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P53990 (IST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
IST1 homolog

Short name=hIST1
Alternative name(s):
Putative MAPK-activating protein PM28
Gene names
Name:IST1
Synonyms:KIAA0174
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proposed to be involved in specific functions of the ESCRT machinery. Is required for efficient abscission during cytokinesis, but not for HIV-1 budding. The involvement in the MVB pathway is not established. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. Ref.7 Ref.8

Subunit structure

Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with the ESCRT-I complex. Interacts with MITD1, in competition with VSP4. Ref.7 Ref.8 Ref.11

Subcellular location

Cytoplasmic vesicle. Note: Localizes to the midbody of dividing cells. Ref.7 Ref.8

Sequence similarities

Belongs to the IST1 family.

Sequence caution

The sequence BAA11491.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
Cell division
   Cellular componentCytoplasmic vesicle
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processabscission

Inferred from direct assay Ref.8Ref.7. Source: UniProtKB

cell division

Inferred from mutant phenotype PubMed 20719964. Source: UniProtKB

cytokinesis

Inferred from mutant phenotype Ref.8Ref.7PubMed 19525971. Source: UniProtKB

establishment of protein localization

Inferred from mutant phenotype Ref.11. Source: UniProt

positive regulation of collateral sprouting

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from direct assay PubMed 20849418. Source: UniProtKB

protein localization

Inferred from mutant phenotype PubMed 20719964. Source: UniProtKB

viral capsid secondary envelopment

Inferred from direct assay Ref.8. Source: UniProtKB

viral release from host cell

Inferred from direct assay Ref.8. Source: UniProtKB

   Cellular_componentFlemming body

Inferred from direct assay Ref.8. Source: UniProtKB

centrosome

Inferred from direct assay Ref.8PubMed 20719964. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay PubMed 10942595. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337PubMed 23376485. Source: UniProt

midbody

Inferred from direct assay Ref.8PubMed 20719964. Source: UniProtKB

   Molecular_functionMIT domain binding

Inferred from physical interaction Ref.8Ref.7. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.7PubMed 19525971PubMed 20719964. Source: UniProtKB

protein complex binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 20719964PubMed 20849418. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN1P542532EBI-945994,EBI-930964
CAPN7Q9Y6W35EBI-945994,EBI-1765641

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P53990-1)

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.
Isoform 2 (identifier: P53990-2)

The sequence of this isoform differs from the canonical sequence as follows:
     228-228: V → VPM
     252-282: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: P53990-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVFKLKTKEEQHSM
     237-237: P → PMP
Isoform 4 (identifier: P53990-4)

The sequence of this isoform differs from the canonical sequence as follows:
     228-228: V → VPM
Isoform 3 (identifier: P53990-3)

The sequence of this isoform differs from the canonical sequence as follows:
     228-228: V → VPM
     283-364: VDDINADKNI...RRFEELKKKT → MTLMLIRISL...LMIFPGGLKS
Note: No experimental confirmation available.
Isoform 6 (identifier: P53990-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     228-228: V → VPM
Note: No experimental confirmation available. Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364IST1 homolog
PRO_0000050727

Regions

Region1 – 168168Interaction with CHMP1A and CHMP1B
Region64 – 279216Interaction with VPS37B
Region190 – 364175Interaction with VTA1
Region348 – 36417Interaction with VPS4A, VTA1, MITD1 STAMBP and USP8
Motif321 – 33212Type-2 MIT-interacting motif
Motif351 – 36111MIT-interacting motif

Amino acid modifications

Modified residue431Phosphotyrosine Ref.6

Natural variations

Alternative sequence1 – 148148Missing in isoform 6.
VSP_055118
Alternative sequence11M → MVFKLKTKEEQHSM in isoform 5.
VSP_047075
Alternative sequence2281V → VPM in isoform 2, isoform 3, isoform 4 and isoform 6.
VSP_017118
Alternative sequence2371P → PMP in isoform 5.
VSP_047076
Alternative sequence252 – 28231Missing in isoform 2.
VSP_017119
Alternative sequence283 – 36482VDDIN…LKKKT → MTLMLIRISLLHRLLVLDPS QKPLQSFLPDLQITMTTLSY QSCHLCQTHYQLHLLVPAPQ HLKTLTLMIFPGGLKS in isoform 3.
VSP_017120

Experimental info

Mutagenesis3231L → D: Diminishes interaction with VPS4A. Ref.7 Ref.8
Mutagenesis3231L → D: Greatly diminishes interaction with VPS4A; when associated with A-353. Ref.7 Ref.8
Mutagenesis3261L → D: Diminishes interaction with VPS4A. Ref.7 Ref.8
Mutagenesis3261L → D: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with A-353. Ref.7 Ref.8
Mutagenesis3261L → D: Greatly diminishes interaction with VPS4A; when associated with A-360.
Mutagenesis3531L → A: Diminishes interaction with VPS4A. Ref.7 Ref.8
Mutagenesis3531L → A: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with D-326. Ref.7 Ref.8
Mutagenesis3531L → A: Greatly diminishes interaction with VPS4A; when associated with D-323.
Mutagenesis360 – 3612LK → AA: Abolishes interaction with VTA1, MITD1 and USP8; diminishes interaction with VPS4A. Ref.7 Ref.8
Mutagenesis3601L → A: Diminishes interaction with VPS4A. Ref.7 Ref.8
Mutagenesis3601L → A: Greatly diminishes interaction with VPS4A; when associated with D-326. Ref.7 Ref.8

Secondary structure

...................... 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 0DD3C186A52A4380

FASTA36439,751
        10         20         30         40         50         60 
MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII 

        70         80         90        100        110        120 
REDYLVEAME ILELYCDLLL ARFGLIQSMK ELDSGLAESV STLIWAAPRL QSEVAELKIV 

       130        140        150        160        170        180 
ADQLCAKYSK EYGKLCRTNQ IGTVNDRLMH KLSVEAPPKI LVERYLIEIA KNYNVPYEPD 

       190        200        210        220        230        240 
SVVMAEAPPG VETDLIDVGF TDDVKKGGPG RGGSGGFTAP VGGPDGTVPM PMPMPMPSAN 

       250        260        270        280        290        300 
TPFSYPLPKG PSDFNGLPMG TYQAFPNIHP PQIPATPPSY ESVDDINADK NISSAQIVGP 

       310        320        330        340        350        360 
GPKPEASAKL PSRPADNYDN FVLPELPSVP DTLPTASAGA STSASEDIDF DDLSRRFEEL 


KKKT 

« Hide

Isoform 2 [UniParc].

Checksum: 7D0714269380E835
Show »

FASTA33536,622
Isoform 5 [UniParc].

Checksum: 37E0FEF4BB93C054
Show »

FASTA37941,566
Isoform 4 [UniParc].

Checksum: E25DE7D7A5693AF8
Show »

FASTA36639,979
Isoform 3 [UniParc].

Checksum: 5D0DDB4113DAA2BC
Show »

FASTA36039,928
Isoform 6 [UniParc].

Checksum: B0405956455B9777
Show »

FASTA21823,089

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[2]"Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways."
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.
Oncogene 22:3307-3318(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung fibroblast.
[3]"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. expand/collapse author list , 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] (ISOFORMS 4 AND 5).
Tissue: Testis and Uterus.
[4]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
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] (ISOFORMS 2; 3 AND 4).
Tissue: Eye and Lung.
[6]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Essential role of hIST1 in cytokinesis."
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J.
Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CHMP1A; CHMP1B; VPS4A; VTA1; MITD1; STAMBP; SPAST AND USP8, MUTAGENESIS OF 360-LEU-LYS-361.
[8]"Biochemical analyses of human IST1 and its function in cytokinesis."
Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH VPS37B; VTA1; CHMP1A; CHMP1B; VPS4A AND VPS4B, INTERACTION WITH THE ESCRT-1 COMPLEX, MUTAGENESIS OF LEU-323; LEU-326; LEU-353 AND LEU-360.
[9]"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.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"MITD1 is recruited to midbodies by ESCRT-III and participates in cytokinesis."
Lee S., Chang J., Renvoise B., Tipirneni A., Yang S., Blackstone C.
Mol. Biol. Cell 23:4347-4361(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MITD1.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB097052 mRNA. Translation: BAC77405.1.
D79996 mRNA. Translation: BAA11491.2. Different initiation.
AK057258 mRNA. Translation: BAG51894.1.
AK293022 mRNA. Translation: BAF85711.1.
AK293040 mRNA. Translation: BAF85729.1.
AC009127 Genomic DNA. No translation available.
AC010653 Genomic DNA. No translation available.
BC000116 mRNA. Translation: AAH00116.1.
BC000430 mRNA. Translation: AAH00430.1.
BC004359 mRNA. Translation: AAH04359.1.
BC103745 mRNA. Translation: AAI03746.1.
CCDSCCDS10905.1. [P53990-3]
CCDS59271.1. [P53990-5]
CCDS59272.1. [P53990-4]
CCDS59273.1. [P53990-2]
RefSeqNP_001257904.1. NM_001270975.1. [P53990-4]
NP_001257905.1. NM_001270976.1. [P53990-5]
NP_001257906.1. NM_001270977.1. [P53990-2]
NP_055576.2. NM_014761.3. [P53990-3]
UniGeneHs.232194.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FRRX-ray1.80A1-189[»]
3FRSX-ray2.61A5-189[»]
ProteinModelPortalP53990.
SMRP53990. Positions 2-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115141. 17 interactions.
DIPDIP-42546N.
IntActP53990. 6 interactions.
MINTMINT-1461091.
STRING9606.ENSP00000330408.

PTM databases

PhosphoSiteP53990.

Polymorphism databases

DMDM1723119.

Proteomic databases

MaxQBP53990.
PaxDbP53990.
PRIDEP53990.

Protocols and materials databases

DNASU9798.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329908; ENSP00000330408; ENSG00000182149. [P53990-3]
ENST00000378798; ENSP00000368075; ENSG00000182149. [P53990-2]
ENST00000378799; ENSP00000368076; ENSG00000182149. [P53990-4]
ENST00000535424; ENSP00000438399; ENSG00000182149. [P53990-5]
ENST00000538850; ENSP00000463711; ENSG00000182149.
ENST00000541571; ENSP00000455860; ENSG00000182149. [P53990-4]
ENST00000544564; ENSP00000457844; ENSG00000182149. [P53990-4]
ENST00000606369; ENSP00000475853; ENSG00000182149.
GeneID9798.
KEGGhsa:9798.
UCSCuc002fbk.2. human. [P53990-3]
uc002fbl.2. human. [P53990-2]
uc002fbm.2. human. [P53990-4]
uc010cgh.2. human.

Organism-specific databases

CTD9798.
GeneCardsGC16P071930.
HGNCHGNC:28977. IST1.
HPAHPA041802.
HPA054532.
neXtProtNX_P53990.
PharmGKBPA142671633.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273475.
HOGENOMHOG000205346.
InParanoidP53990.
OMAPTYESID.
PhylomeDBP53990.
TreeFamTF314258.

Gene expression databases

ArrayExpressP53990.
BgeeP53990.
CleanExHS_KIAA0174.
GenevestigatorP53990.

Family and domain databases

InterProIPR005061. DUF292_euk.
[Graphical view]
PfamPF03398. Ist1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIST1. human.
EvolutionaryTraceP53990.
GenomeRNAi9798.
NextBio35464749.
PMAP-CutDBP53990.
PROP53990.

Entry information

Entry nameIST1_HUMAN
AccessionPrimary (citable) accession number: P53990
Secondary accession number(s): A8KAH5 expand/collapse secondary AC list , J3QLU7, Q3SYM4, Q9BQ81, Q9BWN2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM