NUFP1_HUMAN - dbPTM
NUFP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NUFP1_HUMAN
UniProt AC Q9UHK0
Protein Name Nuclear fragile X mental retardation-interacting protein 1
Gene Name NUFIP1
Organism Homo sapiens (Human).
Sequence Length 495
Subcellular Localization Nucleus . Distributed in the nucleus in a dot-like pattern.
Protein Description Binds RNA..
Protein Sequence MAEPTSDFETPIGWHASPELTPTLGPLSDTAPPRDSWMFWAMLPPPPPPLTSSLPAAGSKPSSESQPPMEAQSLPGAPPPFDAQILPGAQPPFDAQSPLDSQPQPSGQPWNFHASTSWYWRQSSDRFPRHQKSFNPAVKNSYYPRKYDAKFTDFSLPPSRKQKKKKRKEPVFHFFCDTCDRGFKNQEKYDKHMSEHTKCPELDCSFTAHEKIVQFHWRNMHAPGMKKIKLDTPEEIARWREERRKNYPTLANIERKKKLKLEKEKRGAVLTTTQYGKMKGMSRHSQMAKIRSPGKNHKWKNDNSRQRAVTGSGSHLCDLKLEGPPEANADPLGVLINSDSESDKEEKPQHSVIPKEVTPALCSLMSSYGSLSGSESEPEETPIKTEADVLAENQVLDSSAPKSPSQDVKATVRNFSEAKSENRKKSFEKTNPKRKKDYHNYQTLFEPRTHHPYLLEMLLAPDIRHERNVILQCVRYIIKKDFFGLDTNSAKSKDV
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MAEPTSDFETPI
---CCCCCCCCCCCC
32.2224043423
6Phosphorylation--MAEPTSDFETPIG
--CCCCCCCCCCCCC
51.5224043423
10PhosphorylationEPTSDFETPIGWHAS
CCCCCCCCCCCCCCC
21.8726074081
17PhosphorylationTPIGWHASPELTPTL
CCCCCCCCCCCCCCC
13.1526074081
21PhosphorylationWHASPELTPTLGPLS
CCCCCCCCCCCCCCC
16.7426074081
23PhosphorylationASPELTPTLGPLSDT
CCCCCCCCCCCCCCC
38.8326074081
28PhosphorylationTPTLGPLSDTAPPRD
CCCCCCCCCCCCCCC
35.7324043423
30PhosphorylationTLGPLSDTAPPRDSW
CCCCCCCCCCCCCCC
37.3724043423
126MethylationYWRQSSDRFPRHQKS
EEECCCCCCCCCHHH
45.47115485749
133PhosphorylationRFPRHQKSFNPAVKN
CCCCCHHHCCHHHHC
24.5618187866
189PhosphorylationGFKNQEKYDKHMSEH
CCCCHHHHHHHHHHH
29.4830301811
194PhosphorylationEKYDKHMSEHTKCPE
HHHHHHHHHHCCCCC
26.4130301811
205PhosphorylationKCPELDCSFTAHEKI
CCCCCCCCCCCCHHH
25.8725159151
229SumoylationAPGMKKIKLDTPEEI
CCCCCCCCCCCHHHH
49.54-
229SumoylationAPGMKKIKLDTPEEI
CCCCCCCCCCCHHHH
49.54-
232PhosphorylationMKKIKLDTPEEIARW
CCCCCCCCHHHHHHH
42.9328674419
247PhosphorylationREERRKNYPTLANIE
HHHHHHHCCCHHHHH
10.7125159151
257AcetylationLANIERKKKLKLEKE
HHHHHHHHHHCCHHH
70.3469479
260AcetylationIERKKKLKLEKEKRG
HHHHHHHCCHHHHHC
64.5888931
265AcetylationKLKLEKEKRGAVLTT
HHCCHHHHHCCEEEE
68.1769483
265UbiquitinationKLKLEKEKRGAVLTT
HHCCHHHHHCCEEEE
68.1724816145
271PhosphorylationEKRGAVLTTTQYGKM
HHHCCEEEEHHHHCC
22.6220068231
277AcetylationLTTTQYGKMKGMSRH
EEEHHHHCCCCCCCC
32.2925953088
282PhosphorylationYGKMKGMSRHSQMAK
HHCCCCCCCCCHHHC
35.1922210691
292PhosphorylationSQMAKIRSPGKNHKW
CHHHCCCCCCCCCCC
41.2920068231
310PhosphorylationNSRQRAVTGSGSHLC
CCCCEECCCCCCCCC
25.3328555341
312PhosphorylationRQRAVTGSGSHLCDL
CCEECCCCCCCCCCE
27.9725159151
314PhosphorylationRAVTGSGSHLCDLKL
EECCCCCCCCCCEEE
18.2523312004
338PhosphorylationPLGVLINSDSESDKE
CCCEEECCCCCCCCC
35.2026055452
340PhosphorylationGVLINSDSESDKEEK
CEEECCCCCCCCCCC
38.5326055452
342PhosphorylationLINSDSESDKEEKPQ
EECCCCCCCCCCCCC
58.9126055452
351PhosphorylationKEEKPQHSVIPKEVT
CCCCCCCCCCCHHHH
19.2522115753
358PhosphorylationSVIPKEVTPALCSLM
CCCCHHHHHHHHHHH
12.1630177828
363PhosphorylationEVTPALCSLMSSYGS
HHHHHHHHHHHHCCC
28.1428102081
366PhosphorylationPALCSLMSSYGSLSG
HHHHHHHHHCCCCCC
26.2128102081
367PhosphorylationALCSLMSSYGSLSGS
HHHHHHHHCCCCCCC
21.3928102081
368PhosphorylationLCSLMSSYGSLSGSE
HHHHHHHCCCCCCCC
11.9228102081
370PhosphorylationSLMSSYGSLSGSESE
HHHHHCCCCCCCCCC
15.8928102081
372PhosphorylationMSSYGSLSGSESEPE
HHHCCCCCCCCCCCC
41.8028102081
374PhosphorylationSYGSLSGSESEPEET
HCCCCCCCCCCCCCC
34.2828102081
376PhosphorylationGSLSGSESEPEETPI
CCCCCCCCCCCCCCC
61.2128102081
381PhosphorylationSESEPEETPIKTEAD
CCCCCCCCCCCCHHH
28.7528102081
385PhosphorylationPEETPIKTEADVLAE
CCCCCCCCHHHHHHH
36.8129396449
398PhosphorylationAENQVLDSSAPKSPS
HHCCCCCCCCCCCCC
25.0028450419
399PhosphorylationENQVLDSSAPKSPSQ
HCCCCCCCCCCCCCH
48.5422115753
403PhosphorylationLDSSAPKSPSQDVKA
CCCCCCCCCCHHHHH
28.8230266825
405PhosphorylationSSAPKSPSQDVKATV
CCCCCCCCHHHHHHH
46.2130266825
411PhosphorylationPSQDVKATVRNFSEA
CCHHHHHHHHHHHHH
17.8026074081
416PhosphorylationKATVRNFSEAKSENR
HHHHHHHHHHHHHHH
39.9526074081
419UbiquitinationVRNFSEAKSENRKKS
HHHHHHHHHHHHHHH
55.0124816145
420PhosphorylationRNFSEAKSENRKKSF
HHHHHHHHHHHHHHH
47.3426074081
476PhosphorylationVILQCVRYIIKKDFF
HHHHHHHHHHHHHHC
6.1318669648
487PhosphorylationKDFFGLDTNSAKSKD
HHHCCCCCCCCCCCC
35.7918669648
489PhosphorylationFFGLDTNSAKSKDV-
HCCCCCCCCCCCCC-
38.8818669648

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NUFP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NUFP1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NUFP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCNT1_HUMANCCNT1physical
15107825
CDK9_HUMANCDK9physical
15107825
FMR1_HUMANFMR1physical
12837692
FMR1_HUMANFMR1physical
10556305
BRCA1_HUMANBRCA1physical
15107825
KLF6_HUMANKLF6physical
17636026
RUVB1_HUMANRUVBL1physical
17636026
RUVB2_HUMANRUVBL2physical
17636026
NCAM1_HUMANNCAM1physical
26186194
DPYL1_HUMANCRMP1physical
26186194
DPYL3_HUMANDPYSL3physical
26186194
DPYL2_HUMANDPYSL2physical
26186194
DPYL5_HUMANDPYSL5physical
26186194
STXB1_HUMANSTXBP1physical
26186194
ATP4A_HUMANATP4Aphysical
26186194
RAB14_HUMANRAB14physical
26186194
AT2B2_HUMANATP2B2physical
26186194
GPM6B_HUMANGPM6Bphysical
26186194
H15_HUMANHIST1H1Bphysical
26186194
DNM1L_HUMANDNM1Lphysical
26186194
H2B1L_HUMANHIST1H2BLphysical
26186194
VPP1_HUMANATP6V0A1physical
26186194
CNTN1_HUMANCNTN1physical
26186194
DCX_HUMANDCXphysical
26186194
DCLK1_HUMANDCLK1physical
26186194
SCAM5_HUMANSCAMP5physical
26186194
SYN1_HUMANSYN1physical
26186194
TRIM2_HUMANTRIM2physical
26186194
FA49B_HUMANFAM49Bphysical
26186194
AP180_HUMANSNAP91physical
26186194
SYT1_HUMANSYT1physical
26186194
ZNHI3_HUMANZNHIT3physical
26186194
MTAP2_HUMANMAP2physical
26186194
HPCL4_HUMANHPCAL4physical
26186194
VISL1_HUMANVSNL1physical
26186194
AMPH_HUMANAMPHphysical
26186194
BIN1_HUMANBIN1physical
26186194
DYN3_HUMANDNM3physical
26186194
DYN1_HUMANDNM1physical
26186194
CAD13_HUMANCDH13physical
26186194
E41L1_HUMANEPB41L1physical
26186194
STX1A_HUMANSTX1Aphysical
26186194
STX1B_HUMANSTX1Bphysical
26186194
GNAZ_HUMANGNAZphysical
26186194
GNA11_HUMANGNA11physical
26186194
GNAQ_HUMANGNAQphysical
26186194
GPDM_HUMANGPD2physical
26186194
GNAO_HUMANGNAO1physical
26186194
GBG2_HUMANGNG2physical
26186194
GPM6A_HUMANGPM6Aphysical
26186194
PDE2A_HUMANPDE2Aphysical
26186194
ANK2_HUMANANK2physical
26186194
SYUB_HUMANSNCBphysical
26186194
SYUA_HUMANSNCAphysical
26186194
GRIA2_HUMANGRIA2physical
26186194
RAB6B_HUMANRAB6Bphysical
26186194
RAB3B_HUMANRAB3Bphysical
26186194
RAB3A_HUMANRAB3Aphysical
26186194
KCC2B_HUMANCAMK2Bphysical
26186194
KCC2A_HUMANCAMK2Aphysical
26186194
EF1A2_HUMANEEF1A2physical
26186194
HPCA_HUMANHPCAphysical
26186194
NCALD_HUMANNCALDphysical
26186194
RAB5B_HUMANRAB5Bphysical
26186194
MP3B2_HUMANMAP1LC3B2physical
26186194
NDRG4_HUMANNDRG4physical
26186194
S12A5_HUMANSLC12A5physical
26186194
NTRI_HUMANNTMphysical
26186194
CADM2_HUMANCADM2physical
26186194
SNAB_HUMANNAPBphysical
26186194
TAU_HUMANMAPTphysical
26186194
DPYL4_HUMANDPYSL4physical
26186194
MP2K1_HUMANMAP2K1physical
26186194
CAMKV_HUMANCAMKVphysical
26186194
HBD_HUMANHBDphysical
26186194
NCS1_HUMANNCS1physical
26186194
PLXA2_HUMANPLXNA2physical
26186194
CALB2_HUMANCALB2physical
26186194
SRCN1_HUMANSRCIN1physical
26186194
VAMP2_HUMANVAMP2physical
26186194
H2AW_HUMANH2AFY2physical
26186194
CBPE_HUMANCPEphysical
26186194
SYPH_HUMANSYPphysical
26186194
EDIL3_HUMANEDIL3physical
26186194
ADDB_HUMANADD2physical
26186194
GLSK_HUMANGLSphysical
26186194
GSK3B_HUMANGSK3Bphysical
26186194
L1CAM_HUMANL1CAMphysical
26186194
SNP25_HUMANSNAP25physical
26186194
SFXN3_HUMANSFXN3physical
26186194
ZNHI3_HUMANZNHIT3physical
25170085
ZNHI3_HUMANZNHIT3physical
27594683
ZNHI3_HUMANZNHIT3physical
28514442
HPCA_HUMANHPCAphysical
28514442
GRIA2_HUMANGRIA2physical
28514442
SYN1_HUMANSYN1physical
28514442
H2B1L_HUMANHIST1H2BLphysical
28514442
VISL1_HUMANVSNL1physical
28514442
STX1B_HUMANSTX1Bphysical
28514442
DCLK1_HUMANDCLK1physical
28514442
SNP25_HUMANSNAP25physical
28514442
RUVB1_HUMANRUVBL1physical
28514442
DPYL1_HUMANCRMP1physical
28514442
KCC2A_HUMANCAMK2Aphysical
28514442
MTAP2_HUMANMAP2physical
28514442
STX1A_HUMANSTX1Aphysical
28514442
EDIL3_HUMANEDIL3physical
28514442
GPM6B_HUMANGPM6Bphysical
28514442
STXB1_HUMANSTXBP1physical
28514442
DPYL3_HUMANDPYSL3physical
28514442
ATP4A_HUMANATP4Aphysical
28514442
TAU_HUMANMAPTphysical
28514442
CALB2_HUMANCALB2physical
28514442
NDRG4_HUMANNDRG4physical
28514442
HPCL4_HUMANHPCAL4physical
28514442
DNM1L_HUMANDNM1Lphysical
28514442
PDE2A_HUMANPDE2Aphysical
28514442
SNAB_HUMANNAPBphysical
28514442
E41L1_HUMANEPB41L1physical
28514442
RAB5B_HUMANRAB5Bphysical
28514442
SYT1_HUMANSYT1physical
28514442
AP180_HUMANSNAP91physical
28514442
L1CAM_HUMANL1CAMphysical
28514442
S12A5_HUMANSLC12A5physical
28514442
SYPH_HUMANSYPphysical
28514442
SRCN1_HUMANSRCIN1physical
28514442
RAB3A_HUMANRAB3Aphysical
28514442
H2AW_HUMANH2AFY2physical
28514442
CNTN1_HUMANCNTN1physical
28514442
SYUB_HUMANSNCBphysical
28514442
GPM6A_HUMANGPM6Aphysical
28514442
DPYL2_HUMANDPYSL2physical
28514442
H15_HUMANHIST1H1Bphysical
28514442
DCX_HUMANDCXphysical
28514442
NTRI_HUMANNTMphysical
28514442
NCALD_HUMANNCALDphysical
28514442
NCAM1_HUMANNCAM1physical
28514442
ANK2_HUMANANK2physical
28514442
CAMKV_HUMANCAMKVphysical
28514442
RAB6B_HUMANRAB6Bphysical
28514442
DYN1_HUMANDNM1physical
28514442
MP2K1_HUMANMAP2K1physical
28514442
GNAO_HUMANGNAO1physical
28514442
GBG2_HUMANGNG2physical
28514442
MP3B2_HUMANMAP1LC3B2physical
28514442
TRIM2_HUMANTRIM2physical
28514442
AT2B2_HUMANATP2B2physical
28514442
MAP1A_HUMANMAP1Aphysical
28514442
KCC2B_HUMANCAMK2Bphysical
28514442
GNAQ_HUMANGNAQphysical
28514442
GNAZ_HUMANGNAZphysical
28514442
MARE3_HUMANMAPRE3physical
28514442
RAB3B_HUMANRAB3Bphysical
28514442
VATC1_HUMANATP6V1C1physical
28514442
DPYL5_HUMANDPYSL5physical
28514442
GLSK_HUMANGLSphysical
28514442
CBPE_HUMANCPEphysical
28514442
GPDM_HUMANGPD2physical
28514442
BIN1_HUMANBIN1physical
28514442
FA49B_HUMANFAM49Bphysical
28514442
PLXA2_HUMANPLXNA2physical
28514442
ADDB_HUMANADD2physical
28514442
CAD13_HUMANCDH13physical
28514442
SFXN3_HUMANSFXN3physical
28514442
GBG7_HUMANGNG7physical
28514442
CANB1_HUMANPPP3R1physical
28514442
KAP3_HUMANPRKAR2Bphysical
28514442
ZNHI3_HUMANZNHIT3physical
25404746
RUVB1_HUMANRUVBL1physical
25404746
RUVB2_HUMANRUVBL2physical
25404746
SMN_HUMANSMN1physical
26275778
GEMI6_HUMANGEMIN6physical
26275778
DDX20_HUMANDDX20physical
26275778

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NUFP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340; SER-342;TYR-476; THR-487 AND SER-489, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-340 ANDSER-342, AND MASS SPECTROMETRY.

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