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Protein

TRAF3-interacting protein 1

Gene

TRAF3IP1

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

Functioni

Plays an inhibitory role on IL13 signaling by binding to IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation, transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to the microtubules. Involved in kidney development and epithelial morphogenesis. Involved in the regulation of microtubule cytoskeleton organization. Is a negative regulator of microtubule stability, acting through the control of MAP4 levels (PubMed:26487268). Involved in ciliogenesis (By similarity).By similarity4 Publications

GO - Biological processi

  • cilium assembly Source: GO_Central
  • embryonic camera-type eye development Source: Ensembl
  • embryonic digit morphogenesis Source: Ensembl
  • embryonic heart tube development Source: Ensembl
  • intraciliary transport Source: GO_Central
  • kidney development Source: UniProtKB
  • morphogenesis of a polarized epithelium Source: UniProtKB
  • negative regulation of defense response to virus Source: CACAO
  • negative regulation of interferon-beta production Source: Ensembl
  • negative regulation of protein complex assembly Source: CACAO
  • negative regulation of protein phosphorylation Source: CACAO
  • negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: Ensembl
  • negative regulation of type I interferon production Source: CACAO
  • neural tube patterning Source: Ensembl
  • organelle organization Source: Reactome
  • post-anal tail morphogenesis Source: Ensembl
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation

Enzyme and pathway databases

ReactomeiR-HSA-5620924. Intraflagellar transport.

Names & Taxonomyi

Protein namesi
Recommended name:
TRAF3-interacting protein 1
Alternative name(s):
Interleukin-13 receptor alpha 1-binding protein 1
Intraflagellar transport protein 54 homolog
Microtubule-interacting protein associated with TRAF3
Short name:
MIP-T3
Gene namesi
Name:TRAF3IP1
Synonyms:IFT54, MIPT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:17861. TRAF3IP1.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: Ensembl
  • centrosome Source: GO_Central
  • ciliary basal body Source: Ensembl
  • ciliary base Source: UniProtKB
  • ciliary tip Source: UniProtKB
  • ciliary transition zone Source: UniProtKB
  • cilium Source: GO_Central
  • cytoplasm Source: UniProtKB-KW
  • intraciliary transport particle B Source: UniProtKB
  • primary cilium Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Senior-Loken syndrome 9 (SLSN9)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal-retinal disorder characterized by progressive wasting of the filtering unit of the kidney (nephronophthisis), with or without medullary cystic renal disease, and progressive eye disease. Typically this disorder becomes apparent during the first year of life.
See also OMIM:616629
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171I → S in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075068
Natural varianti125 – 1251V → A in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075069
Natural varianti125 – 1251V → M in SLSN9; results in altered folding of the N-terminus; does not localize to the ciliary tip and transition zone; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075070
Natural varianti520 – 5201M → R in SLSN9; does not localize to the ciliary tip. 1 Publication
VAR_075071

Keywords - Diseasei

Ciliopathy, Disease mutation, Leber congenital amaurosis, Nephronophthisis, Senior-Loken syndrome

Organism-specific databases

MIMi616629. phenotype.
PharmGKBiPA134943602.

Polymorphism and mutation databases

BioMutaiTRAF3IP1.
DMDMi74727348.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 691691TRAF3-interacting protein 1PRO_0000299544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171PhosphoserineBy similarity
Modified residuei476 – 4761PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8TDR0.
PaxDbiQ8TDR0.
PRIDEiQ8TDR0.

PTM databases

iPTMnetiQ8TDR0.
PhosphoSiteiQ8TDR0.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8TDR0.
CleanExiHS_TRAF3IP1.
ExpressionAtlasiQ8TDR0. baseline and differential.
GenevisibleiQ8TDR0. HS.

Organism-specific databases

HPAiHPA037857.
HPA037858.

Interactioni

Subunit structurei

Component of the IFT complex B, at least composed of IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88 (By similarity). Interacts with IL13RA1 (PubMed:10791955). Binds to microtubules, TRAF3 and DISC1 (PubMed:12812986, PubMed:12935900). Interacts with MAP4 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DISC1Q9NRI510EBI-928811,EBI-529989
IL13RA1P785523EBI-928811,EBI-1391535
TRAF3Q131148EBI-928811,EBI-357631

Protein-protein interaction databases

BioGridi117577. 69 interactions.
IntActiQ8TDR0. 58 interactions.
STRINGi9606.ENSP00000362424.

Structurei

Secondary structure

1
691
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1613Combined sources
Turni24 – 285Combined sources
Helixi32 – 4514Combined sources
Turni50 – 523Combined sources
Helixi55 – 584Combined sources
Helixi60 – 623Combined sources
Helixi66 – 8419Combined sources
Helixi92 – 954Combined sources
Turni96 – 983Combined sources
Helixi101 – 11616Combined sources
Helixi123 – 1308Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQONMR-A1-133[»]
ProteinModelPortaliQ8TDR0.
SMRiQ8TDR0. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8TDR0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 323323Abolishes microtubules-binding when missingAdd
BLAST
Regioni223 – 691469DISC1-interaction domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili571 – 66696Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 28171Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the TRAF3IP1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3809. Eukaryota.
ENOG410ZHUT. LUCA.
GeneTreeiENSGT00720000108822.
HOGENOMiHOG000007159.
HOVERGENiHBG101388.
InParanoidiQ8TDR0.
KOiK19680.
OMAiFLQKMID.
OrthoDBiEOG7BKCV3.
PhylomeDBiQ8TDR0.
TreeFamiTF315473.

Family and domain databases

InterProiIPR018799. TRAF3IP1.
[Graphical view]
PANTHERiPTHR31363. PTHR31363. 3 hits.

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q8TDR0-1) [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
MNAAVVRRTQ EALGKVIRRP PLTEKLLSKP PFRYLHDIIT EVIRMTGFMK
60 70 80 90 100
GLYTDAEMKS DNVKDKDAKI SFLQKAIDVV VMVSGEPLLA KPARIVAGHE
110 120 130 140 150
PERTNELLQI IGKCCLNKLS SDDAVRRVLA GEKGEVKGRA SLTSRSQELD
160 170 180 190 200
NKNVREEESR VHKNTEDRGD AEIKERSTSR DRKQKEELKE DRKPREKDKD
210 220 230 240 250
KEKAKENGGN RHREGERERA KARARPDNER QKDRGNRERD RDSERKKETE
260 270 280 290 300
RKSEGGKEKE RLRDRDRERD RDKGKDRDRR RVKNGEHSWD LDREKNREHD
310 320 330 340 350
KPEKKSASSG EMSKKLSDGT FKDSKAETET EISTRASKSL TTKTSKRRSK
360 370 380 390 400
NSVEGRKEDN ISAKSLDSIV SGINNEPNQE TTTSEIGTKE ANINSTSISD
410 420 430 440 450
DNSASLRCEN IQPNPTEKQK GDSTSDAEGD AGPAGQDKSE VPETPEIPNE
460 470 480 490 500
LSSNIRRIPR PGSARPAPPR VKRQDSMEAL QMDRSGSGKT VSNVITESHN
510 520 530 540 550
SDNEEDDQFV VEAAPQLSEM SEIEMVTAVE LEEEEKHGGL VKKILETKKD
560 570 580 590 600
YEKLQQSPKP GEKERSLFES AWKKEKDIVS KEIEKLRTSI QTLCKSALPL
610 620 630 640 650
GKIMDYIQED VDAMQNELQM WHSENRQHAE ALQQEQRITD CAVEPLKAEL
660 670 680 690
AELEQLIKDQ QDKICAVKAN ILKNEEKIQK MVYSINLTSR R
Length:691
Mass (Da):78,632
Last modified:June 1, 2002 - v1
Checksum:i0675AA0E5319D2EB
GO
Isoform 2 (identifier: Q8TDR0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     355-420: Missing.

Show »
Length:625
Mass (Da):71,529
Checksum:iFDF49249C140E026
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171I → S in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075068
Natural varianti125 – 1251V → A in SLSN9; results in altered folding of the N-terminus; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075069
Natural varianti125 – 1251V → M in SLSN9; results in altered folding of the N-terminus; does not localize to the ciliary tip and transition zone; does not affect interaction with IFT20; loss of interaction with MAP4. 1 Publication
VAR_075070
Natural varianti228 – 2281N → S.1 Publication
Corresponds to variant rs3769110 [ dbSNP | Ensembl ].
VAR_034841
Natural varianti239 – 2391R → W.
Corresponds to variant rs34723381 [ dbSNP | Ensembl ].
VAR_034842
Natural varianti295 – 2951K → N.
Corresponds to variant rs12464423 [ dbSNP | Ensembl ].
VAR_051185
Natural varianti416 – 4161T → S.
Corresponds to variant rs58277463 [ dbSNP | Ensembl ].
VAR_061685
Natural varianti520 – 5201M → R in SLSN9; does not localize to the ciliary tip. 1 Publication
VAR_075071
Natural varianti620 – 6201M → L.
Corresponds to variant rs3739070 [ dbSNP | Ensembl ].
VAR_034843

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei355 – 42066Missing in isoform 2. 3 PublicationsVSP_027734Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230877 mRNA. Translation: AAF76984.1.
AF242456 mRNA. Translation: AAL90444.1.
AC012485 Genomic DNA. Translation: AAX88977.1.
CH471063 Genomic DNA. Translation: EAW71157.1.
BC059174 mRNA. Translation: AAH59174.1.
AL080153 mRNA. Translation: CAB45744.1.
CCDSiCCDS33415.1. [Q8TDR0-1]
CCDS46557.1. [Q8TDR0-2]
PIRiT12536.
RefSeqiNP_001132962.1. NM_001139490.1. [Q8TDR0-2]
NP_056465.2. NM_015650.3. [Q8TDR0-1]
UniGeneiHs.631898.

Genome annotation databases

EnsembliENST00000373327; ENSP00000362424; ENSG00000204104. [Q8TDR0-1]
ENST00000391993; ENSP00000375851; ENSG00000204104. [Q8TDR0-2]
GeneIDi26146.
KEGGihsa:26146.
UCSCiuc002vye.4. human. [Q8TDR0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230877 mRNA. Translation: AAF76984.1.
AF242456 mRNA. Translation: AAL90444.1.
AC012485 Genomic DNA. Translation: AAX88977.1.
CH471063 Genomic DNA. Translation: EAW71157.1.
BC059174 mRNA. Translation: AAH59174.1.
AL080153 mRNA. Translation: CAB45744.1.
CCDSiCCDS33415.1. [Q8TDR0-1]
CCDS46557.1. [Q8TDR0-2]
PIRiT12536.
RefSeqiNP_001132962.1. NM_001139490.1. [Q8TDR0-2]
NP_056465.2. NM_015650.3. [Q8TDR0-1]
UniGeneiHs.631898.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQONMR-A1-133[»]
ProteinModelPortaliQ8TDR0.
SMRiQ8TDR0. Positions 1-133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117577. 69 interactions.
IntActiQ8TDR0. 58 interactions.
STRINGi9606.ENSP00000362424.

PTM databases

iPTMnetiQ8TDR0.
PhosphoSiteiQ8TDR0.

Polymorphism and mutation databases

BioMutaiTRAF3IP1.
DMDMi74727348.

Proteomic databases

MaxQBiQ8TDR0.
PaxDbiQ8TDR0.
PRIDEiQ8TDR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373327; ENSP00000362424; ENSG00000204104. [Q8TDR0-1]
ENST00000391993; ENSP00000375851; ENSG00000204104. [Q8TDR0-2]
GeneIDi26146.
KEGGihsa:26146.
UCSCiuc002vye.4. human. [Q8TDR0-1]

Organism-specific databases

CTDi26146.
GeneCardsiTRAF3IP1.
HGNCiHGNC:17861. TRAF3IP1.
HPAiHPA037857.
HPA037858.
MIMi607380. gene.
616629. phenotype.
neXtProtiNX_Q8TDR0.
PharmGKBiPA134943602.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3809. Eukaryota.
ENOG410ZHUT. LUCA.
GeneTreeiENSGT00720000108822.
HOGENOMiHOG000007159.
HOVERGENiHBG101388.
InParanoidiQ8TDR0.
KOiK19680.
OMAiFLQKMID.
OrthoDBiEOG7BKCV3.
PhylomeDBiQ8TDR0.
TreeFamiTF315473.

Enzyme and pathway databases

ReactomeiR-HSA-5620924. Intraflagellar transport.

Miscellaneous databases

ChiTaRSiTRAF3IP1. human.
EvolutionaryTraceiQ8TDR0.
GenomeRNAii26146.
NextBioi48201.
PROiQ8TDR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8TDR0.
CleanExiHS_TRAF3IP1.
ExpressionAtlasiQ8TDR0. baseline and differential.
GenevisibleiQ8TDR0. HS.

Family and domain databases

InterProiIPR018799. TRAF3IP1.
[Graphical view]
PANTHERiPTHR31363. PTHR31363. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network."
    Ling L., Goeddel D.V.
    J. Biol. Chem. 275:23852-23860(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH IL13RA1.
  2. "MIP-T3 associates with IL-13Ralpha1 and suppresses STAT6 activation in response to IL-13 stimulation."
    Niu Y., Murata T., Watanabe K., Kawakami K., Yoshimura A., Inoue J., Puri R.K., Kobayashi N.
    FEBS Lett. 550:139-143(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR LOCATION, REGION, INTERACTION WITH TRAF3.
    Tissue: Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), VARIANT SER-228.
    Tissue: PNS.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-691 (ISOFORM 2).
    Tissue: Testis.
  7. "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation."
    Morris J.A., Kandpal G., Ma L., Austin C.P.
    Hum. Mol. Genet. 12:1591-1608(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DISC1, REGION.
  8. "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-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN SLSN9, VARIANTS SLSN9 SER-17; ALA-125; MET-125 AND ARG-520, CHARACTERIZATION OF VARIANTS SLSN9 SER-17; ALA-125; MET-125 AND ARG-520.
  11. "Solution structure of the STN_TRAF3IP1_ND domain of interleukin 13 receptor alpha 1-binding protein-1 [Homo sapiens]."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-133.

Entry informationi

Entry nameiMIPT3_HUMAN
AccessioniPrimary (citable) accession number: Q8TDR0
Secondary accession number(s): Q6PCT1
, Q7L8N9, Q9NRD6, Q9Y4Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 105 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.