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Protein

Activating signal cointegrator 1

Gene

TRIP4

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

Functioni

Transcription coactivator which associates with nuclear receptors, transcriptional coactivators including EP300, CREBBP and NCOA1, and basal transcription factors like TBP and TFIIA to facilitate nuclear receptors-mediated transcription. May thereby play an important role in establishing distinct coactivator complexes under different cellular conditions. Plays a role in thyroid hormone receptor and estrogen receptor transactivation (PubMed:10454579, PubMed:25219498). Also involved in androgen receptor transactivation (By similarity). Plays a pivotal role in the transactivation of NF-kappa-B, SRF and AP1. Acts as a mediator of transrepression between nuclear receptor and either AP1 or NF-kappa-B (PubMed:12077347).By similarity3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri171 – 18717C4-typeAdd
BLAST

GO - Molecular functioni

  1. estrogen receptor binding Source: UniProtKB
  2. histone acetyltransferase binding Source: UniProtKB
  3. ligand-dependent nuclear receptor binding Source: UniProtKB
  4. protease binding Source: UniProtKB
  5. small conjugating protein ligase binding Source: UniProtKB
  6. transcription coactivator activity Source: ProtInc
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. intracellular estrogen receptor signaling pathway Source: UniProtKB
  2. positive regulation of transcription, DNA-templated Source: UniProtKB
  3. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Activating signal cointegrator 11 Publication
Short name:
ASC-11 Publication
Alternative name(s):
Thyroid receptor-interacting protein 41 Publication
Short name:
TR-interacting protein 41 Publication
Short name:
TRIP-41 Publication
Gene namesi
Name:TRIP4Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:12310. TRIP4.

Subcellular locationi

Nucleus 2 Publications. Cytoplasmcytosol 2 Publications. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
Note: Cytoplasmic under conditions of serum deprivation (PubMed:10454579). Colocalizes with NEK6 in the centrosome (PubMed:20873783).2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. microtubule organizing center Source: UniProtKB-SubCell
  3. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36988.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 581580Activating signal cointegrator 1PRO_0000065631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei289 – 2891PhosphotyrosineBy similarity
Cross-linki324 – 324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)1 Publication
Cross-linki325 – 325Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)1 Publication
Cross-linki334 – 334Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)1 Publication
Cross-linki367 – 367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1)1 Publication

Post-translational modificationi

Phosphorylated by NEK6.1 Publication
Polyufmylated by the UFM1-conjugating system composed of the enzymes UBA5, UFC1 and UFL1. Deufmylated by the protease UFSP2. Ufmylation of TRIP4 is promoted by ligand-bound nuclear receptors that compete with UFSP2 for interaction with TRIP4. Nuclear receptors-induced ufmylation promotes the recruitment of additional transcriptional coactivators like EP300 and NCOA1 and therefore the assembly of a coactivator complex facilitating nuclear receptor-mediated transcription.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15650.
PaxDbiQ15650.
PeptideAtlasiQ15650.
PRIDEiQ15650.

PTM databases

PhosphoSiteiQ15650.

Expressioni

Gene expression databases

BgeeiQ15650.
CleanExiHS_TRIP4.
ExpressionAtlasiQ15650. baseline and differential.
GenevestigatoriQ15650.

Organism-specific databases

HPAiHPA016605.
HPA050666.

Interactioni

Subunit structurei

Interacts with the thyroid hormone receptor/TR (via the ligand-binding domain); this interaction requires the presence of thyroid hormone (PubMed:10454579). Interacts with the androgen receptor/AR; in an androgen, testosterone and dihydrotestosterone-dependent manner (PubMed:12390891). Interacts with ESR1 (estrogen ligand-bound); competes with UFSP2 (PubMed:10454579, PubMed:25219498). Interacts with UFSP2; competes with ligand-bound ESR1 (PubMed:25219498). Interacts with DDRGK1 and UFL1; the interaction with DDRGK1 is direct (PubMed:25219498). Interacts with NCOA1 (PubMed:25219498). Interacts with EP300 (PubMed:25219498). Exists as a steady-state complex associated with ASCC1, ASCC2 and HELIC1 (PubMed:12077347). Interacts with NEK6 (PubMed:20873783).5 Publications

Protein-protein interaction databases

BioGridi114735. 36 interactions.
IntActiQ15650. 4 interactions.
STRINGi9606.ENSP00000261884.

Structurei

Secondary structure

1
581
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi435 – 4395Combined sources
Helixi443 – 4486Combined sources
Beta strandi454 – 4596Combined sources
Beta strandi465 – 4717Combined sources
Helixi478 – 49215Combined sources
Beta strandi504 – 51815Combined sources
Helixi521 – 5255Combined sources
Turni530 – 5323Combined sources
Beta strandi535 – 54612Combined sources
Beta strandi557 – 5615Combined sources
Helixi564 – 5729Combined sources
Helixi573 – 5753Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ONMR-A435-581[»]
ProteinModelPortaliQ15650.
SMRiQ15650. Positions 434-581.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15650.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni200 – 300101Mediates interaction with DDRGK11 PublicationAdd
BLAST
Regioni300 – 400101Mediates interaction with UFL11 PublicationAdd
BLAST

Domaini

The C4-type zinc finger mediates a competitive interaction with UFSP2 and ligand-bound nuclear receptors. It also mediates interaction with the transcriptional coactivators and the basal transcription machinery.3 Publications

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri171 – 18717C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG248556.
GeneTreeiENSGT00390000005300.
HOGENOMiHOG000006873.
HOVERGENiHBG061618.
InParanoidiQ15650.
OMAiDCLSQEQ.
OrthoDBiEOG7RZ5PP.
PhylomeDBiQ15650.
TreeFamiTF314842.

Family and domain databases

InterProiIPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view]
PfamiPF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view]
SMARTiSM01022. ASCH. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 2 hits.

Sequencei

Sequence statusi: Complete.

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

Q15650-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVAGAVSGE PLVHWCTQQL RKTFGLDVSE EIIQYVLSIE SAEEIREYVT
60 70 80 90 100
DLLQGNEGKK GQFIEELITK WQKNDQELIS DPLQQCFKKD EILDGQKSGD
110 120 130 140 150
HLKRGRKKGR NRQEVPAFTE PDTTAEVKTP FDLAKAQENS NSVKKKTKFV
160 170 180 190 200
NLYTREGQDR LAVLLPGRHP CDCLGQKHKL INNCLICGRI VCEQEGSGPC
210 220 230 240 250
LFCGTLVCTH EEQDILQRDS NKSQKLLKKL MSGVENSGKV DISTKDLLPH
260 270 280 290 300
QELRIKSGLE KAIKHKDKLL EFDRTSIRRT QVIDDESDYF ASDSNQWLSK
310 320 330 340 350
LERETLQKRE EELRELRHAS RLSKKVTIDF AGRKILEEEN SLAEYHSRLD
360 370 380 390 400
ETIQAIANGT LNQPLTKLDR SSEEPLGVLV NPNMYQSPPQ WVDHTGAASQ
410 420 430 440 450
KKAFRSSGFG LEFNSFQHQL RIQDQEFQEG FDGGWCLSVH QPWASLLVRG
460 470 480 490 500
IKRVEGRSWY TPHRGRLWIA ATAKKPSPQE VSELQATYRL LRGKDVEFPN
510 520 530 540 550
DYPSGCLLGC VDLIDCLSQK QFKEQFPDIS QESDSPFVFI CKNPQEMVVK
560 570 580
FPIKGNPKIW KLDSKIHQGA KKGLMKQNKA V
Length:581
Mass (Da):66,146
Last modified:October 17, 2006 - v4
Checksum:iDADD3994533A808E
GO

Sequence cautioni

The sequence AAC41738.1 differs from that shown. Reason: Frameshift at positions 391, 444 and 476. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571G → R in AAF01278. (PubMed:10454579)Curated
Sequence conflicti157 – 1571G → R in AAC41738. (PubMed:7776974)Curated
Sequence conflicti164 – 1641L → A in AAF01278. (PubMed:10454579)Curated
Sequence conflicti475 – 4751K → N in AAC41738. (PubMed:7776974)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168418 mRNA. Translation: AAF01278.1.
AK314319 mRNA. Translation: BAG36967.1.
CH471082 Genomic DNA. Translation: EAW77685.1.
BC012448 mRNA. Translation: AAH12448.1.
L40371 mRNA. Translation: AAC41738.1. Frameshift.
CCDSiCCDS10194.1.
RefSeqiNP_057297.2. NM_016213.4.
UniGeneiHs.500340.

Genome annotation databases

EnsembliENST00000261884; ENSP00000261884; ENSG00000103671.
GeneIDi9325.
KEGGihsa:9325.
UCSCiuc002anm.3. human.

Polymorphism databases

DMDMi116242828.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF168418 mRNA. Translation: AAF01278.1.
AK314319 mRNA. Translation: BAG36967.1.
CH471082 Genomic DNA. Translation: EAW77685.1.
BC012448 mRNA. Translation: AAH12448.1.
L40371 mRNA. Translation: AAC41738.1. Frameshift.
CCDSiCCDS10194.1.
RefSeqiNP_057297.2. NM_016213.4.
UniGeneiHs.500340.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E5ONMR-A435-581[»]
ProteinModelPortaliQ15650.
SMRiQ15650. Positions 434-581.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114735. 36 interactions.
IntActiQ15650. 4 interactions.
STRINGi9606.ENSP00000261884.

PTM databases

PhosphoSiteiQ15650.

Polymorphism databases

DMDMi116242828.

Proteomic databases

MaxQBiQ15650.
PaxDbiQ15650.
PeptideAtlasiQ15650.
PRIDEiQ15650.

Protocols and materials databases

DNASUi9325.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261884; ENSP00000261884; ENSG00000103671.
GeneIDi9325.
KEGGihsa:9325.
UCSCiuc002anm.3. human.

Organism-specific databases

CTDi9325.
GeneCardsiGC15P065758.
HGNCiHGNC:12310. TRIP4.
HPAiHPA016605.
HPA050666.
MIMi604501. gene.
neXtProtiNX_Q15650.
PharmGKBiPA36988.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248556.
GeneTreeiENSGT00390000005300.
HOGENOMiHOG000006873.
HOVERGENiHBG061618.
InParanoidiQ15650.
OMAiDCLSQEQ.
OrthoDBiEOG7RZ5PP.
PhylomeDBiQ15650.
TreeFamiTF314842.

Miscellaneous databases

ChiTaRSiTRIP4. human.
EvolutionaryTraceiQ15650.
GeneWikiiTRIP4.
GenomeRNAii9325.
NextBioi34931.
PROiQ15650.
SOURCEiSearch...

Gene expression databases

BgeeiQ15650.
CleanExiHS_TRIP4.
ExpressionAtlasiQ15650. baseline and differential.
GenevestigatoriQ15650.

Family and domain databases

InterProiIPR007374. ASCH_domain.
IPR015947. PUA-like_domain.
IPR009349. Znf_C2HC5.
[Graphical view]
PfamiPF04266. ASCH. 1 hit.
PF06221. zf-C2HC5. 1 hit.
[Graphical view]
SMARTiSM01022. ASCH. 1 hit.
[Graphical view]
SUPFAMiSSF88697. SSF88697. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation."
    Kim H.J., Yi J.Y., Sung H.S., Moore D.D., Jhun B.H., Lee Y.C., Lee J.W.
    Mol. Cell. Biol. 19:6323-6332(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
  2. "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].
  3. 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].
    Tissue: Lung.
  5. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-491.
  6. "Activating signal cointegrator 1 is highly expressed in murine testicular Leydig cells and enhances the ligand-dependent transactivation of androgen receptor."
    Lee Y.S., Kim H.-J., Lee H.J., Lee J.W., Chun S.-Y., Ko S.-K., Lee K.
    Biol. Reprod. 67:1580-1587(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DOMAIN.
  7. "Novel transcription coactivator complex containing activating signal cointegrator 1."
    Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J., Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.
    Mol. Cell. Biol. 22:5203-5211(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ASCC1; ASCC2 AND HELIC1.
  8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome."
    Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J.
    J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6, PHOSPHORYLATION BY NEK6.
  12. "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.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Modification of ASC1 by UFM1 is crucial for ERalpha transactivation and breast cancer development."
    Yoo H.M., Kang S.H., Kim J.Y., Lee J.E., Seong M.W., Lee S.W., Ka S.H., Sou Y.S., Komatsu M., Tanaka K., Lee S.T., Noh D.Y., Baek S.H., Jeon Y.J., Chung C.H.
    Mol. Cell 56:261-274(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDRGK1; EP300; ESR1; NCOA1; UFL1 AND UFSP2, SUBCELLULAR LOCATION, REGION, UFMYLATION AT LYS-324; LYS-325; LYS-334 AND LYS-367 BY UFL1, DEUFMYLATION BY UFSP2.
  15. "Solution structure of the TRIP_4C domain of target of activating signal cointegrator 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 435-581.

Entry informationi

Entry nameiTRIP4_HUMAN
AccessioniPrimary (citable) accession number: Q15650
Secondary accession number(s): B2RAS0, Q96ED7, Q9UKH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.