P53990 (IST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
IST1 homolog
Short name=hIST1

Alternative name(s):
Putative MAPK-activating protein PM28

Gene names

Name:	IST1
Synonyms:	KIAA0174

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5 Ref.6
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.5 Ref.6 Ref.9
Subcellular location	Cytoplasmic vesicle. Note: Localizes to the midbody of dividing cells. Ref.5 Ref.6
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 process	Cell cycle Cell division
Cellular component	Cytoplasmic vesicle
Coding sequence diversity	Alternative splicing
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	abscission Inferred from direct assay Ref.6Ref.5. Source: UniProtKB cell cycle cytokinesis Inferred from mutant phenotype Ref.6Ref.5PubMed 19525971. Source: UniProtKB positive regulation of proteolysis Inferred from direct assay PubMed 20849418. Source: UniProtKB protein localization Inferred from mutant phenotype PubMed 20719964. Source: UniProtKB viral release from host cell Inferred from direct assay Ref.6. Source: UniProtKB virus budding from nuclear membrane by viral capsid re-envelopment Inferred from direct assay Ref.6. Source: UniProtKB
Cellular_component	Flemming body Inferred from direct assay Ref.6. Source: UniProtKB centrosome Inferred from direct assay Ref.6PubMed 20719964. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.5. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay PubMed 10942595. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21557262. Source: UniProtKB
Molecular_function	protein complex binding Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	2	EBI-945994,EBI-930964

Alternative products

This entry describes 4 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 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

IST1 homolog

PRO_0000050727

Regions

Region

1 – 168

168

Interaction with CHMP1A and CHMP1B

Region

64 – 279

216

Interaction with VPS37B

Region

190 – 364

175

Interaction with VTA1

Region

348 – 364

17

Interaction with VPS4A, VTA1, MITD1 STAMBP and USP8

Motif

321 – 332

12

Type-2 MIT-interacting motif

Motif

351 – 361

11

MIT-interacting motif

Natural variations

Alternative sequence

228

1

V → VPM in isoform 2, isoform 3 and isoform 4.

VSP_017118

Alternative sequence

252 – 282

31

Missing in isoform 2.

VSP_017119

Alternative sequence

283 – 364

82

VDDIN…LKKKT → MTLMLIRISLLHRLLVLDPS QKPLQSFLPDLQITMTTLSY QSCHLCQTHYQLHLLVPAPQ HLKTLTLMIFPGGLKS in isoform 3.

VSP_017120

Experimental info

Mutagenesis

323

1

L → D: Diminishes interaction with VPS4A. Ref.5 Ref.6

Mutagenesis

323

1

L → D: Greatly diminishes interaction with VPS4A; when associated with A-353. Ref.5 Ref.6

Mutagenesis

326

1

L → D: Diminishes interaction with VPS4A. Ref.5 Ref.6

Mutagenesis

326

1

L → D: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with A-353. Ref.5 Ref.6

Mutagenesis

326

1

L → D: Greatly diminishes interaction with VPS4A; when associated with A-360.

Mutagenesis

353

1

L → A: Diminishes interaction with VPS4A. Ref.5 Ref.6

Mutagenesis

353

1

L → A: Greatly diminishes interaction with VPS4A and abolishes interaction with VTA1; when associated with D-326. Ref.5 Ref.6

Mutagenesis

353

1

L → A: Greatly diminishes interaction with VPS4A; when associated with D-323.

Mutagenesis

360 – 361

2

LK → AA: Abolishes interaction with VTA1, MITD1 and USP8; diminishes interaction with VPS4A. Ref.5 Ref.6

Mutagenesis

360

1

L → A: Diminishes interaction with VPS4A. Ref.5 Ref.6

Mutagenesis

360

1

L → A: Greatly diminishes interaction with VPS4A; when associated with D-326. Ref.5 Ref.6

Secondary structure

1

.

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.

.

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.

.

364

Helix Strand Turn

Details...

Helix

8 – 45

38

Helix

49 – 81

33

Helix

83 – 87

5

Helix

94 – 96

3

Helix

97 – 110

14

Turn

111 – 113

3

Helix

115 – 128

14

Helix

130 – 137

8

Turn

138 – 141

4

Helix

146 – 151

6

Helix

159 – 173

15

Helix

181 – 185

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0DD3C186A52A4380	FASTA	364	39,751
	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
	Isoform 2 [UniParc]. Checksum: 7D0714269380E835	FASTA	335	36,622
	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 PMPMPMPMPS 250 260 270 280 290 300 ANTPFSYPLP KGPVDDINAD KNISSAQIVG PGPKPEASAK LPSRPADNYD NFVLPELPSV 310 320 330 PDTLPTASAG ASTSASEDID FDDLSRRFEE LKKKT
	Isoform 4 [UniParc]. Checksum: E25DE7D7A5693AF8	FASTA	366	39,979
	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 PMPMPMPMPS 250 260 270 280 290 300 ANTPFSYPLP KGPSDFNGLP MGTYQAFPNI HPPQIPATPP SYESVDDINA DKNISSAQIV 310 320 330 340 350 360 GPGPKPEASA KLPSRPADNY DNFVLPELPS VPDTLPTASA GASTSASEDI DFDDLSRRFE ELKKKT
	Isoform 3 [UniParc]. Checksum: 5D0DDB4113DAA2BC	FASTA	360	39,928
	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 PMPMPMPMPS 250 260 270 280 290 300 ANTPFSYPLP KGPSDFNGLP MGTYQAFPNI HPPQIPATPP SYESMTLMLI RISLLHRLLV 310 320 330 340 350 360 LDPSQKPLQS FLPDLQITMT TLSYQSCHLC QTHYQLHLLV PAPQHLKTLT LMIFPGGLKS

References

	« Hide 'large scale' referencesShow '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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[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] (ISOFORMS 2; 3 AND 4). Tissue: Eye and Lung.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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].
[9]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB097052 mRNA. Translation: BAC77405.1.
D79996 mRNA. Translation: BAA11491.2. Different initiation.
AK293022 mRNA. Translation: BAF85711.1.
BC000116 mRNA. Translation: AAH00116.1.
BC000430 mRNA. Translation: AAH00430.1.
BC004359 mRNA. Translation: AAH04359.1.
BC103745 mRNA. Translation: AAI03746.1.

IPI

IPI00024660.
IPI00420088.
IPI00643007.
IPI00939709.

RefSeq

NP_001257904.1. NM_001270975.1.
NP_001257906.1. NM_001270977.1.
NP_055576.2. NM_014761.3.

UniGene

Hs.232194.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FRR	X-ray	1.80	A	1-189	[»]
3FRS	X-ray	2.61	A	5-189	[»]

ProteinModelPortal

P53990.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42546N.

IntAct

P53990. 4 interactions.

MINT

MINT-1461091.

STRING

9606.ENSP00000330408.

PTM databases

PhosphoSite

P53990.

Polymorphism databases

DMDM

1723119.

Proteomic databases

PaxDb

P53990.

PRIDE

P53990.

Protocols and materials databases

DNASU

9798.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000329908; ENSP00000330408; ENSG00000182149.
ENST00000378798; ENSP00000368075; ENSG00000182149.
ENST00000378799; ENSP00000368076; ENSG00000182149.
ENST00000541571; ENSP00000455860; ENSG00000182149.
ENST00000544564; ENSP00000457844; ENSG00000182149.

GeneID

9798.

KEGG

hsa:9798.

UCSC

uc002fbk.1. human.
uc002fbl.1. human.
uc002fbm.1. human.

Organism-specific databases

CTD

9798.

GeneCards

GC16P071930.

HGNC

HGNC:28977. IST1.

HPA

HPA041802.

neXtProt

NX_P53990.

PharmGKB

PA142671633.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG273475.

HOGENOM

HOG000205346.

InParanoid

P53990.

OrthoDB

EOG4DNF4W.

Gene expression databases

ArrayExpress

P53990.

Bgee

P53990.

CleanEx

HS_KIAA0174.

Genevestigator

P53990.

GermOnline

ENSG00000182149. Homo sapiens.

Family and domain databases

InterPro

IPR005061. DUF292_euk.
[Graphical view]

Pfam

PF03398. Ist1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IST1. human.

EvolutionaryTrace

P53990.

GenomeRNAi

9798.

NextBio

36900.

PMAP-CutDB

P53990.

Entry information

Entry name

IST1_HUMAN

Accession

Primary (citable) accession number: P53990
Secondary accession number(s): Q3SYM4, Q9BQ81, Q9BWN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.