Q14980

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession NUMA1_HUMAN; Q14980;
Entrez ID 4926
GenBank Protein ID NM_001286561.1; NM_006185.3; XM_006718564.1;
GenBank Nucleotide ID NP_001273490.1; NP_006176.2; XP_006718627.1;
Protein Name Nuclear mitotic apparatus protein 1 (Nuclear matrix protein-22) (NMP-22) (Nuclear mitotic apparatus protein) (NuMA protein) (SP-H antigen)
Gene Name NUMA1; NMP22; NUMA
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionMicrotubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:7769006, PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:12445386, PubMed:11956313). Plays a role in the establishment of the mitotic spindle orientation during metaph(view all)
Sequence
(Fasta)
MTLHATRGAA LLSWVNSLHV ADPVEAVLQL QDCSIFIKII DRIHGTEEGQ QILKQPVSER 60
LDFVCSFLQK NRKHPSSPEC LVSAQKVLEG SELELAKMTM LLLYHSTMSS KSPRDWEQFE 120
YKIQAELAVI LKFVLDHEDG LNLNEDLENF LQKAPVPSTC SSTFPEELSP PSHQAKREIR 180
FLELQKVASS SSGNNFLSGS PASPMGDILQ TPQFQMRRLK KQLADERSNR DELELELAEN 240
RKLLTEKDAQ IAMMQQRIDR LALLNEKQAA SPLEPKELEE LRDKNESLTM RLHETLKQCQ 300
DLKTEKSQMD RKINQLSEEN GDLSFKLREF ASHLQQLQDA LNELTEEHSK ATQEWLEKQA 360
QLEKELSAAL QDKKCLEEKN EILQGKLSQL EEHLSQLQDN PPQEKGEVLG DVLQLETLKQ 420
EAATLAANNT QLQARVEMLE TERGQQEAKL LAERGHFEEE KQQLSSLITD LQSSISNLSQ 480
AKEELEQASQ AHGARLTAQV ASLTSELTTL NATIQQQDQE LAGLKQQAKE KQAQLAQTLQ 540
QQEQASQGLR HQVEQLSSSL KQKEQQLKEV AEKQEATRQD HAQQLATAAE EREASLRERD 600
AALKQLEALE KEKAAKLEIL QQQLQVANEA RDSAQTSVTQ AQREKAELSR KVEELQACVE 660
TARQEQHEAQ AQVAELELQL RSEQQKATEK ERVAQEKDQL QEQLQALKES LKVTKGSLEE 720
EKRRAADALE EQQRCISELK AETRSLVEQH KRERKELEEE RAGRKGLEAR LQQLGEAHQA 780
ETEVLRRELA EAMAAQHTAE SECEQLVKEV AAWRERYEDS QQEEAQYGAM FQEQLMTLKE 840
ECEKARQELQ EAKEKVAGIE SHSELQISRQ QNELAELHAN LARALQQVQE KEVRAQKLAD 900
DLSTLQEKMA ATSKEVARLE TLVRKAGEQQ ETASRELVKE PARAGDRQPE WLEEQQGRQF 960
CSTQAALQAM EREAEQMGNE LERLRAALME SQGQQQEERG QQEREVARLT QERGRAQADL 1020
ALEKAARAEL EMRLQNALNE QRVEFATLQE ALAHALTEKE GKDQELAKLR GLEAAQIKEL 1080
EELRQTVKQL KEQLAKKEKE HASGSGAQSE AAGRTEPTGP KLEALRAEVS KLEQQCQKQQ 1140
EQADSLERSL EAERASRAER DSALETLQGQ LEEKAQELGH SQSALASAQR ELAAFRTKVQ 1200
DHSKAEDEWK AQVARGRQEA ERKNSLISSL EEEVSILNRQ VLEKEGESKE LKRLVMAESE 1260
KSQKLEERLR LLQAETASNS ARAAERSSAL REEVQSLREE AEKQRVASEN LRQELTSQAE 1320
RAEELGQELK AWQEKFFQKE QALSTLQLEH TSTQALVSEL LPAKHLCQQL QAEQAAAEKR 1380
HREELEQSKQ AAGGLRAELL RAQRELGELI PLRQKVAEQE RTAQQLRAEK ASYAEQLSML 1440
KKAHGLLAEE NRGLGERANL GRQFLEVELD QAREKYVQEL AAVRADAETR LAEVQREAQS 1500
TARELEVMTA KYEGAKVKVL EERQRFQEER QKLTAQVEQL EVFQREQTKQ VEELSKKLAD 1560
SDQASKVQQQ KLKAVQAQGG ESQQEAQRLQ AQLNELQAQL SQKEQAAEHY KLQMEKAKTH 1620
YDAKKQQNQE LQEQLRSLEQ LQKENKELRA EAERLGHELQ QAGLKTKEAE QTCRHLTAQV 1680
RSLEAQVAHA DQQLRDLGKF QVATDALKSR EPQAKPQLDL SIDSLDLSCE EGTPLSITSK 1740
LPRTQPDGTS VPGEPASPIS QRLPPKVESL ESLYFTPIPA RSQAPLESSL DSLGDVFLDS 1800
GRKTRSARRR TTQIINITMT KKLDVEEPDS ANSSFYSTRS APASQASLRA TSSTQSLARL 1860
GSPDYGNSAL LSLPGYRPTT RSSARRSQAG VSSGAPPGRN SFYMGTCQDE PEQLDDWNRI 1920
AELQQRNRVC PPHLKTCYPL ESRPSLSLGT ITDEEMKTGD PQETLRRASM QPIQIAEGTG 1980
ITTRQQRKRV SLEPHQGPGT PESKKATSCF PRPMTPRDRH EGRKQSTTEA QKKAAPASTK 2040
QADRRQSMAF SILNTPKKLG NSLLRRGASK KALSKASPNT RSGTRRSPRI ATTTASAATA 2100
AAIGATPRAK GKAKH 2116

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1PhosphorylationProstate cancer/carcinoma/adenocarcinomaP23097092
[Reference]: Phosphorylation of NuMA by Aurora-A kinase in PC-3 prostate cancer cells affects proliferation, survival, and interphase NuMA localization

※ Disease Cross-ref Annotation

DatabaseAnnotation
Cancer Gene Census
APL
CTD (Curated)
(count: 2)
MESH:D017449 ; Dermatitis, Allergic Contact
MESH:D015473 ; Leukemia, Promyelocytic, Acute
GWASdb
(count: 5)
rs5743684; Triglycerides; coronary artery disease|lipid metabolism disorder|arteriosclerosis
rs2298456; Multiple complex diseases; Null
rs10898815; Blood pressure (response to calcium channel blocker); hypertension
rs4945434; Multiple complex diseases; Null
rs679926; Multiple complex diseases; Null

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 133)
(view all)
107       MLLLYHSTMSSKSPR     dbPAF
1103      KKEKEHASGSGAQSE     dbPAF
1105      EKEHASGSGAQSEAA     dbPAF
1109      ASGSGAQSEAAGRTE     dbPAF
112       HSTMSSKSPRDWEQF     dbPAF
1145      KQQEQADSLERSLEA     dbPAF
Acetylation
(count: 49)
(view all)
1024      QADLALEKAARAELE     PLMD
1088      EELRQTVKQLKEQLA     PLMD
1099      EQLAKKEKEHASGSG     PLMD
111       YHSTMSSKSPRDWEQ     PLMD
1121      RTEPTGPKLEALRAE     PLMD
1131      ALRAEVSKLEQQCQK     PLMD
Ubiquitination
(count: 54)
(view all)
1024      QADLALEKAARAELE     PLMD
1078      GLEAAQIKELEELRQ     PLMD
1121      RTEPTGPKLEALRAE     PLMD
1131      ALRAEVSKLEQQCQK     PLMD
1138      KLEQQCQKQQEQADS     PLMD
1174      LQGQLEEKAQELGHS     PLMD
Sumoylation
(count: 5)
1766      ISQRLPPKVESLESL     PLMD
1822      INITMTKKLDVEEPD     PLMD
2033      STTEAQKKAAPASTK     PLMD
2058      SILNTPKKLGNSLLR     PLMD
276       AASPLEPKELEELRD     PLMD
Glycation
(count: 2)
1059      LAHALTEKEGKDQEL     PLMD
1062      ALTEKEGKDQELAKL     PLMD
Malonylation
(count: 1)
891       ALQQVQEKEVRAQKL     PLMD
Methylation
(count: 1)
1803      VFLDSGRKTRSARRR     PLMD
Succinylation
(count: 1)
708       QEQLQALKESLKVTK     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource