wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase RIPK (EC 2.7.11.1) (ACIK1A/PBL14) (ACRE protein ortholog 264A) (AtACRE264a) (PBS1-like protein 14) (RPM1-induced protein kinase) (Q9ZUF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase involved in disease resistance. During Pseudomonas syringae infection, and in response to the bacterial effectors AvrB and AvrRpm1, RIPK phosphorylates the host target RIN4, which subsequently activates RPM1-dependent effector-triggered immunity (ETI). Seems to act as negative regulator of plant basal defense responses and may play a role in pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI). Required for the bacterial XopAC/AvrAC effector-triggered immunity against Xanthomonas campestris.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21320696}.
Interaction partners:
- RPM1-interacting protein 4
- Disease resistance protein RPM1
- Protein RALF-like 1
- Protein NOI4
- GPI-anchored protein LLG1
- ATPase 2, plasma membrane-type
- ERBB-3 BINDING PROTEIN 1
Sequence:
MAVKKKVSWRSLIVGCLGDPETLMASSKKPKRKNDVIKKQSSFQRLSILDMSNPSSNTLSEDLSISLAGSDLHVFTLAELKVITQSFSSTNFLGEGGFGPVHKGFIDDKLRPGLKAQPVAVKLLDLEGLQGHREWLTEVMFLGQLKHKNLVKLIGYCCEEEHRTLVYEFMPRGSLENQLFRRYSASLPWSTRMKIAHGAATGLQFLHEAENPVIYRDFKASNILLDSDYTAKLSDFGLAKDGPEGDDTHVSTRVMGTQGYAAPEYIMTGHLTARSDVYSFGVVLLELLTGRRSVDKKRSSREQNLVDWARPMLNDPRKLSRIMDPRLEGQYSETGARKAATLAYQCLSHRPKNRPCMSAVVSILNDLKDYNDIPMGTFTYTVPNTPDNKEDDGRVGNKPRKSSHHHHHQQQQSNHPRSSPSPTTKSPSPTAKSPRNSTENHRRTLRNGVNSPLRSEAGGERY
Protein: Leukotriene B4 receptor 1 (LTB4-R 1) (LTB4-R1) (Q9R0Q2)
Organism: Rattus norvegicus (Rat)
Function: Receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Leukotriene B4 receptor 2
- Leukotriene A-4 hydrolase
- Cysteinyl leukotriene receptor 1
- Leukotriene C4 synthase
Sequence:
MAANTTSTAATSSPGGMSLSLLPIVLLSVALVVGLPGNSFVVWSILKRMQKRSVTALLVLNLALADLAVLLTAPFFLHFLARGTWSFEVTGCRLCHYVCGVSMYASVLLITIMSLDRSLAVARPFVSQKVRTKAFARWVLAGIWVVSFLLAIPVLVYRTVTPKNKTLICDSRYPSDGHKVFHLLFEAITGFLLPFLAVVASYSDIGRRLQARRFRRSRRTGRLVVLIILAFAAFWLPYHLVNLVEAGRTLAGWDKNSPAGQRLKLARYVLIALAFLSSSVNPVLYACAGGGLLRSAGVGFVVKLLEGTGSEVSSTRRGGTLVQTPKATPTCPEPGPTDSFMTSSTPPESSK
Protein: UmuC domain-containing protein (O50419)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv3395c
- Error-prone DNA polymerase
- Putative lipoprotein LppK
- Beta sliding clamp
- Calcineurin-like phosphoesterase domain-containing protein
- Protein RecA
- DNA polymerase I
Sequence:
MMASARVLAIWCMDWPAVAAAAAAGLSATAPVAVTLANRVIACSATARAAGVRRGLRRREAAARCPQLFIATADADRDARLFEGVIAAVDDLVPRAELLRPGLLVLPVRGPARFFGSEQMAAERLIDAVAAAGAECQVGIADRLSTAVFAARAGRIVEPGGDARFLSLLSIRQLATEPSLSGPGRDDLTDLLWRMGIRTIGQFAALSRTDVASRFGADAVAAHRFARGEPERAPCGREPPPDLAAELACDPPIDRVDAAAFAGRSLAAELHRALMAAGVGCTRLAIHAVTANGEERSRVWRCAEPLTEDATADRVRWQLDGWLNNRNARDRPTAAVTLLRLQAVETVSASEGLQLPLWGGLGEQDRLRARRALVRVQGLLGPEAVRVPVLSGGHGPAERITLTVLGLVAPEPVPQADPGQPWPGRLPDPSPAVLFDDPVDLLDAQGNPIRVTSRGMFSADPARLRVRGRDDRLRWWAGPWPDDERWWDPDRASGRTARAQVLLDGDPGTALLLCYRQRRWYLEGSYE
Protein: Uncharacterized protein (Q9I550)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
- Probable transcriptional regulator
Sequence:
MFQSTEQALAVAYWMFEHQPGPKSSTAMVIDGLRERFDRSFIEHLPSGLSPHEWQAQAVMTVRFAQRQLAAHPLELAVVRAEFARGRDFVLGLAALRDWLKPGADPIEQRATLALLMRMFRRPPSSIREIERLSGLSKSTLHRWDKEWRERVVALLRQALQRLEEPMAEVGIVGER
Protein: Polyserase-2 (EC 3.4.21.-) (Polyserine protease 2) (Serine protease 36) (Q5K2P8)
Organism: Mus musculus (Mouse)
Function: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1 (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Not attached to membranes. {ECO:0000250}.
Interaction partners:
Sequence:
MSPHLFLPVVVLVVSPTPGAFQDSAVSPTQGEFEDLDCGRPEPSSRIVGGSDAHPGTWPWQVSLHHGGGHICGGSLIAPSWVLSAAHCFVTNGTLEPADEWSVLLGVHSQDGPLEGAHMRSVATILVPDNYSRVELGADLALLRLASPAKLGPSVKPVCLPRASHLFAHGTACWATGWGDVQESDPLPVPWVLQEVELKLLGETACQCLYSRPGPFNLTLQLLPGMLCAGYPEGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAHYESWIREHVMGSEPGPAFPSQLQKPPSEPWEPREENCTFAQPECGKATRPGTWPWEAQVMVPGSTPCYGALVSDSWVLAPASCFLDSLHDFETWRVLLPSRPEEKRVVRLVAHENASRNFASDLALLQLRTRVNLTAAPSAVCLPHREHYFLPGSRCRLARWGHGEPAPRSSAQLEAQLLNSWWCHCLYGRQGESVPPPGDPPHLLCPAYQEEEEAGACWVDSGWSLLCREEGTWFLAGYRTLSNGCLRPRAFSPMQTHGLWISHVTQGAYLEDQLTWDWGPEGEETEKQTCPPHTEHGACGLRPQSTPAGVLWPWLTEVHVTGDRVCTGILVAPGWVLAATHCILRLGSSTVPYIDVYLGLAGVSSLPQGHQVSRSVVSIRLPRHSGLRPPLALLELNSRVEPSPSALPICLHPEGVPPGASCWVLGWKDPQNRVPVAAAVSILTPRLCHCLYQGALTPGTFCVFYTEEQEDRCEMTSAPPLLCQTEGGPWVLVGMAVRGSRELFAAIGPEATWISQTVGEAHFLHLGGSSYWSPEGSDPCPQDLAGSASSPKVAALPLLLALLIPR
Protein: Inositol-trisphosphate 3-kinase A (EC 2.7.1.127) (Inositol 1,4,5-trisphosphate 3-kinase A) (IP3 3-kinase A) (IP3K A) (InsP 3-kinase A) (P17105)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate and participates to the regulation of calcium homeostasis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P23677}.
Interaction partners:
- Calmodulin-1
- Inositol polyphosphate multikinase
- Inositol polyphosphate-5-phosphatase A
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Multiple inositol polyphosphate phosphatase 1
- Inositol polyphosphate 5-phosphatase K
- Inositol-trisphosphate 3-kinase B
- Inositol-trisphosphate 3-kinase C
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Sequence:
MTLPGHPTGMARPRGAGPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAKRRGGQVPNGLPRAAPAPVIPQLTVTSEEDVAPASPGPPDREGNWLPAAGSHLQQPRRLSTSSLSSTGSSSLLEDSEDDLLSDSESRSRGNVQLETSEDVGQKSHWQKIRTMVNLPVMSPFKKRYSWVQLAGHTGSFKAAGTSGLILKRSSEPEHYCLVRLMADVLRGCVPAFHGVVERDGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAPTEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVTRVFEEFMQGDAEVLKRYLNRLQQIRDTLEISDFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKTTPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILANLAER
Protein: 3-ketodihydrosphingosine reductase ksrA (EC 1.1.1.102) (Q4WSZ0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38342}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine palmitoyl CoA transferase subunit LcbA
- Serine palmitoyltransferase 1, putative
- Serine palmitoyltransferase 2, putative
- Ceramide synthase membrane component
- Longevity-assurance protein
- sphingolipid 4-desaturase
- Sphingosine kinase
- Sphinganine hydroxylase Sur2, putative
- Neutral ceramidase
- PAP2 domain protein
Sequence:
MSQIHSFIPSNASPATLGISLILCGFIVYSVSKMFGYRTNHFPVEGRTIVVTGGSDGMGKAVACQLAEKGANVVIVARTVQKLREALEAIKGTAQDVKKQRFHYISADLTDAAECERVIAEVTEWNHGLAPDVVWCCAGYCEPGFFVETPVNTLRSQMDTVYWTAANTAHATLKSWLAPIPPSQQVPLPQRHLIFTCSTLAFVSIAGYAPYSPAKAAIRSLADTLSQEIEVYNGARAASSRNAAPPADVKIHTIFPMGILSPGFDNEQGLKPQLTKELEAADKPQRPIEVAKASIQGLEKGDYLITTMFVGHMMKASALGASPRNSIITDTLTSWLSSLVFLQVIPDLRKKAFNWGLKNGVPSSQSK
Protein: Nuclear RNA export factor 2 (Q9XVS8)
Organism: Caenorhabditis elegans
Function: Involved in the export of cellular mRNA to the cytoplasm. Plays a role in the nuclear retention of unspliced mRNAs.
Subcellular location: Nucleus {ECO:0000269|PubMed:11529502}. Note=Not localized at the nuclear rim.
Interaction partners:
- NTF2-related export protein
- Nsp1_C domain-containing protein
- mRNA export factor rae-1
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- RRM domain-containing protein
- UPF3 domain-containing protein
- Chromatin target of PRMT1 protein C-terminal domain-containing protein
- Nuclear cap-binding protein subunit 2
- THO complex subunit 5
Sequence:
MRGQNRRGYRNIEGRLSLSSHSSHSSPRQTHVTNLRPAEIKVVQDVVDGCYVATDDVLNLSNFSKNTEFVERDMLMCLTKTRVMSVVLQHIGYKYPRISGISFSNNRLCHLDHLSSLSSISKFLKFLDLSHNQISSGEELKKLGTIPVETVFFEGNPVCEKFVQCAEYANFIQKTFPKCSNLDGMEVEPKPDHNRIEQIIPFRNGYYGSDEVRTLVEEFIITYYKIYDGADGQQTRKQLLDAYDTNNSTFTHTVVCLWDPIKFVMYPDSESYRMYLRTSHNVLNQEYFAANRASRISHGAMDIVVALSRLPATIHLMDTFVVDVFLVSATLLGFTLHGTFRDGPSAIKPENTEEHDNYFTRTFMVAPRGEGKVAIVSDQLFISSMSKRRGDQYRMLVETATDIDQ
Protein: Ribonuclease TUDOR 1 (AtTudor1) (TUDOR-SN protein 1) (EC 3.1.-.-) (Q8VZG7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytoprotective ribonuclease (RNase) required for resistance to abiotic stresses, acting as a positive regulator of mRNA decapping during stress. Essential for the integrity and function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes called stress granules (SGs) and processing bodies (PBs), sites of post-transcriptional gene regulation during stress (e.g. salt and heat). Involved in gibberellic acid (GA) biosynthesis. Essential for stress tolerance, probably by regulating mRNAs entering the secretory pathway. Component of stress granules (SGs) that regulates growth under salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3 mRNA. May inhibit the degradation of mRNAs involved in stress adaptation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasmic granule {ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:20484005}. Endoplasmic reticulum {ECO:0000269|PubMed:20484005}. Note=Accumulates heterogeneously in the cytosol, in patches around the nucleus and in the cell periphery, and relocates transiently to a diffuse pattern in response to salt stress (PubMed:20484005). Accumulates in cytoplasmic stress granules (SGs) and processing bodies (PBs) in response to abiotic stresses (e.g. salt and heat) (PubMed:25205572, PubMed:25736060). {ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25205572, ECO:0000269|PubMed:25736060}.
Interaction partners:
- AT5g11760/T22P22_150
- F3E22.8 protein
- Polyadenylate-binding protein 8
- Polyadenylate-binding protein RBP47B'
- Polyadenylate-binding protein RBP47B
- Oligouridylate-binding protein 1A
- Probable RNA helicase SDE3
- SAWADEE protein
Sequence:
MATGAENQWLKGRVKAVTSGDCLVITALSHNRAGPPPEKTITFSSLMAPKMARRGGIDEPFAWESKEFLRKLCIGKEVAFKVDYKVEAIAGREFGSVFLGNENLAKLVVKTGWAKVREPGQQNQDKVSPYIKELLQLEELAKQEGYGRWSKVPGAAEASIRNLPPSAIGDSAGFDAMGLLAANKGKPMEGIVEQVRDGSTIRVYLLPEFQFVQVFVAGVQAPSMGRRTTNGSVVETVPDEPNGDVSAESRGPLTTAQRLAASAASSVEVSSDPFATEAKYFTEHRVLSRDVRIVLEGVDKFNNLIGSVHYSDGETVKDLGLELVENGLAKFVEWSANMMEEEAKKKLKAAELQCKKDKVKMWANYVPPATNSKAIHDQNFTGKVVEVVSGDCLIVADDAVPFGSPAAERRVCLSSIRSPKMGNPRREEKPAPYAREAREFLRQRLIGKQVIVQMEYSRKVTQGDGPTTSGAADRFMDFGSVFLPSAAKADSDEVTAPPAAAIAGSQPVGVNIAELVLVRGFGNVVRHRDFEERSNHYDALLAAEARALAGKKGIHSAKESPAMHITDLTVSAAKKAKDFLPSLQRIRRIPAVVEYVLSGHRFKLYIPKITCSIAFSFSGVRCPGRGEPYSEEAISVMRRRIMQRDVEIEVETVDRTGTFLGSMWESRTNVATVLLEAGLAKMQTSFGADRIAEAHLLEQAERSAKNQKLKIWENYVEGEEVSNGNTNTVETRQKETLKVVVTEVLGGGRFYVQSAGDQKIASIQNQLASLSIKDAPIIGSFNPKRGDIVLAQFSLDNSWNRAMIVTAPRAAVQSPDEKFEVFYIDYGNQETVPYSAIRPIDPSVSAAPGLAQLCRLAYIKVPSLEDDFGPEAGEYLHTVTLGSGKEFKAVIEERDTSGGKVKGQGTGTEFVVTLIAVDDEISVNAAMLQEGIARMEKRQKWGHKGKQAALDALEKFQEEARKSRIGIWQYGDIESDDEDTGPARKPAGGRR
Protein: Somatotropin (Growth hormone) (Q53WZ5)
Organism: Oreochromis niloticus (Nile tilapia) (Tilapia nilotica)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MNSVVLLLSVVCLGVSSQQITDSQRLFSIAVNRVTHLHLLAQRLFSDFESSLQTEEQRQLNKIFLQDFCNSDYIISPIDKHETQRSSVLKLLSISYGLVESWEFPSRSLSGGSSLRNQISPRLSELKTGILLLIRANQDEAENYPDTDTLQHAPYGNYYQSLGGNESLRQTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL
Protein: Signal transducer and activator of transcription A (Dd-STATa) (STAT5 homolog A) (O00910)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development.
Subcellular location: Cytoplasm. Nucleus. Note=Cytoplasmic in growing cells. Translocated into the nucleus in response to cAMP-induced tyrosine phosphorylation. Nuclear at the tight mound stage and in the upper, prestalk region of tipped aggregates and in cells at the tip of the slug. Subject to crm1-dependent nuclear export.
Interaction partners:
- MIZ-type zinc finger-containing protein
- Expansin-like protein 7
- Prestalk protein
- Cellulose-binding domain-containing protein
Sequence:
MSSAEFSMDDFEDTFDSNATISTKDLFEGSDRLPLNQSINTTIQNLYLPNGGFAIGDQSQQQYYQAMPPLNQSDQFNLGRSNNLTPRTNQLQQLQQQQQQQQQPQQQQQQQTYGTQSPIHMSQTPSSPLSSPLPSPTPFSRQQSYNNNNSNNTSSSQNYNNNNININNNNNNNNTNNNNNNNNGNNSNGNNGNNNNNNNNNNNNNTNNNNNNNQQQQQQQQQQQQQQQQQQQQQQQGNPNLSSPQPILDTIYKLLSEQEQTLVQMIHEQSLLLNRLPPTLDENSLAPLKSLSQKQITLSGQMNTEMSALDATKKGMILEPTDLAKLFALKQDLQIQFKQLSLLHNEIQSILNPQHSAPKPNVALVLKSQPFPVVISKGKQLGENQLVVLVLTGARSNFHINGPVKATMICDSHPTNKNNPTTPLEMDSQPIYPATLTAHFPLKFLAGTRKCSVNLKFGVNIRDLDNVTTTVESDASNPFVVITNECQWEGSAGVLLKKDAFDGQLEITWAQFINTLQRHFLIATKQDPVRPKRPLSSYDLKYIQTHFFGNRSIIHQQDFDKFWVWFGKSMQTLRYQRHISTLWQEGIIYGYMGRQEVNDALQNQDPGTFIIRFSERNPGQFGIAYIGVEMPARIKHYLVQPNDTAAAKKTFPDFLSEHSQFVNLLQWTKDTNGAPRFLKLHKDTALGSFAPKRTAPVPVGGYEPLNS
Protein: Dilute domain-containing protein (Q8MYQ0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLEFDEVGTSTPQPSLKSRMASAASSDYYCMTFDEPEEMDDVTLSSSATSKRPSDCSLDEAVRGAHKQTQLLAQQNMDLNDKLTRQSEELAEARAQLRGYSGPLGLENASDEEIIRLEAFEKGSIKHSGFLEVYNVPEFARIIVCELKPTLARLLTKNLPAYLLVAAFRNHDEKRDETALTGLFSSVHLVLKDTISRSHDLDLLSLWLVNLWRLFNLLRQYSGEDSQPEWHVANTETQNSYRFKAYDVAPIRDQLKLRIEECYTSLMKKAIEHVLSPKIVPGILQHESSSDLMTAGQERRDRNSGSVESQRKSLDDLLQFMEIVHTKLTTYGGDDIVVKQVIGQMARWMCALALNYMMFRRELCNFEKAIQIKHNVTQIQNWLNAKGLSDCRDHFEPLVQACHLLQSRKDPSNLDTLCGEMTSRLKPRQVVAILQHYDPSDEMEDGLSPEFLVQIQKKLNERAIANNDPIEDKDKLIMLGTYLPPFDTQPFSYSDFPLETLSLPSCLHMQSVCRLV
Protein: Uncharacterized protein YJR141W (P47172)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Protein MPE1
- Endoribonuclease YSH1
Sequence:
MVQYVVEWLPRIQSISVVVEGWKQVEIKNLKDTLMSISGDEEQVEDILLPVEVEEKVDASYKFKNRGKDLEWMTKLRSKSSKIYDSSIMSLPDGRWTKEELRSDSDFSIECLNCKQKIISKDNCQVLNDMPSEFWFELMDYWHCHKPDVKEDKSSYTRFETLKPSKNEILIGSSYFQGTPATFENVATTKENDNVLCIKCSAVLGQVTAGSLYKLHKWKLQLIRSGNTYKFPPECDITISLINVVKANSCRYVLVKCKTESLLVWIFSVDIGVTLTGNKSFKRAMKLLYTNSVTTINRCLNRQVVEELDFQETSFNAFYSALQHTNALLPSSMKKIGEWTISYTSLI
Protein: Zinc finger and SCAN domain-containing protein 21 (CtFIN51) (Transcription factor RU49) (Zinc finger protein 38) (Zfp-38) (Q07231)
Organism: Mus musculus (Mouse)
Function: Strong transcriptional activator. Plays an important role in spermatogenesis; essential for the progression of meiotic prophase I in spermatocytes.
Subcellular location: Nucleus {ECO:0000269|PubMed:1397691}.
Interaction partners:
Sequence:
MTKVVGMATVLGPRPPQESMGPSPIKVEEDEEKDKCCPTLELSHKHFRQSGNQDTLEPMGPSTIKAEEDESKDKCRPNLEISRKSFKQFGYQDTLEQLGPSTIKAEEDDEKDKGHPSPEISRQRFRQFGYHDTPGPREALSQLRVLCCEWLQPEIHTKEQILELLVLEQFLTILPRELQTWVQQHCPESAEEAVTLLEDLEQELDEPGLQVSSPPNEQKQSWEKMSTSGTAMESLSSTETQHVDASPKYEFWGPLYIQETGEEEVFTQDPRKRQGFKSNPQKEDSADEHRSSEEESHADGLKRTVIPMIPANKYGSRSERQWANNLERERGTKASLQDTGSRKGAEPASTRPAPGEKRYICAECGKAFSNSSNLTKHRRTHTGEKPYVCTKCGKAFSHSSNLTLHYRTHLVDRPYDCKCGKAFGQSSDLLKHQRMHTEEAPYQCKDCGKAFSGKGSLIRHYRIHTGEKPYQCNECGKSFSQHAGLSSHQRLHTGEKPYKCKECGKAFNHSSNFNKHHRIHTGEKPYWCSHCGKTFCSKSNLSKHQRVHTGEGEVQ
Protein: Amino acid transporter (Q56VY0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSIEDLPTVGDVAATRHQMGLWSCMSYVIANIIGAGIFITPGTVLKLALTNGMALVVWLGCGLISLIGGICYIELGTSIRDPGCDFAYNVYVGWEGIAFSFMWVGVIMSFPASAAVQAQTFGQYIVAGLSPIWHLGSPYDVILERGLGFALIIILTVLNLYAIDKYASKFQIFVTIAKLLSLAIIIVTGFWYLIVKGETEHFKDAFTPLPNEKYDIGQISLAFYGALWSFAGWDILNYGTPEIKNPRRTMPIALLGGISAVTLVYMAMNVSYMTVLDTETLKNSSAVAADFARITLGDFSYAIPFMISILLIGTLNSNIFCGSRFTHAAAREGHLPTFLSCINAESNSPRAALLFQLICTIAVTFVDTESLITYVTFVMFGQRVFTMAALLWIRYRNIPVHPDAIRVPLIFSILFFMITIALVVTPFIEDFTTTIVGVGLVLMGFLLYMIFMKPKQLPGFLYRFNDGITRVTCKILFTTPDLKHASEIETLKSDDESVVSNDERTTLSTSQIDTAAAGTAEPMTRL
Protein: Homocysteine S-methyltransferase 2 (EC 2.1.1.10) (S-methylmethionine:homocysteine methyltransferase 2) (AtHMT-2) (SMM:Hcy S-methyltransferase 2) (Q9M1W4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes methyl transfer from S-methylmethionine (SMM) to adenosyl-L-homocysteine (AdoMet). SMM degradation (by HMT-1, HMT-2 and HMT-3) and biosynthesis (by MMT1) constitute the SMM cycle in plants, which is probably required to achieve short term control of AdoMet level.
Interaction partners:
- Cystathionine beta-lyase, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Methionine gamma-lyase
- Adenosylhomocysteinase 2
- Adenosylhomocysteinase 1
- S-adenosylmethionine synthase 4
Sequence:
MTGNSFNSMKDFLKQTGGYAVIDGGLATEFERHGADLNDPLWSAKCLVTSPHLIHTVHLDYLEAGADIISSASYQATIQGFEAKGFSREESESLLKKSVEIATEARNSYYDKCGTSSSMDDKILKKRPILVAASVGSYGAYLADGSEYSGIYGDSITLEKLKDFHRRRLQVLAESGADLIAFETIPNKIEAQAFADLLEEGDVKIPGWFSFNSKDGVNVVSGDSIKECISIAENCEKVVAVGINCTPPRFIEGLVLEIEKVTSKPILVYPNSGESYDADRKEWVENTGVGDEDFVSYVEKWMDAGVSLLGGCCRTTPTTIRAIHKRLVNRRSL
Protein: Misfire, isoform I (B7Z0E6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MFPFLKYRFHPFKGKTPVVKNTTTPVWNYEINFAWMYPSVAQRFLILIFAHEHLQWKCVAEFELCLEEIAFNGTPSLGPTYLHLYDPVNPMIYVGRLLMELRSEMLTDSQPTHTLSSKTVPGLDETRFWHDDVYLIEFLPLMGHHILTSGTAYKISARLAEHTSNVLEGQLRTPLDRFKSAMNSKNFRREAPFQSCMFRVRLPDNRAKYESDFFMLDIVNYMRSELDTFKLFQRKYPLQDDEQAKCLKVIVNNILTRIKEGLDAHRFDHDVQPQRTTWDINRQLYLLDYFAKLPLELQNLKQKLRSCFLEHLDTSIGDVVNELQRLVAEIGSLSSMARTQDEWPELVLSLSASGKDVGVCRLNAKLFLNLRNQDADQDQETLCWRLKSFSFKSAGCSHTCPNCGCTTAIVSGCLSIVVERERKRFLAVVNKEWANIEPMLWQLNPEQTHFLCHVYIHQAKVRPGGEKKNICDSHLRVLFADQACETYTSPGTLSPIWNAVITFNWVSLPGGIGLYLKNPPLLSLEFYNSERSLPEDLVGMGSVAMSVISEDRASDSNWEDAGVFGCSKNPLRKLQRLKYLTPPPLKWVPIARKGTLQAEVLMSAEIIQISMESLTTGQNDKKEPQLATGIPMAIRPTMQNFVLEVFFVGLRNYSKSSMSSAGKRKINLMMGDLVLSSGPSTARIRNSINFLVAYASGVVSLPDQQDYWPAIIATDVLLSGFSSESILGAALIPNSSNFLQRDRTLKCVFKKEQEAAEASTTVSVDEDDEDEEEELEWEEEETKPSRISSWWMRLLFAFGLRPAPYANRHALRFHDDLDDHELVEEREFTWWTKFYNSMYWSAAEMCHEHKHRLVIYYEELEKQAQFGYLQDWAVPVQLVHGVKFKKHGPPKEDIYATLKLQLKLTPCQCPVLEDPGGGGDMVRNMSNPIHPRHQSTLQSLGETVKLLVRVYVVQGVQMRPRDVKGDSDCYVKLFLGGKTFSDRAHFSPNHSNPVFGRLFEMEATLPGDHMLQVMVYDHDKIKDEVIGQTNIDLEDRWRTRHRATVGLANEYTKSGYNHWHDVKLPSEILIDLCQKRGIQAPYYYGNVIEVDGMLFGDETLISKDEELQERLSLAVLKNMDKLPSFGYKLVPEHVETRSLCRDDFPNVEQGKLQLWIELFEANIYVPSPIDITPVPPADFEVRVVVKNLVGIQAGDKNIFGKLMSDVYVIGWCEDEDKRQSTDIHYRSFAGDAAFNWRMVFGLKYSPNEDLMVIRRKAGLLEEIEFKKPPIIYLQVWDKDVLTKDEYLAALELNLSNMYAPYPAAQLCKPYPKKRKRINLFKRKVINGWFPLQSNAHPSQRSQAAVQNGKMQLSIEVCTDVEAVNRPAGRGQDPPMALEPPYRPDSSFNPLTHPCKSFQHILWPVIRKYVLWTLLILIVILGLVLFFSNLPAKLMTIPLE
Protein: Fibronectin type 3 and ankyrin repeat domains protein 1 (Fibronectin type III and ankyrin repeat domains 1) (F6NQ86)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Juxtaposed with another zinc finger protein 1
Sequence:
MDPAEKRHRSEALAVGQVSHHSIELVWSREKGSKWTDPPQNWTCFILEQMNNTKHSFKQIHKGYNTRFTVDNLEPKTTYTFRLKVTWPSGQQQYYPSVTASTEKPPLNGKNLHSAVLKTDEVELCRVLQSGTVTVDVPDRLDYTPLMMAAIKGFTSGVQILVHHGADVSRKNSSGKDSLMLACFHGHLDVVKLLCGCGASWRARDRTGCCSLHWATAGGQLDILQYLIQYGCEVNVQDNIAWTPLMIVSVITGDPAVASLLISAGADVNVQDRDGKTPLMVAVLNNYEHLVQILLKKGADPNIQNKCGVSALEMAKAFDRQNIISLLEDEESERPK
Protein: Speckle-type POZ protein-like (HIB homolog 2) (Roadkill homolog 2) (Q6IQ16)
Organism: Homo sapiens (Human)
Function: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, but with relatively low efficiency. Cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes containing homodimeric SPOPL or the heterodimer formed by SPOP and SPOPL are less efficient than ubiquitin ligase complexes containing only SPOP. May function to down-regulate the activity of cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes that contain SPOP.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-3
- Speckle-type POZ protein
- Zinc finger protein GLI1
- Transcriptional activator GLI3
- Zinc finger protein GLI2
- E3 ubiquitin-protein ligase RBX1
- Suppressor of fused homolog
- Kelch repeat and BTB domain-containing protein 7
- Kelch-like protein 20
- Kelch repeat and BTB domain-containing protein 8
Sequence:
MSREPTPPLPGDMSTGPIAESWCYTQVKVVKFSYMWTINNFSFCREEMGEVLKSSTFSSGPSDKMKWCLRVNPKGLDDESKDYLSLYLLLVSCPKSEVRAKFKFSLLNAKREETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGHTNTNTLKVPECRLAEDLGNLWENTRFTDCSFFVRGQEFKAHKSVLAARSPVFNAMFEHEMEESKKNRVEINDLDPEVFKEMMRFIYTGRAPNLDKMADNLLAAADKYALERLKVMCEEALCSNLSVENVADTLVLADLHSAEQLKAQAIDFINRCSVLRQLGCKDGKNWNSNQATDIMETSGWKSMIQSHPHLVAEAFRALASAQCPQFGIPRKRLKQS
Protein: Ubiquitin carboxyl-terminal hydrolase 37 (EC 3.4.19.12) (Deubiquitinating enzyme 37) (Ubiquitin thioesterase 37) (Ubiquitin-specific-processing protease 37) (Q86T82)
Organism: Homo sapiens (Human)
Function: Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'-linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). Plays an important role in the regulation of DNA replication by stabilizing the licensing factor CDT1.
Subcellular location: Nucleus {ECO:0000269|PubMed:26299517}. Chromosome {ECO:0000269|PubMed:26299517}.
Interaction partners:
- F-box/WD repeat-containing protein 1A
- 26S proteasome regulatory subunit 8
- RuvB-like 1
- Cyclin-A2
- F-box/WD repeat-containing protein 11
- Fizzy-related protein homolog
- Polyubiquitin-C
- Zinc finger protein SNAI1
Sequence:
MSPLKIHGPIRIRSMQTGITKWKEGSFEIVEKENKVSLVVHYNTGGIPRIFQLSHNIKNVVLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLPAAMKPSQGSGSFGAILGSRTSQKETSRQLSYSDNQASAKRGSLETKDDIPFRKVLGNPGRGSIKTVAGSGIARTIPSLTSTSTPLRSGLLENRTEKRKRMISTGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAGSKEHSSGGTNLDRTNVSSQTPSAKRSLGFLPQPVPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVSGEENSPDISATRAYTCPVITNLEFEVQHSIICKACGEIIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRVLILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFTLGWSAHMAISRPLKASQMVNSCITSPSTPSKKFTFKSKSSLALCLDSDSEDELKRSVALSQRLCEMLGNEQQQEDLEKDSKLCPIEPDKSELENSGFDRMSEEELLAAVLEISKRDASPSLSHEDDDKPTSSPDTGFAEDDIQEMPENPDTMETEKPKTITELDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFVDALGSDEDSGNEDVFDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEAAVQSDRDRSGYIFFYMHKEIFDELLETEKNSQSLSTEVGKTTRQAL