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P52948 - NUP98_HUMAN

UniProt

P52948 - NUP98_HUMAN

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Protein

Nuclear pore complex protein Nup98-Nup96

Gene

NUP98

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

Functioni

Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. Nup98 and Nup96 are involved in the bidirectional transport across the NPC. May anchor NUP153 and TPR to the NPC.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei531 – 5322Breakpoint for translocation to form NUP98-CCDC28A
Sitei531 – 5322Breakpoint for translocation to form NUP98-PHF23 oncogene

GO - Molecular functioni

  1. peptide binding Source: Ensembl
  2. structural constituent of nuclear pore Source: UniProtKB
  3. transporter activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. DNA replication Source: UniProtKB
  4. glucose transport Source: Reactome
  5. hexose transport Source: Reactome
  6. mitotic cell cycle Source: Reactome
  7. mitotic nuclear envelope disassembly Source: Reactome
  8. mRNA transport Source: UniProtKB-KW
  9. nuclear pore complex assembly Source: UniProtKB
  10. nuclear pore organization Source: UniProtKB
  11. nucleocytoplasmic transport Source: UniProtKB
  12. protein import into nucleus, docking Source: UniProtKB
  13. regulation of glucose transport Source: Reactome
  14. small molecule metabolic process Source: Reactome
  15. transmembrane transport Source: Reactome
  16. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA transport, Protein transport, Translocation, Transport

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Protein family/group databases

MEROPSiS59.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear pore complex protein Nup98-Nup96
Cleaved into the following 2 chains:
Nuclear pore complex protein Nup98
Alternative name(s):
98 kDa nucleoporin
Nucleoporin Nup98
Short name:
Nup98
Nuclear pore complex protein Nup96
Alternative name(s):
96 kDa nucleoporin
Nucleoporin Nup96
Short name:
Nup96
Gene namesi
Name:NUP98
Synonyms:ADAR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:8068. NUP98.

Subcellular locationi

Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus › nuclear pore complex
Note: Nup96 is localized to the nucleoplasmic side of the nuclear pore complex (NPC), at or near the nucleoplasmic basket. Dissociates from the dissasembled NPC structure early during prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear basket of NPC. Detected in diffuse and discrete intranuclear foci. Remained localized to the nuclear membrane after poliovirus (PV) infection.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nuclear envelope Source: UniProtKB
  3. nuclear inclusion body Source: UniProtKB
  4. nuclear membrane Source: UniProtKB
  5. nuclear periphery Source: UniProtKB
  6. nuclear pore Source: UniProtKB
  7. nuclear pore nuclear basket Source: UniProtKB
  8. nuclear pore outer ring Source: UniProtKB
  9. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving NUP98 is found in a form of acute myeloid leukemia. Translocation t(7;11)(p15;p15) with HOXA9. Translocation t(11;17)(p15;p13) with PHF23.

A chromosomal aberration involving NUP98 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NSD1. Translocation t(8;11)(p11.2;p15) with WHSC1L1.

A chromosomal aberration involving NUP98 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with TOP1.

A chromosomal aberration involving NUP98 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(3;11)(q12.2;p15.4) with LNP1.

A chromosomal aberration involving NUP98 is associated with pediatric acute myeloid leukemia (AML) with intermediate characteristics between M2-M3 French-American-British (FAB) subtypes. Translocation t(9;11)(p22;p15) with PSIP1/LEDGF. The chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1/LEDGF exon 4.

A chromosomal aberration involving NUP98 has been identified in acute leukemias. Translocation t(6;11)(q24.1;p15.5) with CCDC28A. The chimeric transcript is an in-frame fusion of NUP98 exon 13 to CCDC28A exon 2. Ectopic expression of NUP98-CCDC28A in mouse promotes the proliferative capacity and self-renewal potential of hematopoietic progenitors and rapidly induced fatal myeloproliferative neoplasms and defects in the differentiation of the erythro-megakaryocytic lineage.

Organism-specific databases

PharmGKBiPA31856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 880880Nuclear pore complex protein Nup98PRO_0000019929Add
BLAST
Chaini881 – 1817937Nuclear pore complex protein Nup96PRO_0000019930Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241Phosphoserine1 Publication
Modified residuei603 – 6031N6-acetyllysine1 Publication
Modified residuei608 – 6081Phosphoserine5 Publications
Modified residuei612 – 6121Phosphoserine6 Publications
Modified residuei618 – 6181Phosphoserine1 Publication
Modified residuei623 – 6231Phosphoserine5 Publications
Modified residuei625 – 6251Phosphoserine1 Publication
Modified residuei653 – 6531PhosphoserineBy similarity
Modified residuei670 – 6701Phosphothreonine1 Publication
Modified residuei673 – 6731Phosphoserine1 Publication
Modified residuei681 – 6811Phosphoserine1 Publication
Modified residuei683 – 6831Phosphoserine1 Publication
Modified residuei839 – 8391Phosphoserine4 Publications
Modified residuei888 – 8881Phosphoserine6 Publications
Modified residuei934 – 9341Phosphoserine2 Publications
Modified residuei1000 – 10001Phosphothreonine1 Publication
Modified residuei1023 – 10231Phosphoserine1 Publication
Modified residuei1028 – 10281Phosphoserine2 Publications
Modified residuei1043 – 10431Phosphoserine1 Publication
Modified residuei1060 – 10601Phosphoserine2 Publications
Modified residuei1070 – 10701Phosphothreonine1 Publication

Post-translational modificationi

Isoform 1 to isoform 4 are autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98 only, respectively. Cleaved Nup98 is necessary for the targeting of Nup98 to the nuclear pore and the interaction with Nup96.1 Publication
Proteolytically degraded after poliovirus (PV) infection; degradation is partial and NCP- and TPR-binding domains withstand degradation.

Keywords - PTMi

Acetylation, Autocatalytic cleavage, Phosphoprotein

Proteomic databases

MaxQBiP52948.
PaxDbiP52948.
PRIDEiP52948.

PTM databases

PhosphoSiteiP52948.

Miscellaneous databases

PMAP-CutDBP52948.

Expressioni

Gene expression databases

BgeeiP52948.
ExpressionAtlasiP52948. baseline and differential.
GenevestigatoriP52948.

Interactioni

Subunit structurei

Part of the nuclear pore complex (NPC). Nup98 interacts directly with Nup96. Nup98 interacts directly with NUP88 and NUP214, subunits of the cytoplasmic filaments of the NPC (By similarity). Nup96 is part of the Nup160 subcomplex in the nuclear pore which is composed of NUP160, NUP133, NUP107 and Nup96. This complex plays a role in RNA export and in tethering Nup98 and NUP153 to the nucleus. Interacts with RAE1. Does not interact with TPR. Interacts with vesicular stomatitis virus protein M.By similarity7 Publications

Protein-protein interaction databases

BioGridi110982. 57 interactions.
DIPiDIP-32484N.
IntActiP52948. 23 interactions.
MINTiMINT-121544.

Structurei

Secondary structure

1
1817
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi168 – 1725Combined sources
Beta strandi181 – 1866Combined sources
Helixi189 – 1913Combined sources
Turni193 – 1975Combined sources
Helixi200 – 20910Combined sources
Beta strandi741 – 7455Combined sources
Helixi747 – 7537Combined sources
Beta strandi761 – 7699Combined sources
Turni770 – 7723Combined sources
Beta strandi773 – 78210Combined sources
Helixi788 – 7914Combined sources
Beta strandi792 – 7954Combined sources
Beta strandi798 – 8014Combined sources
Helixi805 – 8073Combined sources
Beta strandi819 – 8235Combined sources
Turni831 – 8333Combined sources
Helixi840 – 8456Combined sources
Helixi848 – 85811Combined sources
Beta strandi862 – 8676Combined sources
Turni868 – 8714Combined sources
Beta strandi872 – 8798Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KO6X-ray3.00A/C695-880[»]
B/D881-941[»]
2Q5XX-ray1.90A733-887[»]
2Q5YX-ray2.30A/C729-880[»]
3MMYX-ray1.65B/D/F/H158-213[»]
4OWRX-ray3.15B157-213[»]
ProteinModelPortaliP52948.
SMRiP52948. Positions 158-213, 729-880.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini738 – 880143Peptidase S59PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156FG repeats 1Add
BLAST
Regioni157 – 21357GLEBS; interaction with RAE1Add
BLAST
Regioni214 – 480267FG repeats 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 480474Gly/Thr-richAdd
BLAST
Compositional biasi890 – 8945Poly-Glu

Domaini

Contains G-L-F-G repeats. The FG repeat domains in Nup98 have a direct role in the transport.

Sequence similaritiesi

Belongs to the nucleoporin GLFG family.Curated
Contains 1 peptidase S59 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074799.
HOVERGENiHBG052702.
InParanoidiP52948.
KOiK14297.
OMAiTSFHEES.
OrthoDBiEOG77WWBT.
PhylomeDBiP52948.
TreeFamiTF343335.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P52948-1) [UniParc]FASTAAdd to Basket

Also known as: Nup98-Nup96 precursor

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
MFNKSFGTPF GGGTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG 
        60         70         80         90        100
LFGNSQTKPG GLFGTSSFSQ PATSTSTGFG FGTSTGTANT LFGTASTGTS 
       110        120        130        140        150
LFSSQNNAFA QNKPTGFGNF GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP 
       160        170        180        190        200
SSFTAAPTGT TIKFNPPTGT DTMVKAGVST NISTKHQCIT AMKEYESKSL 
       210        220        230        240        250
EELRLEDYQA NRKGPQNQVG AGTTTGLFGS SPATSSATGL FSSSTTNSGF 
       260        270        280        290        300
AYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTQNTGF 
       310        320        330        340        350
SFGNTSTIGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF 
       360        370        380        390        400
GQTNTGFGAV GSTLFGNNKL TTFGSSTTSA PSFGTTSGGL FGNKPTLTLG 
       410        420        430        440        450
TNTNTSNFGF GTNTSGNSIF GSKPAPGTLG TGLGAGFGTA LGAGQASLFG 
       460        470        480        490        500
NNQPKIGGPL GTGAFGAPGF NTTTATLGFG APQAPVALTD PNASAAQQAV 
       510        520        530        540        550
LQQHINSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA QKALTTPTHY 
       560        570        580        590        600
KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL 
       610        620        630        640        650
VLKNLNNSNL FSPVNRDSEN LASPSEYPEN GERFSFLSKP VDENHQQDGD 
       660        670        680        690        700
EDSLVSHFYT NPIAKPIPQT PESAGNKHSN SNSVDDTIVA LNMRAALRNG 
       710        720        730        740        750
LEGSSEETSF HDESLQDDRE EIENNSYHMH PAGIILTKVG YYTIPSMDDL 
       760        770        780        790        800
AKITNEKGEC IVSDFTIGRK GYGSIYFEGD VNLTNLNLDD IVHIRRKEVV 
       810        820        830        840        850
VYLDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP DRLADINYEG 
       860        870        880        890        900
RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPSKTS 
       910        920        930        940        950
TKKLKTAPLP PASQTTPLQM ALNGKPAPPP QSQSPEVEQL GRVVELDSDM 
       960        970        980        990       1000
VDITQEPVLD TMLEESMPED QEPVSASTHI ASSLGINPHV LQIMKASLLT 
      1010       1020       1030       1040       1050
DEEDVDMALD QRFSRLPSKA DTSQEICSPR LPISASHSSK TRSLVGGLLQ 
      1060       1070       1080       1090       1100
SKFTSGAFLS PSVSVQECRT PRAASLMNIP STSSWSVPPP LTSVFTMPSP 
      1110       1120       1130       1140       1150
APEVPLKTVG TRRQLGLVPR EKSVTYGKGK LLMDMALFMG RSFRVGWGPN 
      1160       1170       1180       1190       1200
WTLANSGEQL NGSHELENHQ IADSMEFGFL PNPVAVKPLT ESPFKVHLEK 
      1210       1220       1230       1240       1250
LSLRQRKPDE DMKLYQTPLE LKLKHSTVHV DELCPLIVPN LGVAVIHDYA 
      1260       1270       1280       1290       1300
DWVKEASGDL PEAQIVKHWS LTWTLCEALW GHLKELDSQL NEPREYIQIL 
      1310       1320       1330       1340       1350
ERRRAFSRWL SCTATPQIEE EVSLTQKNSP VEAVFSYLTG KRISEACSLA 
      1360       1370       1380       1390       1400
QQSGDHRLAL LLSQFVGSQS VRELLTMQLV DWHQLQADSF IQDERLRIFA 
      1410       1420       1430       1440       1450
LLAGKPVWQL SEKKQINVCS QLDWKRSLAI HLWYLLPPTA SISRALSMYE 
      1460       1470       1480       1490       1500
EAFQNTSDSD RYACSPLPSY LEGSGCVIAE EQNSQTPLRD VCFHLLKLYS 
      1510       1520       1530       1540       1550
DRHYDLNQLL EPRSITADPL DYRLSWHLWE VLRALNYTHL SAQCEGVLQA 
      1560       1570       1580       1590       1600
SYAGQLESEG LWEWAIFVLL HIDNSGIREK AVRELLTRHC QLLETPESWA 
      1610       1620       1630       1640       1650
KETFLTQKLR VPAKWIHEAK AVRAHMESDK HLEALCLFKA EHWNRCHKLI 
      1660       1670       1680       1690       1700
IRHLASDAII NENYDYLKGF LEDLAPPERS SLIQDWETSG LVYLDYIRVI 
      1710       1720       1730       1740       1750
EMLRHIQQVD CSGNDLEQLH IKVTSLCSRI EQIQCYSAKD RLAQSDMAKR 
      1760       1770       1780       1790       1800
VANLLRVVLS LHHPPDRTSD STPDPQRVPL RLLAPHIGRL PMPEDYAMDE 
      1810 
LRSLTQSYLR ELAVGSL
Length:1,817
Mass (Da):197,579
Last modified:October 5, 2010 - v4
Checksum:iBC60E5456B936C79
GO
Isoform 2 (identifier: P52948-2) [UniParc]FASTAAdd to Basket

Also known as: Nup98-Nup96 precursor splice variant 1

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
     1502-1576: RHYDLNQLLE...FVLLHIDNSG → S

Show »
Length:1,726
Mass (Da):187,199
Checksum:i0F92C34F9FD7DC92
GO
Isoform 3 (identifier: P52948-3) [UniParc]FASTAAdd to Basket

Also known as: Nup98-specific 1

The sequence of this isoform differs from the canonical sequence as follows:
     932-937: SQSPEV → VEKKGQ
     938-1817: Missing.

Show »
Length:937
Mass (Da):97,836
Checksum:i2CB6CE36734F0B82
GO
Isoform 4 (identifier: P52948-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.
     932-937: SQSPEV → VEKKGQ
     938-1817: Missing.

Show »
Length:920
Mass (Da):96,075
Checksum:i129DABAFB69253AD
GO
Isoform 5 (identifier: P52948-5) [UniParc]FASTAAdd to Basket

Also known as: Nup196, ADIR2

The sequence of this isoform differs from the canonical sequence as follows:
     393-409: Missing.

Show »
Length:1,800
Mass (Da):195,817
Checksum:i4BCA483C2E9E1A8E
GO
Isoform 6 (identifier: P52948-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1085-1188: WSVPPPLTSV...FLPNPVAVKP → C

Show »
Length:1,714
Mass (Da):186,268
Checksum:i158300FBC47A0C0C
GO

Sequence cautioni

The sequence AAD22395.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAD22396.1 differs from that shown.Contaminating sequence. Sequence of unknown origin in the C-terminal part.Curated
The sequence AAF19342.1 differs from that shown. Reason: Frameshift at position 1551. Curated
The sequence AAF19342.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti318 – 3181L → S in AAH41136. (PubMed:15489334)Curated
Sequence conflicti376 – 3761S → G in AAH41136. (PubMed:15489334)Curated
Sequence conflicti756 – 7572EK → VF in AAD22395. (PubMed:10087256)Curated
Sequence conflicti756 – 7572EK → VF in AAD22396. (PubMed:10087256)Curated
Sequence conflicti1281 – 12811G → A in AAD22395. (PubMed:10087256)Curated
Sequence conflicti1281 – 12811G → A in AAD22396. (PubMed:10087256)Curated
Sequence conflicti1281 – 12811G → A in AAL56659. 1 PublicationCurated
Sequence conflicti1534 – 15363ALN → DLK in AAD22395. (PubMed:10087256)Curated
Sequence conflicti1594 – 15941E → D in AAF19342. 1 PublicationCurated
Sequence conflicti1598 – 15981S → T in AAL56659. 1 PublicationCurated
Sequence conflicti1639 – 16391K → N in AAF19342. 1 PublicationCurated
Sequence conflicti1680 – 16801S → T in AAF19342. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1669 – 16691G → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035859

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei393 – 40917Missing in isoform 2, isoform 4 and isoform 5. 7 PublicationsVSP_003619Add
BLAST
Alternative sequencei932 – 9376SQSPEV → VEKKGQ in isoform 3 and isoform 4. 3 PublicationsVSP_007942
Alternative sequencei938 – 1817880Missing in isoform 3 and isoform 4. 3 PublicationsVSP_007943Add
BLAST
Alternative sequencei1085 – 1188104WSVPP…VAVKP → C in isoform 6. 1 PublicationVSP_038328Add
BLAST
Alternative sequencei1502 – 157675RHYDL…IDNSG → S in isoform 2. 1 PublicationVSP_007944Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41815 mRNA. Translation: AAC50366.1.
AB040538 mRNA. Translation: BAB18537.1.
AF071076 mRNA. Translation: AAD22395.1. Sequence problems.
AF071077 mRNA. Translation: AAD22396.1. Sequence problems.
AF231130 mRNA. Translation: AAL56659.1.
AC060812 Genomic DNA. No translation available.
AC090587 Genomic DNA. No translation available.
BC041136 mRNA. Translation: AAH41136.1.
BC012906 mRNA. Translation: AAH12906.2.
AF116074 mRNA. Translation: AAF19342.1. Sequence problems.
BT007349 mRNA. Translation: AAP36013.1.
AL133601 mRNA. Translation: CAB63736.1.
AL137613 mRNA. Translation: CAB70842.1.
CCDSiCCDS31347.1. [P52948-2]
CCDS41605.1. [P52948-3]
CCDS41606.1. [P52948-4]
CCDS7746.1. [P52948-5]
PIRiT43443.
RefSeqiNP_005378.4. NM_005387.5. [P52948-3]
NP_057404.2. NM_016320.4. [P52948-5]
NP_624357.1. NM_139131.3. [P52948-4]
NP_624358.2. NM_139132.3. [P52948-2]
XP_005253007.1. XM_005252950.1. [P52948-1]
UniGeneiHs.524750.

Genome annotation databases

EnsembliENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1]
ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
GeneIDi4928.
KEGGihsa:4928.
UCSCiuc001lyh.3. human. [P52948-5]
uc001lyi.3. human. [P52948-2]
uc001lyj.2. human. [P52948-4]
uc001lyk.2. human. [P52948-3]

Polymorphism databases

DMDMi308153660.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41815 mRNA. Translation: AAC50366.1.
AB040538 mRNA. Translation: BAB18537.1.
AF071076 mRNA. Translation: AAD22395.1. Sequence problems.
AF071077 mRNA. Translation: AAD22396.1. Sequence problems.
AF231130 mRNA. Translation: AAL56659.1.
AC060812 Genomic DNA. No translation available.
AC090587 Genomic DNA. No translation available.
BC041136 mRNA. Translation: AAH41136.1.
BC012906 mRNA. Translation: AAH12906.2.
AF116074 mRNA. Translation: AAF19342.1. Sequence problems.
BT007349 mRNA. Translation: AAP36013.1.
AL133601 mRNA. Translation: CAB63736.1.
AL137613 mRNA. Translation: CAB70842.1.
CCDSiCCDS31347.1. [P52948-2]
CCDS41605.1. [P52948-3]
CCDS41606.1. [P52948-4]
CCDS7746.1. [P52948-5]
PIRiT43443.
RefSeqiNP_005378.4. NM_005387.5. [P52948-3]
NP_057404.2. NM_016320.4. [P52948-5]
NP_624357.1. NM_139131.3. [P52948-4]
NP_624358.2. NM_139132.3. [P52948-2]
XP_005253007.1. XM_005252950.1. [P52948-1]
UniGeneiHs.524750.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KO6X-ray3.00A/C695-880[»]
B/D881-941[»]
2Q5XX-ray1.90A733-887[»]
2Q5YX-ray2.30A/C729-880[»]
3MMYX-ray1.65B/D/F/H158-213[»]
4OWRX-ray3.15B157-213[»]
ProteinModelPortaliP52948.
SMRiP52948. Positions 158-213, 729-880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110982. 57 interactions.
DIPiDIP-32484N.
IntActiP52948. 23 interactions.
MINTiMINT-121544.

Protein family/group databases

MEROPSiS59.001.

PTM databases

PhosphoSiteiP52948.

Polymorphism databases

DMDMi308153660.

Proteomic databases

MaxQBiP52948.
PaxDbiP52948.
PRIDEiP52948.

Protocols and materials databases

DNASUi4928.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000324932; ENSP00000316032; ENSG00000110713. [P52948-5]
ENST00000355260; ENSP00000347404; ENSG00000110713. [P52948-2]
ENST00000359171; ENSP00000352091; ENSG00000110713. [P52948-1]
ENST00000397004; ENSP00000380199; ENSG00000110713. [P52948-4]
ENST00000397007; ENSP00000380202; ENSG00000110713. [P52948-3]
GeneIDi4928.
KEGGihsa:4928.
UCSCiuc001lyh.3. human. [P52948-5]
uc001lyi.3. human. [P52948-2]
uc001lyj.2. human. [P52948-4]
uc001lyk.2. human. [P52948-3]

Organism-specific databases

CTDi4928.
GeneCardsiGC11M003700.
HGNCiHGNC:8068. NUP98.
MIMi601021. gene.
neXtProtiNX_P52948.
PharmGKBiPA31856.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00550000074799.
HOVERGENiHBG052702.
InParanoidiP52948.
KOiK14297.
OMAiTSFHEES.
OrthoDBiEOG77WWBT.
PhylomeDBiP52948.
TreeFamiTF343335.

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_163931. Nuclear Pore Complex (NPC) Disassembly.
REACT_267668. Transcriptional regulation by small RNAs.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_6354. Viral Messenger RNA Synthesis.
REACT_6804. Regulation of Glucokinase by Glucokinase Regulatory Protein.
REACT_682. Mitotic Prometaphase.
REACT_7991. Vpr-mediated nuclear import of PICs.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSiNUP98. human.
EvolutionaryTraceiP52948.
GeneWikiiNUP98.
GenomeRNAii4928.
NextBioi18979.
PMAP-CutDBP52948.
PROiP52948.
SOURCEiSearch...

Gene expression databases

BgeeiP52948.
ExpressionAtlasiP52948. baseline and differential.
GenevestigatoriP52948.

Family and domain databases

Gene3Di3.30.1610.10. 1 hit.
InterProiIPR021967. Nup96.
IPR007230. Peptidase_S59.
[Graphical view]
PfamiPF04096. Nucleoporin2. 1 hit.
PF12110. Nup96. 1 hit.
[Graphical view]
SUPFAMiSSF82215. SSF82215. 1 hit.
PROSITEiPS51434. NUP_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9."
    Borrow J., Shearman A.M., Stanton V.P., Becher R., Collins T., Williams A.J., Dube I., Katz F., Kwong Y.L., Morris C., Ohyashiki K., Toyama K., Rowley J., Housman D.E.
    Nat. Genet. 12:159-167(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), CHROMOSOMAL TRANSLOCATION WITH HOXA9.
  2. "Molecular analysis of the chromosomal breakpoints and identification of the repetitive sequences near the breakpoints of NUP98 in therapy-related leukemia with inv(11)(p15q22)."
    Arai Y., Kaneko Y., Kubo T., Arai K., Hosoda F., Ohki M.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96."
    Fontoura B.M.A., Blobel G., Matunis M.J.
    J. Cell Biol. 144:1097-1112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 1648-1664.
  4. "An alternative splice form of NUP98 encodes a 196kDa NUP196 isoform."
    Borrow J., Housman D.E.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 963-1817 (ISOFORM 6).
    Tissue: Lung carcinoma.
  7. Xu Y.H., Guo B.C., Yu Y.L.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1176-1817 (ISOFORM 5).
    Tissue: Liver.
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-1817 (ISOFORM 5).
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1227-1817 (ISOFORM 5).
    Tissue: Testis.
  10. "The t(11;20)(p15;q11) chromosomal translocation associated with therapy-related myelodysplastic syndrome results in an NUP98-TOP1 fusion."
    Ahuja H.G., Felix C.A., Aplan P.D.
    Blood 94:3258-3261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH TOP1.
  11. "RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains."
    Pritchard C.E., Fornerod M., Kasper L.H., van Deursen J.M.
    J. Cell Biol. 145:237-254(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAE1.
  12. "Vesicular stomatitis virus matrix protein inhibits host cell gene expression by targeting the nucleoporin Nup98."
    von Kobbe C., van Deursen J.M., Rodrigues J.P., Sitterlin D., Bachi A., Wu X., Wilm M., Carmo-Fonseca M., Izaurralde E.
    Mol. Cell 6:1243-1252(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VESICULAR STOMATITIS VIRUS PROTEIN M.
  13. "A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia."
    Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K., Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J., Wainscoat J.S.
    Blood 98:1264-1267(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH NSD1.
  14. "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export."
    Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.
    J. Cell Biol. 155:339-354(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  15. "NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15)."
    Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., Vallespi T., Negrini M., Martelli M.F., Mecucci C.
    Blood 99:3857-3860(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH WHSC1L1.
  16. "Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export."
    Frosst P., Guan T., Subauste C., Hahn K., Gerace L.
    J. Cell Biol. 156:617-630(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex."
    Hase M.E., Cordes V.C.
    Mol. Biol. Cell 14:1923-1940(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ABSENCE OF INTERACTION WITH TPR, SUBCELLULAR LOCATION.
  18. "Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket."
    Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., Cordes V.C.
    Mol. Biol. Cell 15:4261-4277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION.
  19. "Characterization of 6q abnormalities in childhood acute myeloid leukemia and identification of a novel t(6;11)(q24.1;p15.5) resulting in a NUP98-C6orf80 fusion in a case of acute megakaryoblastic leukemia."
    Tosi S., Ballabio E., Teigler-Schlegel A., Boultwood J., Bruch J., Harbott J.
    Genes Chromosomes Cancer 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98, DISEASE.
  20. "t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute myeloid leukemia."
    Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E., Micalizzi C., Panarello C.
    Leuk. Res. 29:467-470(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH PSIP1/LEDGF.
  21. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-839 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: CHROMOSOMAL TRANSLOCATION WITH LNP1.
  23. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-623; SER-1028 AND SER-1060, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "A novel NUP98-PHF23 fusion resulting from a cryptic translocation t(11;17)(p15;p13) in acute myeloid leukemia."
    Reader J.C., Meekins J.S., Gojo I., Ning Y.
    Leukemia 21:842-844(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH PHF23.
    Tissue: Peripheral blood.
  25. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608 AND SER-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623; SER-839; SER-888; SER-934; THR-1000; SER-1023; SER-1028; SER-1043; SER-1060 AND THR-1070, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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-608; SER-612; SER-618; SER-623 AND SER-625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  31. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion."
    Krull S., Dorries J., Boysen B., Reidenbach S., Magnius L., Norder H., Thyberg J., Cordes V.C.
    EMBO J. 29:1659-1673(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
  33. "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-524; SER-608; SER-612; SER-623; THR-670; SER-673; SER-681; SER-839; SER-888 AND SER-934, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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-612; SER-623; SER-683; SER-839 AND SER-888, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
  37. "The three-dimensional structure of the autoproteolytic, nuclear pore-targeting domain of the human nucleoporin Nup98."
    Hodel A.E., Hodel M.R., Griffis E.R., Hennig K.A., Ratner G.A., Xu S., Powers M.A.
    Mol. Cell 10:347-358(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 710-870 OF NUP98, INTERACTION WITH NUP96.
  38. "Structural constraints on autoprocessing of the human nucleoporin Nup98."
    Sun Y., Guo H.C.
    Protein Sci. 17:494-505(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 733-887, SUBUNIT, AUTOPROTEOLYTIC PROCESSING.
  39. "Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1."
    Ren Y., Seo H.S., Blobel G., Hoelz A.
    Proc. Natl. Acad. Sci. U.S.A. 107:10406-10411(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 158-213 IN COMPLEX WITH RAE1.
  40. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-1669.
+Additional computationally mapped references.

Entry informationi

Entry nameiNUP98_HUMAN
AccessioniPrimary (citable) accession number: P52948
Secondary accession number(s): Q8IUT2
, Q8WYB0, Q96E54, Q9H3Q4, Q9NT02, Q9UF57, Q9UHX0, Q9Y6J4, Q9Y6J5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 5, 2010
Last modified: February 4, 2015
This is version 164 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.