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Protein

Nuclear envelope pore membrane protein POM 121C

Gene

POM121C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential component of the nuclear pore complex (NPC). The repeat-containing domain may be involved in anchoring components of the pore complex to the pore membrane. When overexpressed in cells induces the formation of cytoplasmic annulate lamellae (AL).1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear envelope pore membrane protein POM 121C
Alternative name(s):
Nuclear pore membrane protein 121-2
Short name:
POM121-2
Pore membrane protein of 121 kDa C
Gene namesi
Name:POM121C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:34005. POM121C.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei41 – 6121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12291229Nuclear envelope pore membrane protein POM 121CPRO_0000204906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei322 – 3221PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineBy similarity
Modified residuei348 – 3481PhosphoserineCombined sources
Modified residuei370 – 3701PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiA8CG34.
MaxQBiA8CG34.
PaxDbiA8CG34.
PRIDEiA8CG34.

PTM databases

iPTMnetiA8CG34.
PhosphoSiteiA8CG34.
SwissPalmiA8CG34.

Expressioni

Gene expression databases

BgeeiA8CG34.
CleanExiHS_POM121C.

Organism-specific databases

HPAiCAB003710.
HPA043809.
HPA049817.

Interactioni

Protein-protein interaction databases

IntActiA8CG34. 13 interactions.
STRINGi9606.ENSP00000414208.

Structurei

3D structure databases

ProteinModelPortaliA8CG34.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 398398Required for targeting to the nucleus and nuclear pore complexAdd
BLAST
Regioni1 – 4040Cisternal sideSequence analysisAdd
BLAST
Regioni62 – 12291168Pore sideSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 19161Pro-richAdd
BLAST
Compositional biasi322 – 444123Ser-richAdd
BLAST
Compositional biasi728 – 924197Thr-richAdd
BLAST

Domaini

Contains F-X-F-G repeats.

Sequence similaritiesi

Belongs to the POM121 family.Curated

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IM0V. Eukaryota.
ENOG4112BJY. LUCA.
HOGENOMiHOG000015364.
HOVERGENiHBG053628.
InParanoidiA8CG34.
OrthoDBiEOG7QG440.
PhylomeDBiA8CG34.
TreeFamiTF323517.

Family and domain databases

InterProiIPR026090. POM121.
[Graphical view]
PANTHERiPTHR23193:SF5. PTHR23193:SF5. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: A8CG34-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSPAAAAAGA GERRRPIASV RDGRGRGCGG PAGAALLGLS LVGLLLYLVP
60 70 80 90 100
AAAALAWLAV GTTAAWWGLS REPRGSRPLS SFVQKARHRR TLFASPPAKS
110 120 130 140 150
TANGNLLEPR TLLEGPDPAE LLLMGSYLGK PGPPQPAPAP EGQDLRNRPG
160 170 180 190 200
RRPPARPAPR STPPSPPTHR VHHFYPSLPT PLLRPSGRPS PRDRGTLPDR
210 220 230 240 250
FVITPRRRYP IHQTQYSCPG VLPTVCWNGY HKKAVLSPRN SRMVCSPVTV
260 270 280 290 300
RIAPPDRRFS RSAIPEQIIS STLSSPSSNA PDPCAKETVL SALKEKKKKR
310 320 330 340 350
TVEEEDQIFL DGQENKRRRH DSSGSGHSAF EPLVASGVPA SFVPKPGSLK
360 370 380 390 400
RGLNSQSSDD HLNKRSRSSS MSSLTGAYTS GIPSSSRNAI TSSYSSTRGI
410 420 430 440 450
SQLWKRNGPS SSPFSSPASS RSQTPERPAK KIREEELCHH SSSSTPLAAD
460 470 480 490 500
KESQGEKAAD TTPRKKQNSN SQSTPGSSGQ RKRKVQLLPS RRGEQLTLPP
510 520 530 540 550
PPQLGYSITA EDLDLEKKAS LQWFNQALED KSDAASNSVT ETPPTTQPSF
560 570 580 590 600
TFTLPAAATA SPPTSLLAPS TNPLLESLKK MQTPPSLPPC PESAGAATTE
610 620 630 640 650
ALSPPKTPSL LPPLGLSQSG PPGLLPSPSF DSKPPTTLLG LIPAPSMVPA
660 670 680 690 700
TDTKAPPTLQ AETATKPQAT SAPSPAPKQS FLFGTQNTSP SSPAAPAASS
710 720 730 740 750
ASPMFKPIFT APPKSEKEGP TPPGPSVTAT APSSSSLPTT TSTTAPTFQP
760 770 780 790 800
VFSSMGPPAS VPLPAPFFKQ TTTPATAPTT TAPLFTGLAS ATSAVAPITS
810 820 830 840 850
ASPSTDSASK PAFGFGINSV SSSSVSTTTS TATAASQPFL FGAPQASAAS
860 870 880 890 900
FTPAMGSIFQ FGKPPALPTT TTVTTFSQSL PTAVPTATSS SAADFSGFGS
910 920 930 940 950
TLATSAPATS SQPTLTFSNT STPTFNIPFG SSAKSPLPSY PGANPQPAFG
960 970 980 990 1000
AAEGQPPGAA KPALTPSFGS SFTFGNSAAP APATAPTPAP ASTIKIVPAH
1010 1020 1030 1040 1050
VPTPIQPTFG GATHSAFGLK ATASAFGAPA SSQPAFGGST AVFSFGAATS
1060 1070 1080 1090 1100
SGFGATTQTA SSGSSSSVFG STTPSPFTFG GSAAPAGSGS FGINVATPGS
1110 1120 1130 1140 1150
SATTGAFSFG AGQSGSTATS TPFTGGLGQN ALGTTGQSTP FAFNVGSTTE
1160 1170 1180 1190 1200
SKPVFGGTAT PTFGQNTPAP GVGTSGSSLS FGASSAPAQG FVGVGPFGSA
1210 1220
APSFSIGAGS KTPGARQRLQ ARRQHTRKK
Length:1,229
Mass (Da):125,059
Last modified:September 2, 2008 - v2
Checksum:i55E3A0205612434B
GO
Isoform 2 (identifier: A8CG34-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-242: Missing.

Note: No experimental confirmation available.
Show »
Length:987
Mass (Da):99,134
Checksum:iA8A2B549FC6C5735
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti720 – 7201P → L in BC082993 (PubMed:15489334).Curated
Sequence conflicti728 – 7281T → S in BC082993 (PubMed:15489334).Curated
Sequence conflicti965 – 9651T → A in BC082993 (PubMed:15489334).Curated
Sequence conflicti979 – 9802Missing in BC082993 (PubMed:15489334).Curated
Sequence conflicti984 – 9841T → A in BC082993 (PubMed:15489334).Curated
Sequence conflicti991 – 9911A → P in BC082993 (PubMed:15489334).Curated
Sequence conflicti1025 – 10251A → T in BC082993 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791T → A.
Corresponds to variant rs427206 [ dbSNP | Ensembl ].
VAR_045906
Natural varianti1165 – 11651Q → L.
Corresponds to variant rs365436 [ dbSNP | Ensembl ].
VAR_045907

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 242242Missing in isoform 2. 1 PublicationVSP_040759Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006014 Genomic DNA. No translation available.
BC082993 mRNA. No translation available.
AB354586 mRNA. Translation: BAF80888.1.
CCDSiCCDS47617.1. [A8CG34-2]
PIRiT12551.
UniGeneiHs.712563.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC006014 Genomic DNA. No translation available.
BC082993 mRNA. No translation available.
AB354586 mRNA. Translation: BAF80888.1.
CCDSiCCDS47617.1. [A8CG34-2]
PIRiT12551.
UniGeneiHs.712563.

3D structure databases

ProteinModelPortaliA8CG34.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiA8CG34. 13 interactions.
STRINGi9606.ENSP00000414208.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiA8CG34.
PhosphoSiteiA8CG34.
SwissPalmiA8CG34.

Proteomic databases

EPDiA8CG34.
MaxQBiA8CG34.
PaxDbiA8CG34.
PRIDEiA8CG34.

Protocols and materials databases

DNASUi100101267.
Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiPOM121C.
HGNCiHGNC:34005. POM121C.
HPAiCAB003710.
HPA043809.
HPA049817.
MIMi615754. gene.
neXtProtiNX_A8CG34.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IM0V. Eukaryota.
ENOG4112BJY. LUCA.
HOGENOMiHOG000015364.
HOVERGENiHBG053628.
InParanoidiA8CG34.
OrthoDBiEOG7QG440.
PhylomeDBiA8CG34.
TreeFamiTF323517.

Enzyme and pathway databases

ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-159236. Transport of Mature mRNA derived from an Intron-Containing Transcript.
R-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168276. NS1 Mediated Effects on Host Pathways.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-180910. Vpr-mediated nuclear import of PICs.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3301854. Nuclear Pore Complex (NPC) Disassembly.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.

Miscellaneous databases

PROiA8CG34.
SOURCEiSearch...

Gene expression databases

BgeeiA8CG34.
CleanExiHS_POM121C.

Family and domain databases

InterProiIPR026090. POM121.
[Graphical view]
PANTHERiPTHR23193:SF5. PTHR23193:SF5. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Leiomyosarcoma.
  3. "Two distinct human POM121 genes: requirement for the formation of nuclear pore complexes."
    Funakoshi T., Maeshima K., Yahata K., Sugano S., Imamoto F., Imamoto N.
    FEBS Lett. 581:4910-4916(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-398, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Cervix.
  4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322 AND SER-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiP121C_HUMAN
AccessioniPrimary (citable) accession number: A8CG34
Secondary accession number(s): O75115, Q9Y2N3, Q9Y4S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: June 8, 2016
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.