wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium uniporter regulatory subunit MCUb, mitochondrial (MCUb) (Coiled-coil domain-containing protein 109B) (Q9NWR8)
Organism: Homo sapiens (Human)
Function: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:24231807}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium uptake protein 2, mitochondrial
- Essential MCU regulator, mitochondrial
- Calcium uptake protein 1, mitochondrial
- Mitochondrial calcium uniporter regulator 1
- Calcium uptake protein 3, mitochondrial
- Calcium uniporter protein, mitochondrial
- Mitochondrial adenyl nucleotide antiporter SLC25A23
- Histone-lysine N-methyltransferase SETDB1
Sequence:
MLQRGLWPWRTRLLPTPGTWRPARPWPLPPPPQVLRVKLCGNVKYYQSHHYSTVVPPDEITVIYRHGLPLVTLTLPSRKERCQFVVKPMLSTVGSFLQDLQNEDKGIKTAAIFTADGNMISASTLMDILLMNDFKLVINKIAYDVQCPKREKPSNEHTAEMEHMKSLVHRLFTILHLEESQKKREHHLLEKIDHLKEQLQPLEQVKAGIEAHSEAKTSGLLWAGLALLSIQGGALAWLTWWVYSWDIMEPVTYFITFANSMVFFAYFIVTRQDYTYSAVKSRQFLQFFHKKSKQQHFDVQQYNKLKEDLAKAKESLKQARHSLCLQMQVEELNEKN
Protein: TATA box-binding protein-associated factor RNA polymerase I subunit D (TATA box-binding protein-associated factor 1D) (TBP-associated factor 1D) (Transcription initiation factor SL1/TIF-IB subunit D) (Q9D4V4)
Organism: Mus musculus (Mouse)
Function: Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1/TIF-IB with the rDNA promoter. SL1/TIF-IB is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA. Formation of SL1/TIF-IB excludes the association of TBP with TFIID subunits (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- TATA box-binding protein-associated factor RNA polymerase I subunit A
- TATA box-binding protein-associated factor RNA polymerase I subunit B
- TATA box-binding protein-associated factor RNA polymerase I subunit C
- TATA-box-binding protein
- RNA polymerase I-specific transcription initiation factor RRN3
- Transcription termination factor 1
- Nucleolar transcription factor 1
Sequence:
MAQSEVNSVCVASDRAGDTGDQSDDSSDGSLFKTQCAPSPIQKQRHPTVKRVTLPASVETDSSSDSSIEPRPLTLKAIFERFKKKKRKKRKKRKYEPKLRPRGRPRGKPSGTRITRRSQIDAKQIKDKGAVFPFLESESGRKPLPWKKILTYEQAVARGFFHHIEKLKYEHHLKECLKQMHAGEDLEKEDLDSRRHKYMDDDGSLSPIEEPLTEDEATNPQAECDIKLVEDSCFIISSEFSRKRNLEQEKIKKESTFSKKAKDATHREKGHRRTLKGNEHVTIEEDSRPQPRPFAHLQSKVMKKGELEYLEVHHLCGLSQPL
Protein: C-C motif chemokine (D3ZDY4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU361150}.
Interaction partners:
- C-C motif chemokine receptor 8
- C-C chemokine receptor type 5
- Macrophage inflammatory protein-1 alpha receptor
- Atypical chemokine receptor 4
- CX3C chemokine receptor 1
- C-C chemokine receptor type 3
- C-C chemokine receptor type 10
- C-C motif chemokine receptor 9
- C-X-C chemokine receptor type 2
- C-C motif chemokine receptor 7
Sequence:
MKLLNMVLVCLLVAAMWLQNVDSKSMHVVSSRCCLNTLENKIALKFIKCYKEIGPSCPYYPAVIFRLIKGRESCALTNTTWVQDYLKKVKPC
Protein: CCR4-NOT transcription complex subunit 10 (Q38AA1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- CCR4-NOT transcription complex subunit 11
- NOT1
- Cell differentiation protein, putative
Sequence:
MTDDVLRQQLEKVRKAFEAQDYQTCETLLQKMPKDDLQVQHNLAIVRLLLNHADVEQTIAALGDTSSDAFSSTNDKDTKPNVTLLYEGHETAHFNRALLLARSGLVHEAAVILRALLAMHTSISVAVLARVLSLLQAITRMPPGSRHRQRSDDELIQQVLSEKLNAFNEDPALSLMVKAAFSDMGNIHELPHATDGEGAAHFNNLGVLAMGDSKLNVASLCFAKAEKAAQQCNSLLVRQPIVYNAGLCALFRGEYDSAITCFLSVQELMKSSPLFWVRFAEASIGKLHAQKRVRSREEYERMQDCFSEQLHNGKLLPNYEFLTLPWAVITQSPLVDLKDNSVGTALEALASCAIQNALALLLPQNHTTISATDAFPHNAQLIHFALFYWCALEIVRKNYTVVVNVGSDLLLLHDRRPLSPNLHTALLSYMVEALVHLNEPDRALKVLRRSSLSSLVAGSPPEQLDAYQQGRVEVLFINLAITHIVNGSWSQATSVVDSLLSKLYETRAAKEKDESSSGNNQDAVLAYHLLVIFLELAQGNQEKAQEALQRLSWCA
Protein: NAD(+) hydrolase PdTIR (EC 3.2.2.6) (TIR domain-containing protein in P.denitrificans) (PdTIR) (A1AY86)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide.
Interaction partners:
Sequence:
MSANDRAIETLRREIAKLQTDGAAIARKDAGIRAKLASAMAAQAKAKTAPALRLKQAEASRLEKELMATSKSQADIATKIAKKQSSLSAKLVVQANEAKKADAKAKKNQERVSKTQEEATRKLEAGYRKLTLENQSLEQRLQRELSAMKPTAGPTTNADLTSAPPHDIFISHAWEDKADFVEALAHTLRAAGAEVWYDDFSLRPGDSLRRSIDKGLGSSRFGIVVLSTHFFKKEWPQKELDGLFQLESSGRSRILPIWHKVSKDEVASFSPTMADKLAFNTSTKSVDEIVADLMAIIRD
Protein: Protein PET117, mitochondrial (Q02771)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the assembly of cytochrome c oxidase.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
- Heme A synthase COX15
- Protein PET100
- Cytochrome c oxidase copper chaperone
- Cytochrome c oxidase assembly factor 6
- Cytochrome c oxidase assembly protein COX11
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome oxidase assembly protein SHY1
- Mitochondrial protein PET191
- Protein SCO2
- Cytochrome c oxidase assembly protein COX18, mitochondrial
Sequence:
MSRASKITFAASCLITAATVVGVHYVQEMERETLHQGPIKDAKRVEEKRLRKTNGVASLDPTKERKRYFNMSEHEEQKELRKKYETMQPLSGEVVTKDGEVVKESKK
Protein: Protein E6 (P04019)
Organism: Human papillomavirus 11
Function: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response.
Subcellular location: Host cytoplasm {ECO:0000250|UniProtKB:P03126, ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000250|UniProtKB:P03126, ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MESKDASTSATSIDQLCKTFNLSLHTLQIQCVFCRNALTTAEIYAYAYKNLKVVWRDNFPFAACACCLELQGKINQYRHFNYAAYAPTVEEETNEDILKVLIRCYLCHKPLCEIEKLKHILGKARFIKLNNQWKGRCLHCWTTCMEDLLP
Protein: Diacylglycerol kinase gamma (DAG kinase gamma) (EC 2.7.1.107) (88 kDa diacylglycerol kinase) (DGK-III) (Diglyceride kinase gamma) (DGK-gamma) (P49620)
Organism: Rattus norvegicus (Rat)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (By similarity). Has no apparent specificity with regard to the acyl compositions of diacylglycerol (By similarity). Specifically expressed in the cerebellum where it controls the level of diacylglycerol which in turn regulates the activity of protein kinase C gamma. Through protein kinase C gamma, indirectly regulates the dendritic development of Purkinje cells, cerebellar long term depression and ultimately cerebellar motor coordination (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:7809169}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49619}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:7809169}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phosphatidate cytidylyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Phosphatidate cytidylyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Diacylglycerol O-acyltransferase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sequence:
MSDGQWVCLSSEEFDQLQKYSEYSSKKIKDVLAEFNEGGSLKQYDPHKPISYDVFKLFMRAYLEVDLPQPLSTNLFLAFSQKPRQETPDHPKEGASSSEPNVSDSNAESTAKADAACAPDTESKPIKTQVPSEELEAAAPWGEPNAPASSSDAPIVYLKDVVCYLSLMETGRPQDKLEFMFRLYDSDENELLDQAELDQIVSQMLHVAQYLEWDPTELRPILKEMLQGMDYNKDGFVSLEEWVSGGMTTIPLLVLLGMDDSASKGDGRHAWTLKHFKKPTYCNFCHIMLMGVRKQGLCCIYCKYAVHQRCVSNSIPGCVKTYSKAKRSGEVMQHAWVEGNSSVKCDRCHKSIKCYQSVTARHCVWCRMTFHRKCELSTACDGGELKDHILLPTSIYPVTRDRQAGKSDSGAAAKGELVMQYKIIPSPGTHPLLVLVNPKSGGRQGERILQKFHYLLNPKQVFNLDKGGPTPGLNFFQDTPDFRVLACGGDGTVGWILDCIDKANFTKHPPVAVLPLGTGNDLARCLRWGGGYEGGSLTKILKEIEQSPLVMLDRWYLEVMPREEVENGDQVPYNIMNNYFSIGVDASIAHRFHVMREKHPEKFNSRMKNKLWYFEFGTSETFAATCKKLHDHIELECDGVEVDLSNIFLEGIAILNIPSMYGGTNLWGETKKNRAVIRESRKSVTDPKELKCCVQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCSSVTIRTKKLLPMQVDGEPWMQPPCMIKITHKNQAPMMMGPPQKSSFFSLRRKSRSKD
Protein: Pentatricopeptide repeat-containing protein At2g30780 (O49343)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASNFVKLGSQFIGKLTRVTSLPAHHTDLVQRVSILKDELLTIGNSKEKFQNVLDQKGQWLFRTYRDGAGILELMDQLFPRHYLALQVLEWRRGQKDYCIPLTSEEYAKGIKIAGRARDINLAVYLFDEAAKKRMQTASVYNSLMSVYMWNGLAEECQSLFKDFRRQTHCAPTVVTYNILVSVYGRLLMVKNMEAAFEELQKVKLPPNSVTYNFLIAGYMTAWNWDKMEATFQEMKRGPVEPDTDTYQLMLRGYANSGNLNRMEEMYEVIKDQVGVNSGPLVRAMICAYCKKAVEDRVQKIENLLSLLSGEEYLPWLNVLLIRLYAQEDFVEAMESKINEAFEQKTCVNKSSIMRAIIAAYFRCNEVDNLANFVKRAESAGWKLCRSLYHCKIMMYGSQKRFEEMEGVVNEMAETNYGLVTKTFAIMIKAYKNHGMESDAEKVKGKMLKRGL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q580Q4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEHKRPANGNSALPVPPAEEGTEKKDPLEGILGSRAECKYVKKKLLGQGSFGSAWRVEETATGLIFAAKVMDTNNMSAKDRGFVTNEVKCLSRCNNANIIRHRASYDRGGMLLIIMEYADGGDLYRQIKARQHAVRHFKEHEVLYIFLQLCLALDHIHGNNMMHRDLKTANVLLTTTGLVKLGDFGFSRQYEDSLSNPVGTTFCGTPYYLSPELWRRAPYSKKSEMWALGVVLYEVMVLKRPFGGRNMDELIDNIVHARRAPLPNMYSDDLRRVCDQLLSLDPAKRPSLRQLFQLPFIRRGLETLRRSVEIHKKIPQQVFNEIAQNIDEVLSSELPEYEGSRVTPHRGMLQRHTADRGWKDCELSLDHNGVLMRNVETGDVERVDLEALTSVCPIDAAMAHEKYVFALKNQTGKAYWFKDRSEESYERWISVLQNAVPR
Protein: Uncharacterized mitochondrial carrier C12D12.05c (O94502)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 51 kDa subunit homolog SPBC18E5.10, mitochondrial
- NADH-ubiquinone oxidoreductase 24 kDa subunit homolog C11E3.12, mitochondrial
- RNA polymerase I-specific transcription initiation factor rrn11
- Putative acyl carrier protein, mitochondrial
- Heme A synthase-mitochondrial ferredoxin fusion protein
- Putative monoglyceride lipase
- Mitochondrial import inner membrane translocase subunit tim22
- Ubiquinone biosynthesis protein coq11
- UPF0659 protein C216.03
- Mitochondrial import inner membrane translocase subunit tim17
Sequence:
MPTELSDITIQSVLPCDYSLFKNNLRVSRLPESRFVFSPKEEINCQSLLQGPELKTALDNLNFIHKQKFEHQFRHGYWKLHPHPHHQHDSIIPASWIHDTPHMKLVFHRLQNLPDGDLLLENDPKNNVGYFISGGIAGIVSRTCTAPLDRLKVMLISDTGSKPSPKYPFATLLHTTKVLWNRNGIRSFFVGNGINVLKVMPESSIKFGTYEAMKRVLGISSSSENHSPLYSYLAGGMAGSVAQMFIYPVDTLKFRIQCSDLSRGQHGKSIILSNAKELYKSVGIRGYYRGVLVGILGMFPYSATDLGTFEGLKRTWIGILASRDNVDPQDVKLPNGLVMAFGALSGSTGATIVFPLNVIRTRLQTQGTSAHPATYDGFIDCFYKTTKNEGFRGLYKGLSPNLLKVAPSVAISYLVYENCKKWLGLE
Protein: Exocyst complex component SEC15 (P22224)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Note=25% cytoplasmic. 75% is associated with the cell membrane.
Interaction partners:
- Exocyst complex component SEC3
- Exocyst complex component SEC8
- Exocyst complex component EXO70
- Exocyst complex component EXO84
- Exocyst complex component SEC10
- Exocyst complex component SEC5
- Exocyst complex component SEC6
- Ras-related protein SEC4
- Rab guanine nucleotide exchange factor SEC2
- Myosin-2
Sequence:
MDQEGQPLLSKDFQQVLLATASGNNSSWTERAVLNNESTDAVKHEPALGQNDVFDLDPLSFDKWVPFLRRALDKNQLDPVIDELENSIEDNFQGLELQLLQDSQMNDKLETSIDEIANIQGMVQDTLSSEISKFQIRLSESANELIVKKQMYVNNKKISLKISEATILITKVVRILELSSKCQELITERKFFKVLQNLDSLEKLYLQEFKNYNFQFLIEIYNSIPFLQKVTKDECINLIRNSLNLNLGKNLIKVGQEFVAIYENELLPQWLETRSKMKLTNFKFNSPIEISMRDESFLAKLNLGEFFQLDDFHDSIMIFQNLNELSVLSGEFNKEYELRKTKLMYPLIWKKNKTAAYQMDSLLRGTGTTPGSTAHDVSTDDPFTQSLSLHFLQDYFLKILGFLLYDINLNKATEFILVDNNYNSTNEFWDGLMDRLSPYLSYFIDEKLKTEEDMIKLKDFLCIYVAILENFKLNIEPLYKILVSIFEKFCSVSLRAFDDEFQILLNDDDFMPLSINDKTLYEKVLKICWMKEGEHLSLPDPTNGEPFAVTLPFSPLYPMTCTLAKKTYSKITAFLSIFYRHELHTLNNILVKTMDDIFNDIVNKKIRSKLESTSREEIAQILVNLDYFIIAAKEFSNFMTRENILQNPDMEIRLSSIKYLAESRKLAETKLIELIDSKISDILETIEIDWQITEVRQDPDISIIDLAQFLEMMFASTLQNLPYSVQTLLIFREFDSLTRQFMGLLLHDTPSTITHESIMNFEVDVNYLESIIPRIFPSTPGTIDSNGYQSPMTPSTPTFPNANGVDAPTLFENNIKSLEATFMELKQCIELLKTQGKDYNEPEIRLRKYSRIRQEDAALLLSKIQHFVSSVEGANGDDTSVMDSSSIFNSESASVIDSNTSRIAKFFNRR
Protein: Carbonic anhydrase (EC 4.2.1.1) (A2VD39)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MIAFLISFLAALLCESVHSNNSAVAWCYNNPLCNFTTWPELSPHYCNGSSQSPINIVTAQVLENSNLTQFNFTGFDANTTFISMANSGISVVVTLDEEIMSVQGGDLPGLYVSKQFHLHWGNSSSFPGSEHTVDGKQYAMELHIVNVHSKYNGSLSAALAANDSSALAVLGFFIEGTNEASKAKGWGVLTSFLRNITYSGNATVDIMNRTSMNSLLEGVNKTKYYRYRGSLTTPSCNEAVIWTVFKEPIKVNNNLINLFSTTVFAKNASAPVLNVNNFRGVQPLNGRVVTSQVEQTASPTAPSSAATSISSLSLLLLLTSLCCL
Protein: Ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Phosphorylethanolamine cytidylyltransferase 1) (Q9ZVI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP-ethanolamine. Essential for early embryonic development.
Subcellular location: Mitochondrion outer membrane {ECO:0000305|PubMed:17189343, ECO:0000305|PubMed:21896887}; Single-pass membrane protein {ECO:0000305|PubMed:17189343, ECO:0000305|PubMed:21896887}.
Interaction partners:
- Choline/ethanolaminephosphotransferase 2
- Choline/ethanolaminephosphotransferase 1
- Probable ethanolamine kinase
- Probable choline kinase 2
- Probable choline kinase 1
- Probable choline kinase 3
- Phosphoethanolamine N-methyltransferase 1
- Phosphoethanolamine N-methyltransferase 2
- Phosphoethanolamine N-methyltransferase 3
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
Sequence:
MVWEKEKIVGSCIVGGAAFAVGASFLHLFLKGELPLGLGLGLSCPWRILRKRKPVRVYMDGCFDMMHYGHCNALRQARALGDQLVVGVVSDEEIIANKGPPVTPLHERMTMVKAVKWVDEVISDAPYAITEDFMKKLFDEYQIDYIIHGDDPCVLPDGTDAYALAKKAGRYKQIKRTEGVSSTDIVGRMLLCVRERSISDTHSRSSLQRQFSHGHSSPKFEDGASSAGTRVSHFLPTSRRIVQFSNGKGPGPDARIIYIDGAFDLFHAGHVEILRRARELGDFLLVGIHNDQTVSAKRGAHRPIMNLHERSLSVLACRYVDEVIIGAPWEVSRDTITTFDISLVVHGTVAESDDFRKEEDNPYSVPISMGIFQVLDSPLDITTSTIIRRIVANHEAYQKRNAKKEASEKKYYEQKSFVSGD
Protein: Protein FLOWERING LOCUS D (EC 1.-.-.-) (Protein SUPPRESSOR OF OVEREXPRESSED FCA 1) (Q9CAE3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable histone demethylase that promotes flowering independently of the photoperiod and vernalization pathways by repressing FLOWERING LOCUS C (FLC), a floral repressor that blocks the transition from vegetative to reproductive development. Probably mediates histone H3 'Lys-4' demethylation at FLC locus. Seems to act in partial redundancy with LDL1 and LDL2 to repress FLC expression. Required for histone H4 deacetylation of FLC locus. May be a component of the histone deacetylase complex. Forms a histone deacetylase complex with HDA5, HDA6 and MSI4/FVE that represses FLC gene expression to control flowering time. Required for systemic acquired resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas syringae pv tomato DC3000 (avrPto)). Together with FLD and MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a diterpenoid tricyclic diterpene) activation of flowering ans SAR.
Interaction partners:
- WD-40 repeat-containing protein MSI4
- Flowering time control protein FCA
- Histone deacetylase 6
- Flowering time control protein FPA
- Inactive protein FRIGIDA
- Protein MADS AFFECTING FLOWERING 5
- Histone deacetylase 5
- Flowering locus K homology domain
- Putative high mobility group B protein 11
- High mobility group B protein 9
Sequence:
MVSFSAPKKRRRGRSQRSMSSLNSLPVPNVGLLPGNSNFVSSSASSSGRFNVEVVNGSNQTVKSYPGIGDEIITINKEATTEALLALTAGFPADSLTEEEIEFGVVPIVGGIEQVNYILIRNHIISKWRENISSWVTKEMFLNSIPKHCSSLLDSAYNYLVTHGYINFGIAQAIKDKFPAQSSKSSVIIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEANRVGAAADLGGSVLTGTLGNPLGIIARQLGSSLYKVRDKCPLYRVDGKPVDPDVDIKVEVAFNQLLDKASKLRQLMGDVSMDVSLGAALETFRQVSGNDVATEEMGLFNWHLANLEYANAGLVSKLSLAFWDQDDPYDMGGDHCFLPGGNGRLVQALAENVPILYEKTVQTIRYGSNGVKVTAGNQVYEGDMVLCTVPLGVLKNGSIKFVPELPQRKLDCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTEDPNYRGEFFLFYSYAPVAGGALLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEPQGINVPDPLQTVCTRWGGDPFSLGSYSNVAVGASGDDYDILAESVGDGRLFFAGEATTRRYPATMHGAFVTGLREAANMAQSAKARGIRKRIDRNPSRNAHSCAILLADLFRDPDLEFGSFCIIFSRRNPDPKSPAILRVTLSEPRKRNEDPKADQHSNKILFQQLQSHFNQQQQIQVYTLLTRQQALDLREVRGGDEKRLYYLCETLGVKLVGRKGLGVGADSVIASIKAERTGRKLPSSSTSGTKSG
Protein: Membrane-associated progesterone receptor component 2 (Q80UU9)
Organism: Mus musculus (Mouse)
Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250|UniProtKB:O15173}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O15173}. Secreted {ECO:0000250|UniProtKB:O15173}.
Interaction partners:
- Membrane progestin receptor beta
- Membrane progestin receptor alpha
- Membrane progestin receptor gamma
- Progesterone receptor
- Aladin
- Cytochrome b5 type B
- Membrane progestin receptor delta
Sequence:
MAAGDGDVKLSTLGSGGESGGDGSPGGAGATAARSSWVAALLATGGEMLLNVALVALVLLGAYRLWVRWGRRGLCSGPGAGEESPAATLPRMKKRDFSLEQLRQYDGARTPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHSKQD
Protein: Abscisic acid receptor PYL12 (PYR1-like protein 12) (Regulatory components of ABA receptor 6) (Q9FJ49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 37
- Protein phosphatase 2C 56
- Protein phosphatase 2C 77
- Probable protein phosphatase 2C 75
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 7
- Probable protein phosphatase 2C 78
- Serine/threonine-protein kinase SRK2D
Sequence:
MKTSQEQHVCGSTVVQTINAPLPLVWSILRRFDNPKTFKHFVKTCKLRSGDGGEGSVREVTVVSDLPASFSLERLDELDDESHVMVISIIGGDHRLVNYQSKTTVFVAAEEEKTVVVESYVVDVPEGNTEEETTLFADTIVGCNLRSLAKLSEKMMELT
Protein: Cyclin-dependent kinase 5 activator 2 (CDK5 activator 2) (Cyclin-dependent kinase 5 regulatory subunit 2) (p39) (p39I) (Q13319)
Organism: Homo sapiens (Human)
Function: Activator of CDK5/TPKII.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18507738}; Lipid-anchor {ECO:0000269|PubMed:18507738}; Cytoplasmic side {ECO:0000269|PubMed:18507738}.
Interaction partners:
- Cyclin-dependent kinase 5
Sequence:
MGTVLSLSPASSAKGRRPGGLPEEKKKAPPAGDEALGGYGAPPVGKGGKGESRLKRPSVLISALTWKRLVAASAKKKKGSKKVTPKPASTGPDPLVQQRNRENLLRKGRDPPDGGGTAKPLAVPVPTVPAAAATCEPPSGGSAAAQPPGSGGGKPPPPPPPAPQVAPPVPGGSPRRVIVQASTGELLRCLGDFVCRRCYRLKELSPGELVGWFRGVDRSLLLQGWQDQAFITPANLVFVYLLCRESLRGDELASAAELQAAFLTCLYLAYSYMGNEISYPLKPFLVEPDKERFWQRCLRLIQRLSPQMLRLNADPHFFTQVFQDLKNEGEAAASGGGPPSGGAPAASSAARDSCAAGTKHWTMNLDR
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (B4DH19)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
MTIEIDFLQKKSIDSNPYDTDKMAAEFIQQFNNQAFSVGQQLVFSFNEKLFGLLVKDIEAMDPSILKGEPATGKRQKIEVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD
Protein: Ankyrin, isoform B (Ankyrin, isoform C) (Ankyrin, isoform D) (Ankyrin, isoform E) (LD10053p) (Q0KIE7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Karst, isoform E
- Nuclear factor NF-kappa-B p110 subunit
- Transient receptor potential cation channel trpm
- Inactive
- Neuroglian
- SD02261p
- MIP30126p
- Ankyrin 2, isoform U
- Spectrin beta chain
- Eukaryotic translation initiation factor 4G1, isoform B
Sequence:
MTLGDVRVENKIQTRSETCAINGMALDNKNGIIKQNDATISFLRAARSGDIKKVMDFLDCGEISDINSCNANGLNALHLAAKDGYVDICCELLRRGIKIDNATKKGNTALHIASLAGQHDVINQLILYNANVNVQSLNGFTPLYMAAQENHDNCCRTLLANGANPSLSTEDGFTPLAVAMQQGHDKIVAVLLENDVRGKVRLPALHIAAKKNDVNAAKLLLQHDPNADIVSKSGFTPLHIAAHYGNVDIATLLLNNKADVNYVAKHNITPLHVACKWGKLSLCTLLLCRGAKIDAATRDGLTPLHCASRSGHVEVIKHLLQQNAPILTKTKNGLSALHMAAQGEHDEAAHLLLDNKAPVDEVTVDYLTALHVAAHCGHVKVAKLLLDYKANPNARALNGFTPLHIACKKNRIKMVELLIKHGANIGATTESGLTPLHVASFMGCINIVIYLLQHEASADLPTIRGETPLHLAARANQADIIRILLRSAKVDAIAREGQTPLHVASRLGNINIIMLLLQHGAEINAQSNDKYSALHIAAKEGQENIVQVLLENGAENNAVTKKGFTPLHLACKYGKQNVVQILLQNGASIDFQGKNDVTPLHVATHYNNPSIVELLLKNGSSPNLCARNGQCAIHIACKKNYLEIAMQLLQHGADVNIISKSGFSPLHLAAQGGNVDMVQLLLEYGVISAAAKNGLTPLHVAAQEGHVLVSQILLEHGANISERTRNGYTPLHMAAHYGHLDLVKFFIENDADIEMSSNIGYTPLHQAAQQGHIMIINLLLRHKANPNALTKDGNTALHIASNLGYVTVMESLKIVTSTSVINSNIGAIEEKLKVMTPELMQETLLSDSDDESCDDLLDHNHYKYMATDDLKANYGQDQKNFDTTNTDHDLTDVSVLNKKEILPNEMSCIELTEIGHKPDNVVIARSQVHLGFLVSFLVDARGGSMRGYRHNGVRIIVPPKACAEPTRITCRYVKPQRVVNPPPLMEGEALVSRILEMSPVDGMFLSPITLEVPHYGTLRKNEREIIILRSDNGESWREHNLYKDIIGEDINQTEEFHSDRIVRIVTQNVPHFFAVVSRVRQEVHVIGPDGGTVFSTAVPQVKAIFPPHALTKKIRVGLQAQSVDLVECSKLLGQGVAVSPVVTVEPRRRKFHKAITLSIPAPKACTNSMVNACYGNGNSSSPTLRLLCSISGGQTRATWEDVTGSTPLSFVRDSVTFTTTVSARFWLIDCRNIIDAGRMATELYSHLAKVPFYVKFVIFAKRISQTEAKFSVFCMTDDKEDKTLEQQEYFKEVAKSRDIEVLQNQIVYLEFAGNIVPILKKGEQLYTKFQPFCENRLSFSAHIKDQEFPHGRICFMTYPMVGPDEVPLKPLCTLNISVDFKTITNHLERDNLHSLNDCINAHGKLNHNENIVFGVKEQQVKKIDITKACIMSSDIKLIHEADVILDDICSHLGSDWPLLANVLGVSQADIDLVKTEFLLNDSVKQSMAMLQLWLEHGGILTGNVLAEALYKIGRSDIVEKSFKNAEFGTHQPEKVLPTAGIEKDGDYEQ