NIPS1_HUMAN - dbPTM
NIPS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NIPS1_HUMAN
UniProt AC Q9BPW8
Protein Name Protein NipSnap homolog 1
Gene Name NIPSNAP1
Organism Homo sapiens (Human).
Sequence Length 284
Subcellular Localization
Protein Description
Protein Sequence MAPRLCSISVTARRLLGGPGPRAGDVASAAAARFYSKDNEGSWFRSLFVHKVDPRKDAHSTLLSKKETSNLYKIQFHNVKPEYLDAYNSLTEAVLPKLHLDEDYPCSLVGNWNTWYGEQDQAVHLWRFSGGYPALMDCMNKLKNNKEYLEFRRERSQMLLSRRNQLLLEFSFWNEPQPRMGPNIYELRTYKLKPGTMIEWGNNWARAIKYRQENQEAVGGFFSQIGELYVVHHLWAYKDLQSREETRNAAWRKRGWDENVYYTVPLVRHMESRIMIPLKISPLQ
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
37UbiquitinationAAARFYSKDNEGSWF
HHHHHHCCCCCCCCE
53.87-
51AcetylationFRSLFVHKVDPRKDA
EEEEEEEECCCCCCH
42.9319608861
51UbiquitinationFRSLFVHKVDPRKDA
EEEEEEEECCCCCCH
42.9321890473
56UbiquitinationVHKVDPRKDAHSTLL
EEECCCCCCHHHHHC
65.73-
60PhosphorylationDPRKDAHSTLLSKKE
CCCCCHHHHHCCCHH
23.59-
64PhosphorylationDAHSTLLSKKETSNL
CHHHHHCCCHHCCCC
44.8124719451
65AcetylationAHSTLLSKKETSNLY
HHHHHCCCHHCCCCE
55.38-
65UbiquitinationAHSTLLSKKETSNLY
HHHHHCCCHHCCCCE
55.3821890473
66AcetylationHSTLLSKKETSNLYK
HHHHCCCHHCCCCEE
63.95-
66UbiquitinationHSTLLSKKETSNLYK
HHHHCCCHHCCCCEE
63.9521890473
73AcetylationKETSNLYKIQFHNVK
HHCCCCEEEEEECCC
32.95-
80UbiquitinationKIQFHNVKPEYLDAY
EEEEECCCHHHHHHH
37.13-
80AcetylationKIQFHNVKPEYLDAY
EEEEECCCHHHHHHH
37.13-
83PhosphorylationFHNVKPEYLDAYNSL
EECCCHHHHHHHHHH
20.57-
87PhosphorylationKPEYLDAYNSLTEAV
CHHHHHHHHHHHHHH
12.64-
89PhosphorylationEYLDAYNSLTEAVLP
HHHHHHHHHHHHHHH
24.8020166139
91PhosphorylationLDAYNSLTEAVLPKL
HHHHHHHHHHHHHHC
23.0128348404
107PhosphorylationLDEDYPCSLVGNWNT
CCCCCCCCEECCCCC
22.91-
129PhosphorylationAVHLWRFSGGYPALM
HEEEEEECCCHHHHH
23.8028857561
141AcetylationALMDCMNKLKNNKEY
HHHHHHHHHHCCHHH
33.6725953088
143MalonylationMDCMNKLKNNKEYLE
HHHHHHHHCCHHHHH
61.1526320211
143AcetylationMDCMNKLKNNKEYLE
HHHHHHHHCCHHHHH
61.1525953088
146SuccinylationMNKLKNNKEYLEFRR
HHHHHCCHHHHHHHH
58.0723954790
146SuccinylationMNKLKNNKEYLEFRR
HHHHHCCHHHHHHHH
58.07-
146AcetylationMNKLKNNKEYLEFRR
HHHHHCCHHHHHHHH
58.0719608861
146MalonylationMNKLKNNKEYLEFRR
HHHHHCCHHHHHHHH
58.0726320211
148PhosphorylationKLKNNKEYLEFRRER
HHHCCHHHHHHHHHH
17.0925839225
156PhosphorylationLEFRRERSQMLLSRR
HHHHHHHHHHHHHHH
18.3929978859
161PhosphorylationERSQMLLSRRNQLLL
HHHHHHHHHHHCHHH
25.8229978859
180SulfoxidationWNEPQPRMGPNIYEL
CCCCCCCCCCCEEEE
15.4821406390
185PhosphorylationPRMGPNIYELRTYKL
CCCCCCEEEEEEEEC
18.6220068231
188MethylationGPNIYELRTYKLKPG
CCCEEEEEEEECCCC
24.86115485041
191AcetylationIYELRTYKLKPGTMI
EEEEEEEECCCCCEE
49.8025953088
193SuccinylationELRTYKLKPGTMIEW
EEEEEECCCCCEEEE
36.93-
193SuccinylationELRTYKLKPGTMIEW
EEEEEECCCCCEEEE
36.9321890473
193AcetylationELRTYKLKPGTMIEW
EEEEEECCCCCEEEE
36.93-
193UbiquitinationELRTYKLKPGTMIEW
EEEEEECCCCCEEEE
36.9321890473
253UbiquitinationTRNAAWRKRGWDENV
HHHHHHHHCCCCCCC
44.5621890473
254MethylationRNAAWRKRGWDENVY
HHHHHHHCCCCCCCE
42.75115485049
261PhosphorylationRGWDENVYYTVPLVR
CCCCCCCEEEHHHEE
12.6628152594
262PhosphorylationGWDENVYYTVPLVRH
CCCCCCEEEHHHEEE
9.2928152594
263PhosphorylationWDENVYYTVPLVRHM
CCCCCEEEHHHEEEC
9.6528152594
279SuccinylationSRIMIPLKISPLQ--
CEEEEEEEECCCC--
35.4623954790
279AcetylationSRIMIPLKISPLQ--
CEEEEEEEECCCC--
35.4625953088
279UbiquitinationSRIMIPLKISPLQ--
CEEEEEEEECCCC--
35.46-

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 NIPS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NIPS1_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 NIPS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACBP_HUMANDBIphysical
21900206
TCPZ_HUMANCCT6Aphysical
26496610
FAT1_HUMANFAT1physical
26496610
CH60_HUMANHSPD1physical
26496610
PLEC_HUMANPLECphysical
26496610
AAPK2_HUMANPRKAA2physical
26496610
TCF20_HUMANTCF20physical
26496610
TCPA_HUMANTCP1physical
26496610
TCPG_HUMANCCT3physical
26496610
BCL7B_HUMANBCL7Bphysical
26496610
TF3C5_HUMANGTF3C5physical
26496610
KNTC1_HUMANKNTC1physical
26496610
TCPH_HUMANCCT7physical
26496610
TCPD_HUMANCCT4physical
26496610
TCPB_HUMANCCT2physical
26496610
NS1BP_HUMANIVNS1ABPphysical
26496610
TCPQ_HUMANCCT8physical
26496610
HPSE_HUMANHPSEphysical
26496610
POP1_HUMANPOP1physical
26496610
FND3A_HUMANFNDC3Aphysical
26496610
TCPE_HUMANCCT5physical
26496610
GANAB_HUMANGANABphysical
26496610
ARHGC_HUMANARHGEF12physical
26496610
ZN281_HUMANZNF281physical
26496610
LCOR_HUMANC10orf12physical
26496610
HP1B3_HUMANHP1BP3physical
26496610
HAUS6_HUMANHAUS6physical
26496610
RT18A_HUMANMRPS18Aphysical
26496610
ASCC2_HUMANASCC2physical
26496610
TNC18_HUMANTNRC18physical
26496610
DJC21_HUMANDNAJC21physical
26496610
NSE2_HUMANNSMCE2physical
26496610
IF140_HUMANIFT140physical
27173435
WDR19_HUMANWDR19physical
27173435

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 NIPS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-146, AND MASSSPECTROMETRY.

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