PMF1_HUMAN - dbPTM
PMF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PMF1_HUMAN
UniProt AC Q6P1K2
Protein Name Polyamine-modulated factor 1
Gene Name PMF1 {ECO:0000312|EMBL:AAH65031.1}
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization Nucleus . Chromosome, centromere, kinetochore . Associated with the kinetochore.
Protein Description Part of the MIS12 complex which is required for normal chromosome alignment and segregation and kinetochore formation during mitosis. May act as a cotranscription partner of NFE2L2 involved in regulation of polyamine-induced transcription of SSAT..
Protein Sequence MAEASSANLGSGCEEKRHEGSSSESVPPGTTISRVKLLDTMVDTFLQKLVAAGSYQRFTDCYKCFYQLQPAMTQQIYDKFIAQLQTSIREEISDIKEEGNLEAVLNALDKIVEEGKVRKEPAWRPSGIPEKDLHSVMAPYFLQQRDTLRRHVQKQEAENQQLADAVLAGRRQVEELQLQVQAQQQAWQALHREQRELVAVLREPE
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
2Acetylation------MAEASSANL
------CCCCCCCCC		22.51-
5Phosphorylation---MAEASSANLGSG
---CCCCCCCCCCCC		22.8419691289
6Phosphorylation--MAEASSANLGSGC
--CCCCCCCCCCCCC		28.3719691289
11PhosphorylationASSANLGSGCEEKRH
CCCCCCCCCCCCCCC		43.3622199227
16UbiquitinationLGSGCEEKRHEGSSS
CCCCCCCCCCCCCCC		36.4433845483
21PhosphorylationEEKRHEGSSSESVPP
CCCCCCCCCCCCCCC		27.9219691289
22PhosphorylationEKRHEGSSSESVPPG
CCCCCCCCCCCCCCC		49.3219691289
23PhosphorylationKRHEGSSSESVPPGT
CCCCCCCCCCCCCCC		35.2719691289
25PhosphorylationHEGSSSESVPPGTTI
CCCCCCCCCCCCCCH		41.70-
36UbiquitinationGTTISRVKLLDTMVD
CCCHHHHHHHHHHHH		42.0721890473
36 (in isoform 3)Ubiquitination-42.0721890473
36 (in isoform 1)Ubiquitination-42.0721890473
36UbiquitinationGTTISRVKLLDTMVD
CCCHHHHHHHHHHHH		42.0721890473
36 (in isoform 5)Ubiquitination-42.0721890473
36UbiquitinationGTTISRVKLLDTMVD
CCCHHHHHHHHHHHH		42.0723000965
36 (in isoform 2)Ubiquitination-42.0721890473
40PhosphorylationSRVKLLDTMVDTFLQ
HHHHHHHHHHHHHHH		21.0425690035
44PhosphorylationLLDTMVDTFLQKLVA
HHHHHHHHHHHHHHH		18.1625690035
48 (in isoform 5)Ubiquitination-47.2621890473
48 (in isoform 1)Ubiquitination-47.2621890473
48 (in isoform 3)Ubiquitination-47.2621890473
48UbiquitinationMVDTFLQKLVAAGSY
HHHHHHHHHHHCCCC		47.2621906983
56 (in isoform 4)Ubiquitination-35.3921906983
63UbiquitinationQRFTDCYKCFYQLQP
HHHHHHHHHHHHCCH		24.9717623298
86PhosphorylationKFIAQLQTSIREEIS
HHHHHHHHHHHHHHH		34.4120068231
87PhosphorylationFIAQLQTSIREEISD
HHHHHHHHHHHHHHH		13.4920068231
96UbiquitinationREEISDIKEEGNLEA
HHHHHHHHHHCCHHH		55.4921906983
96 (in isoform 1)Ubiquitination-55.4921890473
96 (in isoform 3)Ubiquitination-55.4921890473
96 (in isoform 5)Ubiquitination-55.4921890473
98 (in isoform 2)Ubiquitination-48.6721890473
110UbiquitinationAVLNALDKIVEEGKV
HHHHHHHHHHHCCCC		49.8829967540
112UbiquitinationLNALDKIVEEGKVRK
HHHHHHHHHCCCCCC		7.2529967540
114 (in isoform 4)Ubiquitination-54.1121906983
116UbiquitinationDKIVEEGKVRKEPAW
HHHHHCCCCCCCCCC		41.9929967540
118UbiquitinationIVEEGKVRKEPAWRP
HHHCCCCCCCCCCCC		40.9029967540
119UbiquitinationVEEGKVRKEPAWRPS
HHCCCCCCCCCCCCC		71.6621963094
121UbiquitinationEGKVRKEPAWRPSGI
CCCCCCCCCCCCCCC		39.9121963094
126PhosphorylationKEPAWRPSGIPEKDL
CCCCCCCCCCCHHHH		40.5623909892
131UbiquitinationRPSGIPEKDLHSVMA
CCCCCCHHHHHHHHH		61.3029967540
133UbiquitinationSGIPEKDLHSVMAPY
CCCCHHHHHHHHHHH		4.8629967540
150 (in isoform 3)Phosphorylation-37.1222210691
154 (in isoform 1)Ubiquitination-49.3621890473
154AcetylationTLRRHVQKQEAENQQ
HHHHHHHHHHHHHHH		49.3625953088
154UbiquitinationTLRRHVQKQEAENQQ
HHHHHHHHHHHHHHH		49.3627667366
156 (in isoform 2)Ubiquitination-66.0521890473
156 (in isoform 3)Phosphorylation-66.0522210691
156UbiquitinationRRHVQKQEAENQQLA
HHHHHHHHHHHHHHH		66.0521963094
160 (in isoform 3)Phosphorylation-31.0422210691
195 (in isoform 5)Phosphorylation-34.1722210691
201 (in isoform 5)Phosphorylation-3.5622210691
205 (in isoform 5)Phosphorylation-69.3822210691
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 PMF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PMF1_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 PMF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NF2L2_HUMANNFE2L2physical
10419538
GDF9_HUMANGDF9physical
16169070
CE126_HUMANKIAA1377physical
16169070
MED31_HUMANMED31physical
16169070
DPYL1_HUMANCRMP1physical
16169070
PTN_HUMANPTNphysical
16169070
CSN6_HUMANCOPS6physical
16169070
GIT1_HUMANGIT1physical
16169070
CSN7A_HUMANCOPS7Aphysical
12020345
NF2L2_HUMANNFE2L2physical
12020345
TCP1L_HUMANTCP10Lphysical
21988832
CU077_HUMANTCP10Lphysical
21988832
KDM1A_HUMANKDM1Aphysical
23455924
MIS12_HUMANMIS12physical
25416956
USBP1_HUMANUSHBP1physical
25416956
SGTB_HUMANSGTBphysical
26186194
SEC63_HUMANSEC63physical
26186194
PGRC2_HUMANPGRMC2physical
26186194
ZRAN1_HUMANZRANB1physical
26186194
WIPI3_HUMANWDR45Bphysical
26186194
GNPAT_HUMANGNPATphysical
26186194
PP1G_HUMANPPP1CCphysical
26186194
FACE1_HUMANZMPSTE24physical
26186194
CKLF6_HUMANCMTM6physical
26186194
ALR_HUMANGFERphysical
26186194
DSN1_HUMANDSN1physical
28514442
NSL1_HUMANNSL1physical
28514442
SPC25_HUMANSPC25physical
28514442
KI21B_HUMANKIF21Bphysical
28514442
SPC24_HUMANSPC24physical
28514442
BICD2_HUMANBICD2physical
28514442
ZWINT_HUMANZWINTphysical
28514442
RUFY2_HUMANRUFY2physical
28514442
GCC2_HUMANGCC2physical
28514442
MIS12_HUMANMIS12physical
28514442
NDC80_HUMANNDC80physical
28514442
ZC4H2_HUMANZC4H2physical
28514442
CEP89_HUMANCEP89physical
28514442
KNL1_HUMANCASC5physical
28514442
FBX28_HUMANFBXO28physical
28514442
RUFY1_HUMANRUFY1physical
28514442
TSNAX_HUMANTSNAXphysical
28514442
NUF2_HUMANNUF2physical
28514442
A16L1_HUMANATG16L1physical
28514442
NRBF2_HUMANNRBF2physical
28514442
AF10_HUMANMLLT10physical
28514442
PP1G_HUMANPPP1CCphysical
28514442
RGPD8_HUMANRGPD8physical
28514442
STXB4_HUMANSTXBP4physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PMF1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-11,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-11,ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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