Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein Hook homolog 1

Gene

HOOK1

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

Functioni

Required for spermatid differentiation. Probably involved in the positioning of the microtubules of the manchette and the flagellum in relation to the membrane skeleton (By similarity). Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex).By similarity

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

GO - Biological processi

  • early endosome to late endosome transport Source: UniProtKB
  • endosome organization Source: UniProtKB
  • endosome to lysosome transport Source: UniProtKB
  • lysosome organization Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • protein transport Source: UniProtKB-KW
  • spermatid development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Protein transport, Spermatogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Hook homolog 1
Short name:
h-hook1
Short name:
hHK1
Gene namesi
Name:HOOK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:19884. HOOK1.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity
  • Cytoplasm 1 Publication

  • Note: Localizes to the spermatid manchette during spermiogenesis but is not present in mature spermatozoa (By similarity). Localizes to punctate cytoplasmic foci which do not appear to overlap with early or late endosomes, the endoplasmic reticulum, the Golgi complex, multivesicular bodies (MVBs), lysosomes, or mitochondria. Often found in close association with microtubules.By similarity

GO - Cellular componenti

  • cytosol Source: GOC
  • FHF complex Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi661 – 6622EE → AA: Abrogates interaction with AKTIP, VPS16, VPS18, VPS39 and VPS41, but does not affect interaction with HOOK2 or HOOK3; when associated with 669-A-A-670. 1 Publication
Mutagenesisi669 – 6702WY → AA: Abrogates interaction with AKTIP, VPS16, VPS18, VPS39 and VPS41, but does not affect interaction with HOOK2 or HOOK3; when associated with 661-A-A-662. 1 Publication

Organism-specific databases

PharmGKBiPA134945565.

Polymorphism and mutation databases

BioMutaiHOOK1.
DMDMi41688595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 728728Protein Hook homolog 1PRO_0000219192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei235 – 2351PhosphoserineCombined sources
Modified residuei699 – 6991PhosphothreonineCombined sources
Modified residuei719 – 7191PhosphoserineCombined sources
Modified residuei727 – 7271PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UJC3.
MaxQBiQ9UJC3.
PaxDbiQ9UJC3.
PeptideAtlasiQ9UJC3.
PRIDEiQ9UJC3.

PTM databases

iPTMnetiQ9UJC3.
PhosphoSiteiQ9UJC3.

Expressioni

Gene expression databases

BgeeiQ9UJC3.
CleanExiHS_HOOK1.
ExpressionAtlasiQ9UJC3. baseline and differential.
GenevisibleiQ9UJC3. HS.

Organism-specific databases

HPAiHPA018537.
HPA018820.

Interactioni

Subunit structurei

Self-associates. Component of the FTS/Hook/FHIP complex (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more members of the Hook family of proteins HOOK1, HOOK2, and HOOK3. May interact directly with AKTIP/FTS, HOOK2 and HOOK3. Associates with several subunits of the homotypic vesicular sorting complex (the HOPS complex) including VPS16, VPS18, VPS39 and VPS41; these interactions may be indirect. Interacts with microtubules.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKTIPQ9H8T03EBI-746704,EBI-711399
CDK4P118023EBI-746704,EBI-295644
LMO2P257913EBI-746704,EBI-739696
SYCE1Q8N0S23EBI-746704,EBI-6872807
TBC1D7Q9P0N93EBI-746704,EBI-3258000
TFIP11Q9UBB93EBI-746704,EBI-1105213
USP2O756043EBI-746704,EBI-743272
ZNF785A8K8V03EBI-746704,EBI-3925400

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119496. 32 interactions.
IntActiQ9UJC3. 14 interactions.
MINTiMINT-5006697.
STRINGi9606.ENSP00000360252.

Structurei

3D structure databases

ProteinModelPortaliQ9UJC3.
SMRiQ9UJC3. Positions 12-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 555555Sufficient for interaction with microtubulesAdd
BLAST
Regioni657 – 72872Sufficient for interaction with AKTIP and VPS18Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili169 – 434266Sequence analysisAdd
BLAST
Coiled coili477 – 658182Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the hook family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG1M. Eukaryota.
ENOG410XQ3G. LUCA.
GeneTreeiENSGT00690000101702.
HOGENOMiHOG000199504.
HOVERGENiHBG051920.
InParanoidiQ9UJC3.
KOiK16612.
OMAiCSDTGAC.
OrthoDBiEOG7ZD1V5.
PhylomeDBiQ9UJC3.
TreeFamiTF320231.

Family and domain databases

InterProiIPR008636. Hook-related_fam.
[Graphical view]
PANTHERiPTHR18947. PTHR18947. 1 hit.
PfamiPF05622. HOOK. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9UJC3-1) [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
MEETQPPPQP KLPLCDSLMI WLQTFNTASP CQDVKQLTSG VAMAQVLHQI
60 70 80 90 100
DAAWFNESWL SRIKEDVGDN WRIKASNVKK VLQGIMSYYH EFLGQQISEA
110 120 130 140 150
LIPDLNQITE CSDPVELGRL LQLILGCAIN CEKKQEHIQN IMTLEESVQH
160 170 180 190 200
VVMTAIQELM SKEILSSPPN DAVGELEQQL KRALEELQEA LAEKEELRQR
210 220 230 240 250
CEELDMQVTT LQDEKNSLVS ENEMMNEKLD QLDGSFDDPN TVVAKKYFHA
260 270 280 290 300
QLQLEQLQEE NFRLEAAKDD YRVHCEELEK QLIEFQHRND ELTSLAEETR
310 320 330 340 350
ALKDEIDVLR ATSDKANKLE STVEIYRQKL QDLNDLRKQV KTLQETNMMY
360 370 380 390 400
MHNTVSLEEE LKKANAARTQ LETYKRQVQD LHVKLSSESK RADTLAFEMK
410 420 430 440 450
RLEEKHEALL KEKERLIEQR DTLKETNEEL RCSQVQQDHL NQTDASATKS
460 470 480 490 500
YENLAAEIMP VEYREVFIRL QHENKMLRLQ QEGSENERIE ELQEQLEQKH
510 520 530 540 550
RKMNELETEQ RLSKERIREL QQQIEDLQKS LQEQGSKSEG ESSSKLKQKL
560 570 580 590 600
EAHMEKLTEV HEELQKKQEL IEDLQPDINQ NVQKINELEA ALQKKDEDMK
610 620 630 640 650
AMEERYKMYL EKARNVIKTL DPKLNPASAE IMLLRKQLAE KERRIEILES
660 670 680 690 700
ECKVAKFRDY EEKLIVSAWY NKSLAFQKLG MESRLVSGGG ACSDTGACTP
710 720
ARSFLAQQRH ITNTRRNLSV KVPATTSD
Length:728
Mass (Da):84,648
Last modified:February 2, 2004 - v2
Checksum:iE35CA91F2BB89B3E
GO
Isoform 2 (identifier: Q9UJC3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Note: No experimental confirmation available.
Show »
Length:686
Mass (Da):80,021
Checksum:iF4896D49D819EDA9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti433 – 4331S → L in a breast cancer sample; somatic mutation. 1 Publication
VAR_035709

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4242Missing in isoform 2. 1 PublicationVSP_056226Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044923 mRNA. Translation: AAC09298.1.
AK292314 mRNA. Translation: BAF85003.1.
AK301768 mRNA. Translation: BAG63227.1.
AL035416, AC113175 Genomic DNA. Translation: CAI22779.1.
CH471059 Genomic DNA. Translation: EAX06615.1.
BC011621 mRNA. Translation: AAH11621.1.
CCDSiCCDS612.1. [Q9UJC3-1]
RefSeqiNP_056972.1. NM_015888.4. [Q9UJC3-1]
UniGeneiHs.378836.

Genome annotation databases

EnsembliENST00000371208; ENSP00000360252; ENSG00000134709. [Q9UJC3-1]
GeneIDi51361.
KEGGihsa:51361.
UCSCiuc001czo.3. human. [Q9UJC3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044923 mRNA. Translation: AAC09298.1.
AK292314 mRNA. Translation: BAF85003.1.
AK301768 mRNA. Translation: BAG63227.1.
AL035416, AC113175 Genomic DNA. Translation: CAI22779.1.
CH471059 Genomic DNA. Translation: EAX06615.1.
BC011621 mRNA. Translation: AAH11621.1.
CCDSiCCDS612.1. [Q9UJC3-1]
RefSeqiNP_056972.1. NM_015888.4. [Q9UJC3-1]
UniGeneiHs.378836.

3D structure databases

ProteinModelPortaliQ9UJC3.
SMRiQ9UJC3. Positions 12-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119496. 32 interactions.
IntActiQ9UJC3. 14 interactions.
MINTiMINT-5006697.
STRINGi9606.ENSP00000360252.

PTM databases

iPTMnetiQ9UJC3.
PhosphoSiteiQ9UJC3.

Polymorphism and mutation databases

BioMutaiHOOK1.
DMDMi41688595.

Proteomic databases

EPDiQ9UJC3.
MaxQBiQ9UJC3.
PaxDbiQ9UJC3.
PeptideAtlasiQ9UJC3.
PRIDEiQ9UJC3.

Protocols and materials databases

DNASUi51361.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371208; ENSP00000360252; ENSG00000134709. [Q9UJC3-1]
GeneIDi51361.
KEGGihsa:51361.
UCSCiuc001czo.3. human. [Q9UJC3-1]

Organism-specific databases

CTDi51361.
GeneCardsiHOOK1.
HGNCiHGNC:19884. HOOK1.
HPAiHPA018537.
HPA018820.
MIMi607820. gene.
neXtProtiNX_Q9UJC3.
PharmGKBiPA134945565.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG1M. Eukaryota.
ENOG410XQ3G. LUCA.
GeneTreeiENSGT00690000101702.
HOGENOMiHOG000199504.
HOVERGENiHBG051920.
InParanoidiQ9UJC3.
KOiK16612.
OMAiCSDTGAC.
OrthoDBiEOG7ZD1V5.
PhylomeDBiQ9UJC3.
TreeFamiTF320231.

Miscellaneous databases

ChiTaRSiHOOK1. human.
GeneWikiiHOOK1.
GenomeRNAii51361.
PROiQ9UJC3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJC3.
CleanExiHS_HOOK1.
ExpressionAtlasiQ9UJC3. baseline and differential.
GenevisibleiQ9UJC3. HS.

Family and domain databases

InterProiIPR008636. Hook-related_fam.
[Graphical view]
PANTHERiPTHR18947. PTHR18947. 1 hit.
PfamiPF05622. HOOK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic analysis of hook, a gene required for endocytic trafficking in Drosophila."
    Kraemer H., Phistry M.
    Genetics 151:675-684(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Testis.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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 1).
    Tissue: Placenta.
  6. "The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins."
    Walenta J.H., Didier A.J., Liu X., Kraemer H.
    J. Cell Biol. 152:923-934(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION.
  7. "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-235 AND THR-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "An FTS/Hook/p107(FHIP) complex interacts with and promotes endosomal clustering by the homotypic vacuolar protein sorting complex."
    Xu L., Sowa M.E., Chen J., Li X., Gygi S.P., Harper J.W.
    Mol. Biol. Cell 19:5059-5071(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE FHF COMPLEX, SELF-ASSOCIATION, INTERACTION WITH AKTIP; HOOK2; HOOK3; VPS16; VPS18; VPS39 AND VPS41, MUTAGENESIS OF 661-GLU-GLU-662 AND 669-TRP-TYR-670.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, 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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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-719, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-433.

Entry informationi

Entry nameiHOOK1_HUMAN
AccessioniPrimary (citable) accession number: Q9UJC3
Secondary accession number(s): A8K8E9
, A8MU44, B4DX15, O60561, Q5TG44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: July 6, 2016
This is version 128 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. 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.