinase 1
- Wee1-like protein kinase
- Serine/threonine-protein kinase Chk2
- M-phase inducer phosphatase 2
- Cytoskeleton-associated protein 5
- Protein PAT1 homolog 2
- M-phase inducer phosphatase 1
Sequence:
MDDKDIDKELRQKLNFSYCEETEIEGQKKVEESREASSQTPEKGEVQDSEAKGTPPWTPLSNVHELDTSSEKDKESPDQILRTPVSHPLKCPETPAQPDSRSKLLPSDSPSTPKTMLSRLVISPTGKLPSRGPKHLKLTPAPLKDEMTSLALVNINPFTPESYKKLFLQSGGKRKIRGDLEEAGPEEGKGGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKTFTELSNENSALHEVYAHAVLGHHPHVVRYYSSWAEDDHMIIQNEYCNGGSLQAAISENTKSGNHFEEPKLKDILLQISLGLNYIHNSSMVHLDIKPSNIFICHKMQSESSGVIEEVENEADWFLSANVMYKIGDLGHATSINKPKVEEGDSRFLANEILQEDYRHLPKADIFALGLTIAVAAGAESLPTNGAAWHHIRKGNFPDVPQELSESFSSLLKNMIQPDAEQRPSAAALARNTVLRPSLGKTEELQQQLNLEKFKTATLERELREAQQAQSPQGYTHHGDTGVSGTHTGSRSTKRLVGGKSARSSSFTSGEREPLH
Protein: Threonylcarbamoyladenosine tRNA methylthiotransferase (EC 2.8.4.5) (CDK5 regulatory subunit-associated protein 1-like 1) (tRNA-t(6)A37 methylthiotransferase) (Q91WE6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the methylthiolation of N6-threonylcarbamoyladenosine (t(6)A), leading to the formation of 2-methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position 37 in tRNAs that read codons beginning with adenine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5VV42}; Single-pass membrane protein {ECO:0000255}. Note=Is a tail-anchored protein that exploits the TCR40 assisted pathway for insertion into the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q5VV42}.
Interaction partners:
- Proton-coupled zinc antiporter SLC30A8
- Hematopoietically-expressed homeobox protein Hhex
- Transcription factor 7-like 2
- Insulin-like growth factor 2 mRNA-binding protein 2
- ATP-sensitive inward rectifier potassium channel 11
- Alpha-ketoglutarate-dependent dioxygenase FTO
- Translation initiation factor eIF2 assembly protein
- Melatonin receptor type 1B
Sequence:
MPSASCDVLLDDIEDIISQEDSKPQDRQFSRKHVFPKVRRRNTQKYLQEEPRPPSDSTIPGIQKIWIRTWGCSHNNSDGEYMAGQLAAYGYKITENASDADLWLLNSCTVKNPAEDHFRNSIKKAQEENKKVVLAGCVPQAQPRQDYLKGLSIIGVQQIDRVVEVVEETIKGHSVRLLGQKKDNGKRLGGARLDLPKIRKNPLIEIISINTGCLNACTYCKTKHARGNLASYPIDELVERAKQSFQEGVCEIWLTSEDTGAYGRDIGTDLPTLLWKLVEVIPEGAMLRLGMTNPPYILEHLEEMAKILNHPRVYAFLHIPVQSASDSVLMDMKREYCVADFKRVVDFLKEKVPGITIATDIICGFPGETDQDFQETVKLVEEYKFPSLFINQFYPRPGTPAAKAEQVPAHVKKQRTKDLSRVFHSYNPYDHKIGERQQVLVTEESFDSKFYVAHNRFYEQVLVPKNPAFMGKMVEVDIYESGKHFLKGQPVSETRVYTPSISKPLAKGEVSGLTKEFRNRLGNHPNGTSDTCPATQHGSAYSRMVLQMSQYDCALKVATGLALLALLLHFWPDSLLTM
Protein: Uncharacterized oxidoreductase P32A8.02 (EC 1.-.-.-) (Q9C1X5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Zinc-type alcohol dehydrogenase-like protein C16A3.02c
- Zinc-type alcohol dehydrogenase-like protein C337.11
- Zinc-type alcohol dehydrogenase-like protein C2E1P3.01
- Putative S-
- 3-keto-steroid reductase erg27
Sequence:
MSESQTESTTVTLTNGMVIPRIGFGAFMLKYNECYGLVTQALDSGYRHIDTAAVYGNEDICGKAIVDWCEKNNVKRTDIFLTSKLANCSDYYSTRAAIRSSLHHLGTYIDLFLIQSPAGGKKSRIASWKAMEEFVDSGDIRSVGVSNYGVKHLQELYASNPKFYPCVNQIELHPFLSQDDIVKYCQSHDIAIEAYSPLTHGIRLNDEKLVPIAKKLNISVAQLLIRWSLQKGYIPIIKSTKKEHMLSDLDVFNFTIPDDVVQELSSFDEHWHAGTTYDPTVCD
Protein: Jetlag, isoform A (Q9VMY0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein timeless
- Cryptochrome-1
- Timeout
- Crystallin, isoform A
- GEO01111p1
- 
- BRWD3
- Protein cycle
- Circadian locomoter output cycles protein kaput
- Period circadian protein
Sequence:
MCTLHPEEEAHLMAMASGGQPTRTASPRPLVTASIAAPRSLFDVCWDDVLIPQVAVYLSLKDLFNLRCCSRTAQRFVEAALEKRQELHLSGNNTKNIDVAFRVLARCCQRLEVLHLACCRWLTDELLLPLLANNKKRLWAVNLNECVNITALSLQPIIVECKELRVLKLSKCQWLTTGAVDALTLHQSKLVEFDISYCGAIGERCLIIFFRKLNKLTVLSLANTPSVTDQVLIQIGNYCRELEHINVIGCAAISDYGVHALTVHCLRLRTLLIRRCPRVTELSLAPLRQRRLYIDRPQPDVGLNAYNLNDFYPSDFLVY
Protein: T-complex protein 1 subunit delta (TCP-1-delta) (CCT-delta) (P39078)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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. In yeast may play a role in mitotic spindle formation.
Subcellular location: Cytoplasm.
Interaction partners:
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta
- Phosducin-like protein 2
- Prefoldin subunit 5
- Peroxisomal membrane protein import receptor PEX19
Sequence:
MSAKVPSNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEIIISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLGAAERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAASTSLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTIDDTEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVNDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLSKLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLGSADLVEEIDSDGSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCLVKERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLAENAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVSTSAITLASECVKSILRIDDIAFSR