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Protein

Nuclear export mediator factor NEMF

Gene

NEMF

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

Functioni

Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. NEMF is responsible for selective recognition of stalled 60S subunits by recognizing an exposed, nascent chain-conjugated tRNA moiety. NEMF is important for the stable association of LTN1 to the complex (PubMed:25578875). May indirectly play a role in nuclear export (PubMed:16103875).2 Publications

GO - Biological processi

  • nuclear export Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear export mediator factor NEMF
Alternative name(s):
Antigen NY-CO-1
Serologically defined colon cancer antigen 1
Gene namesi
Name:NEMF
Synonyms:SDCCAG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:10663. NEMF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35593.

Polymorphism and mutation databases

BioMutaiNEMF.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10761076Nuclear export mediator factor NEMFPRO_0000097642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei417 – 4171PhosphoserineCombined sources
Modified residuei747 – 7471PhosphoserineCombined sources
Modified residuei748 – 7481PhosphoserineCombined sources
Modified residuei763 – 7631PhosphoserineCombined sources
Modified residuei831 – 8311PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO60524.
MaxQBiO60524.
PaxDbiO60524.
PRIDEiO60524.

PTM databases

iPTMnetiO60524.
PhosphoSiteiO60524.

Expressioni

Tissue specificityi

Expressed in brain, heart, liver, lung, spleen, and skeletal muscle. Also expressed at lower levels in stomach and testis.1 Publication

Gene expression databases

BgeeiO60524.
CleanExiHS_SDCCAG1.
ExpressionAtlasiO60524. baseline and differential.
GenevisibleiO60524. HS.

Organism-specific databases

HPAiHPA004160.

Interactioni

Subunit structurei

Component of the ribosome quality control complex (RQC), composed of at least the E3 ubiquitin ligase LTN1 and NEMF (PubMed:25578875). The complex probably also contains TCF25 as well as VCP/p97 and its ubiquitin-binding cofactors (By similarity). RQC forms a stable complex with 60S ribosomal subunits (PubMed:25578875). Interacts (via its N-terminus) with XPO1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

IntActiO60524. 10 interactions.
STRINGi9606.ENSP00000298310.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J92electron microscopy3.60u/v1-501[»]
ProteinModelPortaliO60524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili296 – 35964Sequence analysisAdd
BLAST
Coiled coili483 – 51432Sequence analysisAdd
BLAST
Coiled coili869 – 89426Sequence analysisAdd
BLAST

Domaini

The N-terminal domain contains a nuclear export signal. The C-terminal domain may interact with cargo proteins (By similarity).By similarity

Sequence similaritiesi

Belongs to the NEMF family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2030. Eukaryota.
COG1293. LUCA.
GeneTreeiENSGT00390000018516.
HOVERGENiHBG079170.
InParanoidiO60524.
OMAiMFLEFFA.
OrthoDBiEOG76T9QJ.
PhylomeDBiO60524.
TreeFamiTF300515.

Family and domain databases

InterProiIPR021846. DUF3441.
IPR008532. DUF814.
[Graphical view]
PfamiPF11923. DUF3441. 1 hit.
PF05670. DUF814. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60524-1) [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
MKSRFSTIDL RAVLAELNAS LLGMRVNNVY DVDNKTYLIR LQKPDFKATL
60 70 80 90 100
LLESGIRIHT TEFEWPKNMM PSSFAMKCRK HLKSRRLVSA KQLGVDRIVD
110 120 130 140 150
FQFGSDEAAY HLIIELYDRG NIVLTDYEYV ILNILRFRTD EADDVKFAVR
160 170 180 190 200
ERYPLDHARA AEPLLTLERL TEIVASAPKG ELLKRVLNPL LPYGPALIEH
210 220 230 240 250
CLLENGFSGN VKVDEKLETK DIEKVLVSLQ KAEDYMKTTS NFSGKGYIIQ
260 270 280 290 300
KREIKPSLEA DKPVEDILTY EEFHPFLFSQ HSQCPYIEFE SFDKAVDEFY
310 320 330 340 350
SKIEGQKIDL KALQQEKQAL KKLDNVRKDH ENRLEALQQA QEIDKLKGEL
360 370 380 390 400
IEMNLQIVDR AIQVVRSALA NQIDWTEIGL IVKEAQAQGD PVASAIKELK
410 420 430 440 450
LQTNHVTMLL RNPYLLSEEE DDDVDGDVNV EKNETEPPKG KKKKQKNKQL
460 470 480 490 500
QKPQKNKPLL VDVDLSLSAY ANAKKYYDHK RYAAKKTQKT VEAAEKAFKS
510 520 530 540 550
AEKKTKQTLK EVQTVTSIQK ARKVYWFEKF LWFISSENYL IIGGRDQQQN
560 570 580 590 600
EIIVKRYLTP GDIYVHADLH GATSCVIKNP TGEPIPPRTL TEAGTMALCY
610 620 630 640 650
SAAWDARVIT SAWWVYHHQV SKTAPTGEYL TTGSFMIRGK KNFLPPSYLM
660 670 680 690 700
MGFSFLFKVD ESCVWRHQGE RKVRVQDEDM ETLASCTSEL ISEEMEQLDG
710 720 730 740 750
GDTSSDEDKE EHETPVEVEL MTQVDQEDIT LQSGRDELNE ELIQEESSED
760 770 780 790 800
EGEYEEVRKD QDSVGEMKDE GEETLNYPDT TIDLSHLQPQ RSIQKLASKE
810 820 830 840 850
ESSNSSDSKS QSRRHLSAKE RREMKKKKLP SDSGDLEALE GKDKEKESTV
860 870 880 890 900
HIETHQNTSK NVAAVQPMKR GQKSKMKKMK EKYKDQDEED RELIMKLLGS
910 920 930 940 950
AGSNKEEKGK KGKKGKTKDE PVKKQPQKPR GGQRVSDNIK KETPFLEVIT
960 970 980 990 1000
HELQDFAVDD PHDDKEEQDL DQQGNEENLF DSLTGQPHPE DVLLFAIPIC
1010 1020 1030 1040 1050
APYTTMTNYK YKVKLTPGVQ KKGKAAKTAL NSFMHSKEAT AREKDLFRSV
1060 1070
KDTDLSRNIP GKVKVSAPNL LNVKRK
Length:1,076
Mass (Da):122,954
Last modified:November 24, 2009 - v4
Checksum:iFCC5F95A0DB22F79
GO
Isoform 2 (identifier: O60524-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MKSRFSTIDLRAVLAELNASL → MPKTCQCYVGTKTTNPSAWPS
     22-821: Missing.

Show »
Length:276
Mass (Da):31,151
Checksum:i49B37757681B0E51
GO
Isoform 3 (identifier: O60524-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     562-582: Missing.

Show »
Length:1,055
Mass (Da):120,761
Checksum:i6D69BA826390F146
GO
Isoform 4 (identifier: O60524-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     78-119: Missing.

Show »
Length:1,034
Mass (Da):118,025
Checksum:i8B42E666C724AB60
GO
Isoform 5 (identifier: O60524-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     221-245: Missing.

Note: No experimental confirmation available.
Show »
Length:1,051
Mass (Da):120,140
Checksum:iF0CA1E8446FC3739
GO

Sequence cautioni

The sequence AAC18036.1 differs from that shown. Reason: Frameshift at position 1065. Curated
The sequence AAH06001.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH20794.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH56687.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAI07765.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG52763.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAG58070.1 differs from that shown.Intron retention.Curated
The sequence BAG58070.1 differs from that shown. Reason: Frameshift at positions 246 and 1025. Curated
The sequence BAG58070.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531E → K in BAG56774 (PubMed:14702039).Curated
Sequence conflicti438 – 4381P → S in AAH56687 (PubMed:15489334).Curated
Sequence conflicti495 – 4951E → G in BAG56774 (PubMed:14702039).Curated
Sequence conflicti560 – 5601P → PV in BAG58070 (PubMed:14702039).Curated
Sequence conflicti593 – 5931A → V in CAE45889 (PubMed:17974005).Curated
Sequence conflicti696 – 6961E → K in BAG65465 (PubMed:14702039).Curated
Sequence conflicti766 – 7661E → V in BX648753 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti257 – 2571S → C.2 Publications
Corresponds to variant rs3100906 [ dbSNP | Ensembl ].
VAR_034488

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MKSRF…LNASL → MPKTCQCYVGTKTTNPSAWP S in isoform 2. 1 PublicationVSP_008396Add
BLAST
Alternative sequencei22 – 821800Missing in isoform 2. 1 PublicationVSP_010462Add
BLAST
Alternative sequencei78 – 11942Missing in isoform 4. 2 PublicationsVSP_041064Add
BLAST
Alternative sequencei221 – 24525Missing in isoform 5. 1 PublicationVSP_041065Add
BLAST
Alternative sequencei562 – 58221Missing in isoform 3. 1 PublicationVSP_041066Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000913 mRNA. No translation available.
AK093783 mRNA. Translation: BAG52763.1. Different initiation.
AK293236 mRNA. Translation: BAG56774.1.
AK295010 mRNA. Translation: BAG58070.1. Sequence problems.
AK304695 mRNA. Translation: BAG65465.1.
BX640804 mRNA. Translation: CAE45886.1.
BX640807 mRNA. Translation: CAE45889.1.
BX648753 mRNA. No translation available.
AL591767 Genomic DNA. No translation available.
AL627171 Genomic DNA. No translation available.
BC006001 mRNA. Translation: AAH06001.1. Sequence problems.
BC020794 mRNA. Translation: AAH20794.2. Different initiation.
BC056687 mRNA. Translation: AAH56687.1. Sequence problems.
BC064364 mRNA. Translation: AAH64364.1.
BC107764 mRNA. Translation: AAI07765.1. Different initiation.
AF039687 mRNA. Translation: AAC18036.1. Frameshift.
CCDSiCCDS9694.1. [O60524-1]
RefSeqiNP_001288661.1. NM_001301732.1.
NP_004704.2. NM_004713.4.
UniGeneiHs.655964.

Genome annotation databases

EnsembliENST00000298310; ENSP00000298310; ENSG00000165525. [O60524-1]
GeneIDi9147.
KEGGihsa:9147.
UCSCiuc001wxc.4. human. [O60524-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK000913 mRNA. No translation available.
AK093783 mRNA. Translation: BAG52763.1. Different initiation.
AK293236 mRNA. Translation: BAG56774.1.
AK295010 mRNA. Translation: BAG58070.1. Sequence problems.
AK304695 mRNA. Translation: BAG65465.1.
BX640804 mRNA. Translation: CAE45886.1.
BX640807 mRNA. Translation: CAE45889.1.
BX648753 mRNA. No translation available.
AL591767 Genomic DNA. No translation available.
AL627171 Genomic DNA. No translation available.
BC006001 mRNA. Translation: AAH06001.1. Sequence problems.
BC020794 mRNA. Translation: AAH20794.2. Different initiation.
BC056687 mRNA. Translation: AAH56687.1. Sequence problems.
BC064364 mRNA. Translation: AAH64364.1.
BC107764 mRNA. Translation: AAI07765.1. Different initiation.
AF039687 mRNA. Translation: AAC18036.1. Frameshift.
CCDSiCCDS9694.1. [O60524-1]
RefSeqiNP_001288661.1. NM_001301732.1.
NP_004704.2. NM_004713.4.
UniGeneiHs.655964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J92electron microscopy3.60u/v1-501[»]
ProteinModelPortaliO60524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO60524. 10 interactions.
STRINGi9606.ENSP00000298310.

PTM databases

iPTMnetiO60524.
PhosphoSiteiO60524.

Polymorphism and mutation databases

BioMutaiNEMF.

Proteomic databases

EPDiO60524.
MaxQBiO60524.
PaxDbiO60524.
PRIDEiO60524.

Protocols and materials databases

DNASUi9147.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298310; ENSP00000298310; ENSG00000165525. [O60524-1]
GeneIDi9147.
KEGGihsa:9147.
UCSCiuc001wxc.4. human. [O60524-1]

Organism-specific databases

CTDi9147.
GeneCardsiNEMF.
H-InvDBHIX0011634.
HGNCiHGNC:10663. NEMF.
HPAiHPA004160.
MIMi608378. gene.
neXtProtiNX_O60524.
PharmGKBiPA35593.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2030. Eukaryota.
COG1293. LUCA.
GeneTreeiENSGT00390000018516.
HOVERGENiHBG079170.
InParanoidiO60524.
OMAiMFLEFFA.
OrthoDBiEOG76T9QJ.
PhylomeDBiO60524.
TreeFamiTF300515.

Miscellaneous databases

ChiTaRSiNEMF. human.
GenomeRNAii9147.
NextBioi34311.
PROiO60524.
SOURCEiSearch...

Gene expression databases

BgeeiO60524.
CleanExiHS_SDCCAG1.
ExpressionAtlasiO60524. baseline and differential.
GenevisibleiO60524. HS.

Family and domain databases

InterProiIPR021846. DUF3441.
IPR008532. DUF814.
[Graphical view]
PfamiPF11923. DUF3441. 1 hit.
PF05670. DUF814. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1041 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1049 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-518 (ISOFORM 1), VARIANT CYS-257.
    Tissue: Astrocyte, Brain, Embryo, Thymus and Uterus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-1076 (ISOFORM 1).
    Tissue: Small intestine.
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] OF 1-438 AND 620-1076 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-432 (ISOFORM 4), VARIANT CYS-257.
    Tissue: Brain, Kidney and Placenta.
  5. "Characterization of human colon cancer antigens recognized by autologous antibodies."
    Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
    Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 712-1076.
    Tissue: Colon carcinoma.
  6. "Drosophila caliban, a nuclear export mediator, can function as a tumor suppressor in human lung cancer cells."
    Bi X., Jones T., Abbasi F., Lee H., Stultz B., Hursh D.A., Mortin M.A.
    Oncogene 24:8229-8239(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, MISCELLANEOUS.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417; SER-747; SER-748 AND SER-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-831, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-417; SER-747 AND SER-748, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Structure and assembly pathway of the ribosome quality control complex."
    Shao S., Brown A., Santhanam B., Hegde R.S.
    Mol. Cell 57:433-444(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNEMF_HUMAN
AccessioniPrimary (citable) accession number: O60524
Secondary accession number(s): A0JLQ3
, B3KSK1, B4DDL3, B4DHA9, B4E3F3, Q32Q66, Q8WW70, Q9NWG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: November 24, 2009
Last modified: March 16, 2016
This is version 128 of the entry and version 4 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

Miscellaneous

Active in normal lung tissue, but is inactive in several lung cancer cell lines.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.