wanglab/gogpt-training-data huggingface dataset:
Protein: Calcium-dependent protein kinase 7 (EC 2.7.11.17) (Q8IID2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGLQTEKDKEKEHQKNNFKICSKKFETDELEVLKKIYKELGSRSGSSYIDKETFLQFFPLPGLWGERLFLKFNFKNTGFIDFEEFIIGIAICCRGTKSDKINVLFDIFDLNADGFIQKSEMVAMLSNIPYIHKLKNIFFNKDNRKNIYRDDYTKDDDNADDENEDHENGDAIIDSNVGTNSDGNIDIDSDADVEYNDSDSDDFTIDDDEDVDSLDDISDSFSSAYEDEDEYSNNNNNNNNNNIENMNISSDNKNVEENNIGNCSKCIKQQKNKALNANINSKRNANGNNTSLNVKELAKKIRKEEKRKFVKKLRELNAVHLYKDNQLSNKKEKDKERKKKNKDPNVSKNSPFFKSESEDYNSSSSNNTDAFVHDHIKYINKYKKKSLKNEVKKNGHKYKDTTNPYISSTTDSSTSNESNYNINNDEFESCSSNKDHREVCSSDTSDSFISIYGYLIKNRRSKNIKEKNHHSKEKDKKDQDVKGKNKADDNIKRKEKGDDEIKRKDKPLDDIKEKEQIKYEAKNKDHKMKEEISEGKENLKYKDVEKKKDGEKNKDGEKNKDGEKNKDGEKNKDGEKKKDGEKKKDGEKEEGKNEEKENEEENKIKKEKCFTRNDINIYKKEKKKEKKKNKLYVNEFCLPSKTARSILNDEENNKPSDKNVDVEAIVDIMLEECEFLDNDKITLIQFKSVIHKYDFFLYIFFNCLHEDIWGLQGNVLYGRDYISNFVIKSENFKNKEIEQDEDDAITEELYFKIRQLFIVQAPDYDCVNDDLCVNFLNTKNIEQDIKEDDEEEKEKEEKKNGADKKDTIEKEEEEYITNNFSKDKNDTSINKKKTKNENNAKLVSFVSDIKTGEENIVDKDKIKEYEKEYSIHKDKDDKKNANSSFESEHEDLKRQFINMKEKKKKSLKEKDELNNMKEDNKIYKKLEEYDKKSINNIENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQNENQKNNNNILKEKNSYEDDKGKIKVINNEIKKSVHHLSDNVSDLSYDEKWLKLSSNGTNKKKELNNDNSNNFDESQRIQEYQNDNKNNVIEENNILINQKKNSHNMKEDSINIQVDMKSNIHMNIIINKVNDMNDVNDVNNANDVNNVNDVNNVNDMNNVEGINNEQKENDFVKMNKQNTNRNELMSKKDIVGKNNTTIINNNMTNLNDDLLNVENTENKNRYECDFNLLTNQLNDIFSKEIVEFIQASKISFNINDVCKERNLHKKKERLQKGRRNYLKNNKNNLNISLNYQKQKKYPFNKLFLEELEKDEKNEEINKAEEHVTDESSFEYNQNGVFRNKVVPTKTNKNVSTINNQNNEEDMKQKEKDVNEQTVEKKEDNNILINKLCKKKSFSGLKLQNIEKMDILEKFGLSYKKSEKTSLGCSIFHNKVDEKRGSFSKSQDGIEADVIKQGELNNEKVKKNETNDDKAKKNETYDDKAKKNETYDDKAKKNETYDDKAKKNETYDDKAKKNETYDDKAKKNETYDEKVKKNETYDEKVKKNETYDEKVKKNETYDEKVKKNEQKCEDLKEPISNVDKISYQKSTSDKDLSKKKNSNVGALNKMDTFKKDESSSNDMASSYFSSNKKKKYDLTKKHGKDINLYSCPNCKGPFLMCPNCHCRYPRFCVNDNKIAMECEYCDCEHCYFYNCIYCNFDFQKCLDMIKKNSLKEGILYKIGKHLHQFKARYYILFDNLLYYYDKKRNLKPRGFMFLEGCYVELIAKNDNINKYGFSICHKGTKQVQKRNLYVNTLEERDEWVQALYSSTKQNTLYNLYELHEQLGQGKFSTVYRGINKQTNSEFAIKVIDKRSVSIYEKELLRSEISILRLLRHPNVIYLKEIINTKETLYISMELVKGGELYDFLLAETRLSEIHANKIITQLIKTVAYLHRCGIIHRDIKPENILLTDKSRDAQIKLTDFGLSTLCAPNELLKEPCGTLAYVAPEVITLQGYNHKVDAWSIGIILYLLLSGKLPFPINKNTEMNIQKNYVLSFKDYIWKSISSSAKDLISKLLELNVEKRISANEALEHIWVKNPTAVINENSFIYKNEEINILNLQDVSVSTFNIPRYTPLHIEEEKNTEEIENKELIFNIHENNILCENNDSIDEPVIPLPYSSAPLKEHINEKKNIQNISSPMEDISMNKQENAVYESINKETSNPMKNCSQNVRDQNDTTPHHNNENQNEQGNLNTCIHKINECKKSSTDGHTVQINDNTNKEHDK
Protein: UPF0500 protein C1orf216 (Q8TAB5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFAIQPGLAEGGQFLGDPPPGLCQPELQPDSNSNFMASAKDANENWHGMPGRVEPILRRSSSESPSDNQAFQAPGSPEEGVRSPPEGAEIPGAEPEKMGGAGTVCSPLEDNGYASSSLSIDSRSSSPEPACGTPRGPGPPDPLLPSVAQAVQHLQVQERYKEQEKEKHHVHLVMYRRLALLQWIRGLQHQLIDQQARLQESFDTILDNRKELIRCLQQRAAPSRPQDQA
Protein: Chaperone protein dnaJ 15 (AtDjB15) (AtJ15) (Protein ALTERED RESPONSE TO GRAVITY) (AtARG1) (Q9ZSY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a continuous role in plant development probably in the structural organization of compartments (By similarity). Seems to be involved in early gravitropic signal transduction within the gravity-perceiving cells (statocytes), where it influences pH changes and auxin distribution. Probably affects the localization and/or activity of auxin efflux carrier components (PIN proteins) or other proteins involved in lateral auxin transport.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14507996}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14507996}; Peripheral membrane protein {ECO:0000269|PubMed:14507996}. Golgi apparatus membrane {ECO:0000269|PubMed:14507996}; Peripheral membrane protein {ECO:0000269|PubMed:14507996}. Note=Found in endoplasmic reticulum, Golgi, vesicles near the plasma membrane and around cell plate, and bound to the plasma membrane. Probably interacts with integral membrane proteins. Also interacts with cytoskeleton.
Interaction partners:
- At2g15220/F15A23.4
- Solute carrier family 40 member 3, chloroplastic
- Translocase of chloroplast 132, chloroplastic
- Auxin efflux carrier component 3
- Auxin efflux carrier component 2
- Protein TOC75-3, chloroplastic
- Translocase of chloroplast 120, chloroplastic
Sequence:
MSAKKLEGSSAPANRRDPYEVLCVSKDANDQEIKSAYRKLALKYHPDKNANNPDASELFKEVAFSYSILSDPEKRRHYDNAGFEALDADGMDMEIDLSNLGTVNTMFAALFSKLGVPIKTTVSANVLEEAMNGTVTVRPLPIGTSVSGKVEKQCAHFFGVTISEQQAESGVVVRVTSTAQSKFKLLYFEQDSSGGYGLALQEEREKTGKVTSAGMYFLHFQVYRMDTTVNALAAAKDPESAFFKRLEGLQPCEVSELKAGTHIFAVYGDNFFKTASYTIEALCAKTYEDTTEKLKEIEAQILRKRNELRQFETEYRKALARFQEVTNRYTQEKQTVDELLKQRDTIHSTFSVVKTPSGNNLSNGSSSKAQGDESKGDGDSAGEEGGTENRDKSKRKWFNLNLKGSDKKLG
Protein: Btn1a1 protein (Butyrophilin, subfamily 1, member A1) (Q921X1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAVPTNSCLLVCLLTLTVLQLPTLDSAAPFDVTAPQEPVLALVGSDAELTCGFSPNASSEYMELLWFRQTRSTAVLLYRDGQEQEGQQMTEYRGRATLATAGLLDGRATLLIRDVRVSDQGEYRCLFKDNDDFEEAAVYLKVAGGYRRDVSPRHSARRLSLWGESSCSFSKSKRIFTFT
Protein: Phosphoinositide 3-kinase regulatory subunit 4 (PI3-kinase regulatory subunit 4) (EC 2.7.11.1) (Q8VD65)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and cytokinesis, probably in the context of PI3KC3-C2 (By similarity).
Subcellular location: Late endosome {ECO:0000250}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Membrane {ECO:0000250|UniProtKB:Q99570}; Lipid-anchor {ECO:0000250|UniProtKB:Q99570}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes. Localizes also to discrete punctae along the ciliary axoneme (PubMed:24089209). {ECO:0000269|PubMed:24089209, ECO:0000305}.
Interaction partners:
- Activating molecule in BECN1-regulated autophagy protein 1
- Nuclear receptor-binding factor 2
- Beclin-1
- Beclin 1-associated autophagy-related key regulator
- UV radiation resistance-associated protein
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- RB1-inducible coiled-coil protein 1
- Serine/threonine-protein kinase ULK2
- Serine/threonine-protein kinase ULK1
- Autophagy-related protein 13
Sequence:
MGNQLAGIAPSQILSVESYFSDIHDFEYDKSLGSTRFFKVARAKHREGLVVVKVFAIQDPTLPLTSYKQELEELKIRLHSAQNCLPFQKAAEKASEKAAMLFRQYVRDNLYDRISTRPFLNNIEKRWIAFQILTAVDQAHKSGVRHGDIKTENVMVTSWNWVLLTDFASFKPTYLPEDNPADFNYFFDTSRRRTCYIAPERFVDGGMFATELEYMRDPSTPLVDLNSNQRARGELKRAMDIFSAGCVIAELFTEGVPLFDLSQLLAYRNGHFFPEQVLNKIEDRSIRDLVTQMINREPEKRLEAEDYLKQQRGNAFPEIFYTFLQPYMAQFAKETFLSADERILVIRKDLGNIIHNLCGHDLPEKAEGESRASGLVVLVSVITSCLQTLKSCDSKLAALELILHLAPRLSVEILLDRITPYLLHFSNDSVPRVRAEALRTLTKVLALVQEVPRNDVNIYPEYILPGIAHLAQDDATIVRLAYAENIALLAETALRFLELVQLKTLNMENEPDNEEVDEATRPNGDYDTELQALHEMVQQKVVTLLSDPENIVKQTLMESGITRLCVFFGRQKANDVLLSHMITFLNDKNDWHLRGAFFDSIVGVAAYVGWQSSSILKPLLQQGLSDAEEFVIVKALNALTCMCQLGLLQKPHVYEFASDIAPFLCHPNLWIRYGAVGFITVVAHQISTADVYCKLMPYLDPYITQPVIQIERKLVLLSVLKEPVSRSIFDYALRSKDIASLFRHLHMRQKKRNGSLLDCPPPEDPTIAQLLKKLLSQGMTEEEEDKLLALKDFMMKSNRAKANAVDQSHLHDSSQKGVIDLAALGITGRQVDLVKTKQEPDEKRARKHVKQDSNVNEEWKSMFGSLEPPNIPQALPKTSDHEVVQPGKPPRSESSAGICVPLSTSPQVSEAAHIPSKKPVIPVVSSTVLPSTYQIRITTCKTELQQLIQQKREQCNAERIAKQMMENAEWESKPPPPGWRPKGLLVAHLHEHKSAVNRIRVSDEHLLFATCSNDGTVKIWNSQKMEGKTTTTRSILTYSRIGGRVKTLTFCQGSHYLAIASDNGAVQLLGIEASKLPKSPKIHPLQSRILDQKEDGCVVDMHHFNSGAQSVLAYATVNGSLVGWDLRSSSNAWTLKHDLKSGLITSFAVDIHQCWLCIGTSSGAMACWDMRFQLPISSHCHPSRARIRRLSMHPLYQSWVIAAVQGNNEVSMWDMETGDRRLTLWASSAPPLSELQPSPHSVHGIYCSPADGNPILLTAGSDMKIRFWDLVSPERSYVVAGSTGSPSVSYYKKIIEGTEVVQEIQNKQKVGPSDDTPRRGPESLPVGHHDIITDIATFQTTQGFIVTASRDGIVKVWK
Protein: Wnt ligand secretion mediator (E9PKJ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRR
Protein: Numb (Q3MUI1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MNKLRQSFRRKKDVYVPEASRPHQWQTDEEGVRTGKCSFPVKYLGHVEVDESRGMHICEDAVKRLKATGKKAVKAVLWVSADGLRVVDEKTKDLIVDQTIEKVSFCAPDRNFDRAFSYICRDGTTRRWICHCFMAVKDTGERLSHAVGCAFAACLERKQKREKECGVTATFDASRTTFTREGSFRVTTATEQAEREEIMKQLQDAKKAETDKTVGPSVAPGNSAPSPSSPTSPTLDPTASLEMNNPHAIPRRHAPIEQLARQGSFRGFPALSQKMSPFKRQLSLRINELPSTMQRKTDFPIKNTVPEVEGEAESISSLCSQITSAFSTPCEDPFSSAPMTKPVTLVAPQSPVLQGTEWGQSSGAASPGLFQAGHRRTPSEADRWLEEVSKSVRAQQPQASAAPLQPVLQPPPPAAIAPPAPPFQGHAFLTSQPVPVGVVPPLQPAFVSTQSYPVANGMPYPASNVPVVGITPSQMVANVFGTAGHPQATHPHQSPSLAKQQTFPQYETSSATTSPFFKPSAQHLNGSAAFNGVDNSGLVSGNRPAQVPPGTCPVDPFEAQWAALESKPKQRTNPSPTNPFSSDAQKAFEIEL
Protein: Pantothenate kinase 1 (mPank) (mPank1) (EC 2.7.1.33) (Pantothenic acid kinase 1) (Q8K4K6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of pantothenate to generate 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) synthesis. Required for the hepatic CoA increase during the switch from glucose to fatty acid oxidation that occurs in the fasting state.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:23152917}. Nucleus, nucleolus {ECO:0000269|PubMed:23152917}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16040613, ECO:0000269|PubMed:23152917}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:23152917}. Recycling endosome {ECO:0000269|PubMed:23152917}.
Interaction partners:
- Bifunctional coenzyme A synthase
- Phosphopantothenoylcysteine decarboxylase
- Phosphopantothenate--cysteine ligase
- Pantetheinase
- Pantothenate kinase 3
- Pantothenate kinase 2
- Vascular non-inflammatory molecule 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MRGRRAPRPGSTEVPAAARDADTLRARAASPVRGAQLAEDVGTPTGGGEERRGHQLPTAAPRLRESKPQGGSEDRGTADRDLQRGCQSRSPRTAPPVPGMGDRGAQHERAALQSPGAPEGAAAAVNGLLHNGFHPSAASSRDPPAPRFQLPSELQPQPLFAQHDSPAKKCRLRRRMDSGRKNRPPFPWFGMDIGGTLVKLVYFEPKDITAEEEQEEVENLKSIRKYLTSNTAYGKTGIRDVHLELKNLTMCGRKGNLHFIRFPTCAMHLFIQMGSEKNFSSLHTTLCATGGGAFKFEEDFRMIADLQLHKLDELDCLIQGLLYVDSVGFNGKPECYYFENPTNPELCQKKPYCLDNPYPMLLVNMGSGVSILAVYSKDNYKRVTGTSLGGGTFLGLCCLLTGCETFEEALDMAAKGDSTNVDKLVKDIYGGDYERFGLQGSAVASSFGNMMSKEKRESISKEDLARATLVTITNNIGSIARMCALNENIDRVVFVGNFLRINMVSMKLLAYAMDFWSKGQLKALFLEHEGYFGAVGALLELFKMTDTQ
Protein: Large ribosomal subunit protein uL23y (60S ribosomal protein L23a-2) (Q9M3C3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to a specific region on the 26S rRNA.
Interaction partners:
- Small ribosomal subunit protein eS24y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL6z/uL6y
- Large ribosomal subunit protein eL19x
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein uL4z
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein uL24z
- Large ribosomal subunit protein uL30y
- Large ribosomal subunit protein uL18y
Sequence:
MSPAKVDVTKKADPKAKALKAAKAVKSGQIVKKPAKKIRTKVTFHRPKTLTVPRKPKYPKISATPRNKLDHYQILKYPLTTESAMKKIEDNNTLVFIVDIRADKKKIKDAVKKMYDIQTKKVNTLIRPDGTKKAYVRLTPDYDALDVANKIGII
Protein: CCR4-NOT transcription complex subunit 7 (EC 3.1.13.4) (CCR4-associated factor 1) (CAF-1) (Q60809)
Organism: Mus musculus (Mouse)
Function: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT8. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Required for miRNA-mediated mRNA deadenylation. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:20133598}. Cytoplasm, P-body {ECO:0000269|PubMed:20133598}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q9UIV1}. Note=NANOS2 promotes its localization to P-body (PubMed:20133598). Recruited to cytoplasmic ribonucleoprotein membraneless compartments by CAPRIN1, promoting deadenylation of mRNAs (By similarity). {ECO:0000250|UniProtKB:Q9UIV1, ECO:0000269|PubMed:20133598}.
Interaction partners:
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 6-like
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 4
- CCR4-NOT transcription complex subunit 10
- Protein PAT1 homolog 1
- CCR4-NOT transcription complex subunit 11
Sequence:
MPAATVDHSQRICEVWACNLDEEMKKIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFMNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTTSGIQFKKHEEEGIETQYFAELLMTSGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEEELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELERIGPQHQAGSDSLLTGMAFFKMREMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEASKQS
Protein: C5a anaphylatoxin chemotactic receptor 1 (C5a anaphylatoxin chemotactic receptor) (C5a-R) (C5aR) (CD antigen CD88) (P97520)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a. The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events. Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12464600, ECO:0000269|PubMed:9464523}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21730}. Cytoplasmic vesicle {ECO:0000269|PubMed:12464600}. Note=Phosphorylated C5aR colocalizes with ARRB1 and ARRB2 in cytoplasmic vesicles. {ECO:0000269|PubMed:12464600}.
Interaction partners:
- Complement C5
- Small ribosomal subunit protein eS19
- C-C chemokine receptor type 5
- Integrin alpha-D
- Toll-like receptor 2
Sequence:
MDPISNDSSEITYDYSDGTPNPDMPADGVYIPKMEPGDIAALIIYLAVFLVGVTGNALVVWVTAFEAKRTVNAIWFLNLAVADLLSCLALPILFTSIVKHNHWPFGDQACIVLPSLILLNMYSSILLLATISADRFLLVFKPIWCQKFRRPGLAWMACGVTWVLALLLTIPSFVFRRIHKDPYSDSILCNIDYSKGPFFIEKAIAILRLMVGFVLPLLTLNICYTFLLIRTWSRKATRSTKTLKVVMAVVTCFFVFWLPYQVTGVILAWLPRSSSTFQSVERLNSLCVSLAYINCCVNPIIYVMAGQGFHGRLRRSLPSIIRNVLSEDSLGRDSKSFTRSTMDTSTQKSQAV
Protein: Late expression factor 3 (LEF-3) (Single-stranded DNA-binding protein) (SSB) (P41453)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Single-stranded DNA-binding protein that plays a role in viral DNA replication. Forms a stable complex with the alkaline nuclease and mediates the transport of the helicase to the host nucleus.
Subcellular location: Host nucleus {ECO:0000269|PubMed:16103143, ECO:0000269|PubMed:19073335, ECO:0000269|PubMed:9683569}.
Interaction partners:
Sequence:
MATKRSLSGESSGEPLIKRMAMASSPKKIRENYKRISGKLMSKMTLSIDNEYHYTFRIMSDNKIQEYYGDSQSFKDMEEGKCYDISLNYVKTKFSQMIQINEYKECEMEIETATPMSDYLTNKHFENEDGVNIIVKYKFIYKKINSGLYKVVFEVVYKNLNDDPDVVQVECSVNAKTLINLFKNNIKGSDDINEVFKYLKDNENQIFTIYSIKCQQIFNGSNVYMNWNVVNSTRIELCEAKESEAYSNLQNCTNAKINISRSNKHVASYNVNVLKSELEENDMGDNKFIVQFKSDELNIADSDDCSTSSDLGKWNKSVFYVNTNKKTEADSLQKLCADFNQISMLLEDNLIKVTIYVTVENGENHNMNVLGLLKYDEDENEYKFL
Protein: Zinc finger and BTB domain-containing protein 32 (Repressor of GATA) (Testis zinc finger protein) (Q9JKD9)
Organism: Mus musculus (Mouse)
Function: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3' core sequence. May function as a transcriptional transactivator and transcriptional repressor (By similarity). Probably exerts its repressor effect by preventing GATA3 from binding to DNA. May play a role in regulating the differentiation and activation of helper T-cells.
Subcellular location: Nucleus. Note=Located in nuclear speckles. {ECO:0000250}.
Interaction partners:
Sequence:
MPQTPTRLVSPYGSDRLVQLAARLRPALCDTLITVGGLEFPAHSLVLAGASPRLGCRGRWALVEDISPSTFAQILTFVYGESIELQPGELGDLEEAAKALGVQALEEACQRAQKGKDEDELDPGLKRHQQSEDFMRGSERGLGSPGEKQKPEKDFRSNGREQEMSHKHKAPGERPEMAGATRMMSSEEVMRGIESHKGSEESLRGCPDPLSPPGSLLTSLIPRPWWAEVPRLGEGQSALWSILLWPSRYGAPFSHSTPITAAWQVRPQDQRIPLTLNHSKALWSQNQLASSSPTPGSFPQGTESLSPWQIETSGQGFTGTLATCVSQERTLNCPSHQHPPLPSPARSRPYSCSVCGKRFSLKHQMETHYRVHTGEKPFSCSLCPQRSRDFSAMTKHLRTHGAAPYRCPLCRAGCPSLASMQAHMRGHSPSRLPPGWTIRSTFLYSSSRPTRASSSPGSPTSSAAT
Protein: LysM domain receptor-like kinase 3 (LysM-containing receptor-like kinase 3) (MtLYK3) (EC 2.7.11.1) (LysM receptor kinase K1B) (Protein HAIR CURLING) (Q6UD73)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Putative receptor for S.meliloti Nod factor signals essential for the establishment of the nitrogen-fixing, root nodule symbiosis with S.meliloti. Involved in the control of root hair curling after S.meliloti infection, probably by modulating the reorganization of the microtubular cytoskeleton in epidermal and cortical cells. Regulates a subset of Nod factor-induced genes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20971894, ECO:0000269|PubMed:25351493}; Single-pass membrane protein {ECO:0000255}. Vacuole lumen {ECO:0000269|PubMed:25351493}. Note=Removed from the plasma membrane upon the release of rhizobia into the host cytoplasm. Vacuolar localization is observed in cells undergoing breakdown of the receptors. {ECO:0000269|PubMed:25351493}.
Interaction partners:
- U-box domain-containing protein 1
- Serine/threonine receptor-like kinase NFP
- Protein VAPYRIN
- Myosin heavy chain-like protein, putative
Sequence:
MNLKNGLLLFILFLDCVFFKVESKCVKGCDVALASYYIIPSIQLRNISNFMQSKIVLTNSFDVIMSYNRDVVFDKSGLISYTRINVPFPCECIGGEFLGHVFEYTTKEGDDYDLIANTYYASLTTVELLKKFNSYDPNHIPVKAKINVTVICSCGNSQISKDYGLFVTYPLRSDDTLAKIATKAGLDEGLIQNFNQDANFSIGSGIVFIPGRDQNGHFFPLYSRTGIAKGSAVGIAMAGIFGLLLFVIYIYAKYFQKKEEEKTKLPQTSRAFSTQDASGSAEYETSGSSGHATGSAAGLTGIMVAKSTEFTYQELAKATNNFSLDNKIGQGGFGAVYYAELRGEKTAIKKMDVQASSEFLCELKVLTHVHHLNLVRLIGYCVEGSLFLVYEHIDNGNLGQYLHGIGTEPLPWSSRVQIALDSARGLEYIHEHTVPVYIHRDVKSANILIDKNLRGKVADFGLTKLIEVGNSTLHTRLVGTFGYMPPEYAQYGDVSPKIDVYAFGVVLYELITAKNAVLKTGESVAESKGLVQLFEEALHRMDPLEGLRKLVDPRLKENYPIDSVLKMAQLGRACTRDNPLLRPSMRSIVVALMTLSSPTEDCDDDSSYENQSLINLLSTR
Protein: Dihydropyrimidinase-related protein 1 (DRP-1) (Collapsin response mediator protein 1) (CRMP-1) (Inactive dihydropyrimidinase) (Q62950)
Organism: Rattus norvegicus (Rat)
Function: Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton (By similarity). Plays a role in axon guidance (By similarity). During the axon guidance process, acts downstream of SEMA3A to promote FLNA dissociation from F-actin which results in the rearrangement of the actin cytoskeleton and the collapse of the growth cone (By similarity). Involved in invasive growth and cell migration. May participate in cytokinesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14194}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14194}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14194}. Cell projection, growth cone {ECO:0000250|UniProtKB:P97427}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P97427}. Perikaryon {ECO:0000250|UniProtKB:P97427}. Note=Associated with centrosomes and the mitotic spindle during metaphase (By similarity). Colocalizes with FLNA and tubulin in the central region of DRG neuron growth cone. Following SEMA3A stimulation of DRG neurons, colocalizes with F-actin (By similarity). {ECO:0000250|UniProtKB:P97427, ECO:0000250|UniProtKB:Q14194}.
Interaction partners:
- Dihydropyrimidinase-related protein 3
- Semaphorin-3A
- Guanine deaminase
- Stress-induced-phosphoprotein 1
- Plexin-A1
- Cyclin-dependent kinase 5
- Plexin-A4
- Dihydroorotate dehydrogenase
- Neuropilin-1
- Dihydropyrimidine dehydrogenase [NADP
Sequence:
MSHQGKKSIPHITSDRLLIRGGRIINDDQSFYADVYLEDGLIKQIGENLIVPGGVKTIEANGRMVIPGGIDVNTYLQKPSQGMTSADDFFQGTRAALAGGTTMIIDHVVPEPGSSLLTSFEKWHEAADTKSCCDYSLHVDITSWYDGVREELEVLVQDKGVNSFQVYMAYKDLYQMSDSQLYEAFTFLKGLGAVILVHAENGDLIAQEQKRILEMGITGPEGHALSRPEELEAEAVFRAIAIAGRINCPVYITKVMSKSAADIIALARKKGPLVFGEPIAASLGTDGTHYWSKNWAKAAAFVTSPPLSPDPTTPDYLTSLLACGDLQVTGSGHCPYSTAQKAVGKDNFTLIPEGVNGIEERMTVVWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDADVVIWDPDKMKTLTAKSHKSTVEYNIFEGMECHGSPLVVISQGKIVFEDGNISVSKGMGRFIPRKPFPEHLYQRVRIRSKVFGLHSVSRGMYDGPVYEVPATPKHAAPAPSAKSSPSKHQPPPIRNLHQSNFSLSGAQIDDNNPRRTGHRIVAPPGGRSNITSLG
Protein: Rab5 GDP/GTP exchange factor (Q8I100)
Organism: Caenorhabditis elegans
Interaction partners:
- FYVE-type domain-containing protein
- small monomeric GTPase
- Vacuolar fusion protein MON1 homolog
- PH domain-containing protein
- FYVE-type domain-containing protein
Sequence:
MSDKHGEEDKKAKMHLKANDLLCVNGCGFYGTPQWENRCSKCWRAHQNEMKKCQDFAKNRSLLSFDQFQERRKSTTESKSRGIKNLFKTSPIPEGGTSSPTSTSPASTPTRRRELSPDSLEARQQFTDFLVANLSTGMAQEIARSVKNAVNKISEMRMSSDDMSELVMSYYQYLGERIGGHSLFDSPDCKVKVEDVMDQVEKYISTFCYSIFFCANHEEEVADMSLQDRIRSLHWVTAGFLETKMVFKKQTVRDKIDEAISELIEINAKRSAFEKLDCLTKSCKAIFEALKESEASTSADEFLPTLIYVLFRGNPPLIQSNVKFISRFAIPARLMSGEAAYFFTNLSCALEFARNMNHESLQMEKSEFEAYTSGHLAPPLSVINSACNQAIYVLEGTIETITNVAKKAGSLAKNLTNMHGKSDDDLEKMLAVIKETVDFYPTDEYMNMKQSIFAEEKETADILVSLSRQSSESGRGTLTDTQPSTPQPDTSLESPLIAEIQAINLTSSGNQEHVEEA
Protein: Rho GTPase-activating protein 42 (Rho-type GTPase-activating protein 42) (B2RQE8)
Organism: Mus musculus (Mouse)
Function: May influence blood pressure by functioning as a GTPase-activating protein for RHOA in vascular smooth muscle.
Interaction partners:
Sequence:
MGLPTLEFSDSYLDSPDFRERLQCHEIELERTNKFIKELLKDGSLLIGALRNLSMAVQKFSQSLQDFQFECIGDAETDDEISIAQSLKEFARLLIAVEEERRRLIQNANDVLIAPLEKFRKEQIGAAKADSQIGREHQNFYEASLEYVFKIQEVQEKKKFEFVEPLLSFLQGLFTFYHEGYELAQEFAPYKQQLQFNLQNTRNNFESTRQEVERLMQRMKSANQDYRPPSQWTMEGYLYVQEKRPLGFTWTKHYCTYDKGSKMFTMSVSDVKASGKMNGLVTGSPEMFKLKSCIRRKTDSIDKRFCFDIEVVERHGIITLQAFSEANRKLWLEAMDGKEPIYTLPAIISKKEEMYLNEAGFNFVRKCIQAVEMRGITILGLYRIGGVNSKVQKLMNTTFSPKSPPDMDIDIELWDNKTITSGLKNYLRCLAEPLMTYKLHKDFIIAVKSDDQNYRVEAVHALVHKLPEKNREMLDILIKHLLKVSLHSQQNLMTISNLGVIFGPTLMRAQEETVAAMMNIKFQNIVVEILIEHYEKIFHTAPDPNIPLPQPQSRSGSRRTRAICLSTGSRKPRGRYTPCLAEPDSDSYSSSPDSTPMGSIESLSSHSSEQNSTTKSTACQPREKSGGIPWITTPSSSNGQKSQGLWTTSPESSSREDATKTDVESDCQSVASITIPGNVSPPIDLVKKGPYGLSGLKRSSASSSLRSISAAEGNKSYSGSIQSLTSIGSKESPKAIPNPELPPKMCRRLRLDTASSNGYQRPGSVVAAKAQLFENAGSPKPVSSGRQAQAMYSCKAEHSHELSFPQGAIFSNVHPSVEPGWLKATYEGRTGLVPENYVVFL
Protein: proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (Q86P96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNKASRIFCPALITPKNAVVKQTEQLSRSQKLLTELGFVKSGSNGTYQIMPMAQRSVDKCIDLVQSNMQQAGGQKITLPILTPTGLWKKTGRLDGDISEFYMVRDRSGKQFLMSPTHEEAVTAMLATTSPISYRQLPLRLFQIGPKFRDELKTRFGLMRAKEFLMKDMYSFDVSEETAMETYTVVNAAYDRLFKQLEVPFVKVNAATGIMGGSVSHEYHYVSPVGEDNLLQCSSCGFAGNSEVVKAPASCPSCNSSDLKEVRGVEVAHTFLLGDKYSKPLGATFLNTSGKPQSLVMGCYGIGITRVIAAALEVLSSDHELRWPKLLAPYDVCLIGPKQGSKEQPEAEVIENELLLNVGEICGHQELLHDDRKELTIGKRLLEAKRLGHPLTIVVGAKSARLDSPKLEVHTSKGETYELDFSETLKLVAEHSQHKKSLKRGCFQSETDESKSRSVGHQL