NRAM2_HUMAN - dbPTM
NRAM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NRAM2_HUMAN
UniProt AC P49281
Protein Name Natural resistance-associated macrophage protein 2
Gene Name SLC11A2
Organism Homo sapiens (Human).
Sequence Length 568
Subcellular Localization Isoform 2: Cell membrane
Multi-pass membrane protein . Early endosome .
Endosome membrane
Multi-pass membrane protein . Mitochondrion outer membrane
Multi-pass membrane protein. Cell membrane
Multi-pass membrane protein . Also found in extra
Protein Description Important in metal transport, in particular iron. Can also transport manganese, cobalt, cadmium, nickel, vanadium and lead. Involved in apical iron uptake into duodenal enterocytes. Involved in iron transport from acidified endosomes into the cytoplasm of erythroid precursor cells. May play an important role in hepatic iron accumulation and tissue iron distribution. May serve to import iron into the mitochondria..
Protein Sequence MVLGPEQKMSDDSVSGDHGESASLGNINPAYSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILWLMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMYLHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQVVEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTCHLGLTAQPELYLLNTMDADSLVSR
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
10PhosphorylationLGPEQKMSDDSVSGD
CCCCCCCCCCCCCCC
45.3526074081
13PhosphorylationEQKMSDDSVSGDHGE
CCCCCCCCCCCCCCC
24.1526074081
15PhosphorylationKMSDDSVSGDHGESA
CCCCCCCCCCCCCCC
42.3226074081
18 (in isoform 4)Phosphorylation-45.5024719451
18 (in isoform 3)Phosphorylation-45.5024719451
21PhosphorylationVSGDHGESASLGNIN
CCCCCCCCCCCCCCC
27.9626074081
23PhosphorylationGDHGESASLGNINPA
CCCCCCCCCCCCCCC
46.2026074081
23 (in isoform 4)Phosphorylation-46.2028348404
23 (in isoform 3)Phosphorylation-46.2028348404
25 (in isoform 4)Phosphorylation-30.4028348404
25 (in isoform 3)Phosphorylation-30.4028348404
28 (in isoform 4)Phosphorylation-21.1028348404
28 (in isoform 3)Phosphorylation-21.1028348404
29 (in isoform 4)Phosphorylation-28.8628348404
29 (in isoform 3)Phosphorylation-28.8628348404
31PhosphorylationLGNINPAYSNPSLSQ
CCCCCCCCCCCCHHC
15.3927251275
32PhosphorylationGNINPAYSNPSLSQS
CCCCCCCCCCCHHCC
44.3529802988
35PhosphorylationNPAYSNPSLSQSPGD
CCCCCCCCHHCCCCC
44.9228348404
37PhosphorylationAYSNPSLSQSPGDSE
CCCCCCHHCCCCCCH
32.7127251275
39PhosphorylationSNPSLSQSPGDSEEY
CCCCHHCCCCCCHHH
27.7228348404
43PhosphorylationLSQSPGDSEEYFATY
HHCCCCCCHHHHHHH
37.9428348404
46PhosphorylationSPGDSEEYFATYFNE
CCCCCHHHHHHHHCC
8.4128348404
56PhosphorylationTYFNEKISIPEEEYS
HHHCCCCCCCHHHHC
43.0629507054
64S-palmitoylationIPEEEYSCFSFRKLW
CCHHHHCCCHHHHHH
3.0329575903
66PhosphorylationEEEYSCFSFRKLWAF
HHHHCCCHHHHHHHH
28.5924719451
81PhosphorylationTGPGFLMSIAYLDPG
HCCCEEEEEEECCCC
13.2523663014
84PhosphorylationGFLMSIAYLDPGNIE
CEEEEEEECCCCCCC
15.2323663014
129PhosphorylationAARLGVVTGLHLAEV
HHHHCCHHHHHHHHH
31.45-
176PhosphorylationAIAINLLSVGRIPLW
HHHHHHHCCCCCCCC
26.20-
250PhosphorylationPSCSGCRTPQIEQAV
CCCCCCCCHHHHHHH
24.50-
273PhosphorylationPHNMYLHSALVKSRQ
CCHHHHHHHHHHHHC
22.24-
336N-linked_GlycosylationQVVEVCTNTSSPHAG
CEEEHHCCCCCCCCC
32.60UniProtKB CARBOHYD
349N-linked_GlycosylationAGLFPKDNSTLAVDI
CCCCCCCCCEEEEEE
42.91UniProtKB CARBOHYD
536PhosphorylationCLIALGMSFLDCGHT
HHHHHHCHHHCCCCC
22.36-
555 (in isoform 5)Phosphorylation-13.89-
559 (in isoform 2)Phosphorylation-19.19-
564PhosphorylationLNTMDADSLVSR---
EECCCHHHHHCC---
32.1825137130
567PhosphorylationMDADSLVSR------
CCHHHHHCC------
37.2525137130
588 (in isoform 3)Phosphorylation--

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
-KUbiquitinationE3 ubiquitin ligaseWWP2O00308
PMID:18776082
-KUbiquitinationE3 ubiquitin ligaseNEDD4LQ96PU5
PMID:19706893

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NRAM2_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 NRAM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFIP1_HUMANNDFIP1physical
18776082
NFIP2_HUMANNDFIP2physical
18776082
PRKN_HUMANPARK2physical
20089134
NFIP1_HUMANNDFIP1physical
19706893
NEDD4_HUMANNEDD4physical
19706893

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NRAM2_HUMAN

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Related Literatures of Post-Translational Modification

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